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Conserved domains on  [gi|1034635487|ref|XP_016862662|]
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voltage-gated potassium channel subunit beta-1 isoform X4 [Homo sapiens]

Protein Classification

aldo-keto reductase family protein( domain architecture ID 305)

aldo-keto reductase family protein may be an NAD(P)(H) oxidoreductase that reduces aldehydes and ketones to primary and secondary alcohols

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AKR_SF super family cl00470
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ...
1-287 0e+00

Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.


The actual alignment was detected with superfamily member cd19159:

Pssm-ID: 444925 [Multi-domain]  Cd Length: 323  Bit Score: 625.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19159    37 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19159   117 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19159   197 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 276
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 287
Cdd:cd19159   277 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 323
 
Name Accession Description Interval E-value
AKR_KCAB1B_AKR6A3-like cd19159
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ...
1-287 0e+00

voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.


Pssm-ID: 381385 [Multi-domain]  Cd Length: 323  Bit Score: 625.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19159    37 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19159   117 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19159   197 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 276
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 287
Cdd:cd19159   277 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 323
Kv_beta TIGR01293
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ...
1-283 0e+00

voltage-dependent potassium channel beta subunit, animal; This model describes the conserved core region of the beta subunit of voltage-gated potassium (Kv) channels in animals. Amino-terminal regions differ substantially, in part by alternative splicing, and are not included in the model. Four beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions, and the structure of the complex is solved. The beta subunit belongs to a family of NAD(P)H-dependent aldo-keto reductases, binds NADPH, and couples voltage-gated channel activity to the redox potential of the cell. Plant beta subunits and their closely related bacterial homologs (in Deinococcus radiudurans, Xylella fastidiosa, etc.) appear more closely related to each other than to animal forms. However, the bacterial species lack convincing counterparts the Kv alpha subunit and the Kv beta homolog may serve as an enzyme. Cutoffs are set for this model such that yeast and plant forms and bacterial close homologs score between trusted and noise cutoffs.


Pssm-ID: 213602 [Multi-domain]  Cd Length: 317  Bit Score: 527.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:TIGR01293  35 LTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:TIGR01293 115 DIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPEL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:TIGR01293 195 YHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKILSEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCL 274
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNIL 283
Cdd:TIGR01293 275 RNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
PdxI COG0667
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ...
4-287 9.25e-87

Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440431 [Multi-domain]  Cd Length: 316  Bit Score: 262.04  E-value: 9.25e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:COG0667    42 ALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDVVIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfNMIPPVCEQAEYHLFQREkVEVQLPELYH 162
Cdd:COG0667   120 YQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAAR 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGIISGKYGNG--VPESSRASLkcyqWLKERIVSEEGRKqqnKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:COG0667   197 ELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAAT----NFVQGYLTERNLA---LVDALRAIAAEHGVTPAQLALAWLL 269
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKP 287
Cdd:COG0667   270 AQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAALDAALAAVP 314
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
4-283 4.36e-59

Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.


Pssm-ID: 425554 [Multi-domain]  Cd Length: 290  Bit Score: 190.22  E-value: 4.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:pfam00248  27 ALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWPSGGSKENIRKSLEESLKRLGTDYIDLY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFqREKVEVQLPELYHK 163
Cdd:pfam00248 106 YLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----IPIVAVQVEYNLL-RRRQEEELLEYCKK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 164 IGVGAMTWSPLACGIISGKY--GNGVPESSRASLKCYQWlkerivseegRKQQNKLKDLSPIAERLGCTLPQLAVAWCLR 241
Cdd:pfam00248 181 NGIPLIAYSPLGGGLLTGKYtrDPDKGPGERRRLLKKGT----------PLNLEALEALEEIAKEHGVSPAQVALRWALS 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034635487 242 NEGVSSVLLGSSTPEQLIENLGAIQvlPKMTSHVVNEIDNIL 283
Cdd:pfam00248 251 KPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
PRK09912 PRK09912
L-glyceraldehyde 3-phosphate reductase; Provisional
4-268 6.12e-53

L-glyceraldehyde 3-phosphate reductase; Provisional


Pssm-ID: 182140 [Multi-domain]  Cd Length: 346  Bit Score: 176.33  E-value: 6.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSLVITTKL---YWGGKAETerGLSRKHIIEGLKGSLQRLQL 77
Cdd:PRK09912   52 AFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDELIISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQL 157
Cdd:PRK09912  130 EYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGL 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 158 PELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASL--KCYQWLKERIVSEegrKQQNKLKDLSPIAERLGCTLPQLA 235
Cdd:PRK09912  209 LDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHRegNKVRGLTPKMLTE---ANLNSLRLLNEMAQQRGQSMAQMA 285
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034635487 236 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 268
Cdd:PRK09912  286 LSWLLKDERVTSVLIGASRAEQLEENVQALNNL 318
 
Name Accession Description Interval E-value
AKR_KCAB1B_AKR6A3-like cd19159
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ...
1-287 0e+00

voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.


Pssm-ID: 381385 [Multi-domain]  Cd Length: 323  Bit Score: 625.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19159    37 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19159   117 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19159   197 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 276
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 287
Cdd:cd19159   277 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 323
Aldo_ket_red_shaker cd19141
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ...
1-275 0e+00

Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.


Pssm-ID: 381367 [Multi-domain]  Cd Length: 310  Bit Score: 586.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19141    36 VTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYV 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19141   116 DIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPEL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19141   196 FHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKILSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCL 275
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHV 275
Cdd:cd19141   276 KNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
AKR_KCAB3B_AKR6A9-like cd19160
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ...
1-287 0e+00

voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.


Pssm-ID: 381386 [Multi-domain]  Cd Length: 325  Bit Score: 556.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19160    39 LTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYV 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19160   119 DIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPEL 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19160   199 YHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLKEKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCL 278
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 287
Cdd:cd19160   279 RSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDALLGNKP 325
Kv_beta TIGR01293
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ...
1-283 0e+00

voltage-dependent potassium channel beta subunit, animal; This model describes the conserved core region of the beta subunit of voltage-gated potassium (Kv) channels in animals. Amino-terminal regions differ substantially, in part by alternative splicing, and are not included in the model. Four beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions, and the structure of the complex is solved. The beta subunit belongs to a family of NAD(P)H-dependent aldo-keto reductases, binds NADPH, and couples voltage-gated channel activity to the redox potential of the cell. Plant beta subunits and their closely related bacterial homologs (in Deinococcus radiudurans, Xylella fastidiosa, etc.) appear more closely related to each other than to animal forms. However, the bacterial species lack convincing counterparts the Kv alpha subunit and the Kv beta homolog may serve as an enzyme. Cutoffs are set for this model such that yeast and plant forms and bacterial close homologs score between trusted and noise cutoffs.


Pssm-ID: 213602 [Multi-domain]  Cd Length: 317  Bit Score: 527.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:TIGR01293  35 LTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:TIGR01293 115 DIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPEL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:TIGR01293 195 YHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKILSEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCL 274
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNIL 283
Cdd:TIGR01293 275 RNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
AKR_KCAB2B_AKR6A1-like cd19158
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ...
1-288 0e+00

voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.


Pssm-ID: 381384 [Multi-domain]  Cd Length: 324  Bit Score: 521.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19158    37 MTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19158   117 DVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPEL 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19158   197 FHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCL 276
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKPY 288
Cdd:cd19158   277 RNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILGNKPY 324
AKR_AKR6C1_2 cd19143
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ...
1-282 3.50e-164

AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.


Pssm-ID: 381369 [Multi-domain]  Cd Length: 319  Bit Score: 458.60  E-value: 3.50e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAE--TERGLSRKHIIEGLKGSLQRLQLE 78
Cdd:cd19143    37 MKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKIFWGGGGPppNDRGLSRKHIVEGTKASLKRLQLD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  79 YVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLP 158
Cdd:cd19143   117 YVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 159 ELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERiVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAW 238
Cdd:cd19143   197 PLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLKDR-KEELGQEKIEKVRKLKPIAEELGCSLAQLAIAW 275
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034635487 239 CLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNI 282
Cdd:cd19143   276 CLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
AKR_AKR6B1 cd19142
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ...
1-287 1.57e-142

AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.


Pssm-ID: 381368 [Multi-domain]  Cd Length: 325  Bit Score: 404.15  E-value: 1.57e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAEtERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19142    37 VTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVSTKIYWSYGSE-ERGLSRKHIIESVRASLRRLQLDYI 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19142   116 DIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREKMELYMPEL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSR---ASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVA 237
Cdd:cd19142   196 YNKVGVGLITWSPLSLGLDPGISEETRRLVTKlsfKSSKYKVGSDGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIA 275
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034635487 238 WCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 287
Cdd:cd19142   276 WSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEELERILDNKP 325
Aldo_ket_red_shaker-like cd19074
Shaker potassium channel beta subunit family and similar proteins; This family includes ...
4-265 2.21e-139

Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.


Pssm-ID: 381300 [Multi-domain]  Cd Length: 297  Bit Score: 395.04  E-value: 2.21e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKLYWGGKAE-TERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd19074    31 AYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGPGpNDRGLSRKHIFESIHASLKRLQLDYVDI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEvQLPELYH 162
Cdd:cd19074   109 YYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEE-EVIPLCE 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGIISGKYGNGVPESSRASLKcYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRN 242
Cdd:cd19074   188 KNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT-DEDNRDKKRRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRN 266
                         250       260
                  ....*....|....*....|...
gi 1034635487 243 EGVSSVLLGSSTPEQLIENLGAI 265
Cdd:cd19074   267 PAVSSAIIGASRPEQLEENVKAS 289
PdxI COG0667
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ...
4-287 9.25e-87

Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 440431 [Multi-domain]  Cd Length: 316  Bit Score: 262.04  E-value: 9.25e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:COG0667    42 ALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDVVIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfNMIPPVCEQAEYHLFQREkVEVQLPELYH 162
Cdd:COG0667   120 YQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAAR 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGIISGKYGNG--VPESSRASLkcyqWLKERIVSEEGRKqqnKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:COG0667   197 ELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAAT----NFVQGYLTERNLA---LVDALRAIAAEHGVTPAQLALAWLL 269
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKP 287
Cdd:COG0667   270 AQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAALDAALAAVP 314
AKR_AKR12A1_B1_C1 cd19087
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ...
4-282 5.09e-77

AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.


Pssm-ID: 381313 [Multi-domain]  Cd Length: 310  Bit Score: 237.09  E-value: 5.09e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYWG-GKAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd19087    39 ALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLATKVFGPmGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYH 162
Cdd:cd19087   116 YQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAAR 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGIISGKYGNG-VPESSR-ASLKCYQwlkERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19087   195 AYGLGVIPYSPLAGGLLTGKYGKGkRPESGRlVERARYQ---ARYGLEEYRDI---AERFEALAAEAGLTPASLALAWVL 268
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNI 282
Cdd:cd19087   269 SHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDEL 308
AKR_PsAKR cd19091
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ...
3-267 4.44e-70

Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.


Pssm-ID: 381317 [Multi-domain]  Cd Length: 319  Bit Score: 219.41  E-value: 4.44e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   3 IAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKL-YWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19091    47 IALDAGINFFDTADVYSEGESEEILGKALKG---RRDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYID 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  82 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELY 161
Cdd:cd19091   124 LYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKCYQWLkerIVSEEgrKQQNKLKDLSPIAERLGCTLPQLAVAWC 239
Cdd:cd19091   203 LDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSRLRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQVALAWL 277
                         250       260
                  ....*....|....*....|....*...
gi 1034635487 240 LRNEGVSSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19091   278 LSRPTVSSVIIGARNEEQLEDNLGAAGL 305
AKR_AKR11B1-like cd19084
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ...
4-280 8.01e-69

AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.


Pssm-ID: 381310 [Multi-domain]  Cd Length: 296  Bit Score: 215.47  E-value: 8.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTK--LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19084    34 AIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLRWDGGKGVTKDLSPESIRKEVEQSLRRLQTDYID 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  82 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAysvarqFNMIPPVCEQAEYHLFQREKVEVQLPeLY 161
Cdd:cd19084   111 LYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA------RKYGPIVSLQPPYSMLEREIEEELLP-YC 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGIISGKYGNG---VPESSRASLKCYQwlkerivSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAW 238
Cdd:cd19084   184 RENGIGVLPYGPLAQGLLTGKYKKEptfPPDDRRSRFPFFR-------GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAW 256
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034635487 239 CLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 280
Cdd:cd19084   257 TLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
AKR_AKR14A1_2 cd19089
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ...
4-269 7.09e-67

AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.


Pssm-ID: 381315 [Multi-domain]  Cd Length: 308  Bit Score: 210.96  E-value: 7.09e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVY--AAGKAEVILGSIIKK-KGWRRSSLVITTKL-Y--WGGKaeTERGLSRKHIIEGLKGSLQRLQL 77
Cdd:cd19089    38 AFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVISTKAgYgmWPGP--YGDGGSRKYLLASLDQSLKRMGL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQReKVEVQL 157
Cdd:cd19089   116 DYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELG-VPLIIHQPRYSLLDR-WAEDGL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 158 PELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRAsLKCYQWLKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVA 237
Cdd:cd19089   194 LEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR-AAESKFLTEEALTPE---KLEQLRKLNKIAAKRGQSLAQLALS 269
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034635487 238 WCLRNEGVSSVLLGSSTPEQLIENLGAIQVLP 269
Cdd:cd19089   270 WVLRDPRVTSVLIGASSPSQLEDNVAALKNLD 301
AKR_SF cd06660
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ...
4-263 7.71e-66

Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.


Pssm-ID: 381296 [Multi-domain]  Cd Length: 232  Bit Score: 205.83  E-value: 7.71e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL-YWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd06660    26 ALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSRSRLSPEHIRRDLEESLRRLGTDYIDL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYH 162
Cdd:cd06660   105 YYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPGFAAVQPQYSLLDRSPMEEELLDWAE 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGiisgkygngvpessraslkcyqwlkerivseegrkqqnklkdlspiaerlgctLPQLAVAWCLRN 242
Cdd:cd06660   185 ENGLPLLAYSPLARG-----------------------------------------------------PAQLALAWLLSQ 211
                         250       260
                  ....*....|....*....|.
gi 1034635487 243 EGVSSVLLGSSTPEQLIENLG 263
Cdd:cd06660   212 PFVTVPIVGARSPEQLEENLA 232
AKR_AKR9C1 cd19081
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ...
6-280 9.05e-65

AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).


Pssm-ID: 381307 [Multi-domain]  Cd Length: 308  Bit Score: 205.53  E-value: 9.05e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   6 ESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwRRSSLVITTKLYWGgKAETERGLSRKHIIEGLKGSLQRLQLE 78
Cdd:cd19081    37 DAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVVIATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTD 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  79 YVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLP 158
Cdd:cd19081   115 YIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 159 ELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKcyqwlKERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLAV 236
Cdd:cd19081   195 PLCREEGIGVIPYSPLAGGFLTGKYrsEADLPGSTRRGEA-----AKRYLNERGLRI---LDALDEVAAEHGATPAQVAL 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034635487 237 AWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 280
Cdd:cd19081   267 AWLLARPGVTAPIAGARTVEQLEDLLAAAGL--RLTDEEVARLD 308
AKR_EcYajO-like cd19079
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ...
4-267 3.39e-63

Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.


Pssm-ID: 381305 [Multi-domain]  Cd Length: 312  Bit Score: 201.66  E-value: 3.39e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd19079    44 ALDLGINFFDTANVYSGGASEEILGRALKEFA-PRDEVVIATKVYFpMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKvEVQLPELYH 162
Cdd:cd19079   123 YQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCE 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGIISGKYGNGVP-ESSRASLKCYQWLKErivSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLR 241
Cdd:cd19079   202 EEGIGVIPWSPLARGRLARPWGDTTErRRSTTDTAKLKYDYF---TEADKEIVDRVEE---VAKERGVSMAQVALAWLLS 275
                         250       260
                  ....*....|....*....|....*.
gi 1034635487 242 NEGVSSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19079   276 KPGVTAPIVGATKLEHLEDAVAALDI 301
AKR_AKR14A2 cd19151
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ...
4-266 7.96e-60

Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).


Pssm-ID: 381377 [Multi-domain]  Cd Length: 309  Bit Score: 193.00  E-value: 7.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYA--AGKAEVILGSIIKK--KGWRrSSLVITTKL--------Y--WGgkaeterglSRKHIIEGLK 69
Cdd:cd19151    39 AFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DELIISTKAgytmwpgpYgdWG---------SKKYLIASLD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  70 GSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQ 149
Cdd:cd19151   109 QSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSMFN 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 150 REkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASlKCYQWLKERIVSEEgrkQQNKLKDLSPIAERLGC 229
Cdd:cd19151   188 RW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAA-KGSSFLKPEQITEE---KLAKVRRLNEIAQARGQ 262
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034635487 230 TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 266
Cdd:cd19151   263 KLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
AKR_Tas-like cd19094
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ...
1-282 4.20e-59

Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.


Pssm-ID: 381320 [Multi-domain]  Cd Length: 328  Bit Score: 191.62  E-value: 4.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK-----LYWGGKAETERGLSRKHIIEGL 68
Cdd:cd19094    24 LDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKvagpgEGITWPRGGGTRLDRENIREAV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  69 KGSLQRLQLEYVDVVFANRPDSNTP------------------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVA 130
Cdd:cd19094   103 EGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLELA 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 131 RQFNMIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLkcYQWLKERIVSE 208
Cdd:cd19094   183 EQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYldGAARPEGGRLNL--FPGYMARYRSP 259
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034635487 209 EGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV-LPKmtsHVVNEIDNI 282
Cdd:cd19094   260 QALEAVAEYVK---LARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDVpLSD---ELLAEIDAV 328
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
4-283 4.36e-59

Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.


Pssm-ID: 425554 [Multi-domain]  Cd Length: 290  Bit Score: 190.22  E-value: 4.36e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:pfam00248  27 ALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWPSGGSKENIRKSLEESLKRLGTDYIDLY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFqREKVEVQLPELYHK 163
Cdd:pfam00248 106 YLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----IPIVAVQVEYNLL-RRRQEEELLEYCKK 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 164 IGVGAMTWSPLACGIISGKY--GNGVPESSRASLKCYQWlkerivseegRKQQNKLKDLSPIAERLGCTLPQLAVAWCLR 241
Cdd:pfam00248 181 NGIPLIAYSPLGGGLLTGKYtrDPDKGPGERRRLLKKGT----------PLNLEALEALEEIAKEHGVSPAQVALRWALS 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034635487 242 NEGVSSVLLGSSTPEQLIENLGAIQvlPKMTSHVVNEIDNIL 283
Cdd:pfam00248 251 KPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
AKR_AKR14A1 cd19150
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ...
4-268 3.91e-57

Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.


Pssm-ID: 381376 [Multi-domain]  Cd Length: 309  Bit Score: 186.12  E-value: 3.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSLVITTKL---YWGGKAeTERGlSRKHIIEGLKGSLQRLQL 77
Cdd:cd19150    39 AFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELIISTKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQL 157
Cdd:cd19150   117 DYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 158 PELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASlkcyqwlKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLA 235
Cdd:cd19150   196 LDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRAS-------KERSLSPKMLTEANlnSIRALNEIAQKRGQSLAQMA 268
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034635487 236 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 268
Cdd:cd19150   269 LAWVLRDGRVTSALIGASRPEQLEENVGALDNL 301
PRK09912 PRK09912
L-glyceraldehyde 3-phosphate reductase; Provisional
4-268 6.12e-53

L-glyceraldehyde 3-phosphate reductase; Provisional


Pssm-ID: 182140 [Multi-domain]  Cd Length: 346  Bit Score: 176.33  E-value: 6.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSLVITTKL---YWGGKAETerGLSRKHIIEGLKGSLQRLQL 77
Cdd:PRK09912   52 AFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDELIISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQL 157
Cdd:PRK09912  130 EYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGL 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 158 PELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASL--KCYQWLKERIVSEegrKQQNKLKDLSPIAERLGCTLPQLA 235
Cdd:PRK09912  209 LDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHRegNKVRGLTPKMLTE---ANLNSLRLLNEMAQQRGQSMAQMA 285
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034635487 236 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 268
Cdd:PRK09912  286 LSWLLKDERVTSVLIGASRAEQLEENVQALNNL 318
AKR_AKR9A_9B cd19080
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ...
5-267 6.33e-52

AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.


Pssm-ID: 381306 [Multi-domain]  Cd Length: 307  Bit Score: 172.40  E-value: 6.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   5 YESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYWG--GKAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd19080    41 VEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLATKYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYH 162
Cdd:cd19080   118 LYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMAR 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGIISGKYGNGvpESSRASLKCYQWLKERIVSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRN 242
Cdd:cd19080   197 ALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTVGFGKLTERNWAIVDVVAA---VAEELGRSAAQVALAWVRQK 271
                         250       260
                  ....*....|....*....|....*
gi 1034635487 243 EGVSSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19080   272 PGVVIPIIGARTLEQLKDNLGALDL 296
AKR_AKR11B3 cd19085
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ...
4-285 2.03e-50

Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.


Pssm-ID: 381311 [Multi-domain]  Cd Length: 292  Bit Score: 168.15  E-value: 2.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19085    32 ALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS-------PDNLTPEDVRKSCERSLKRLGTDYIDLY 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmipPVCEQAEYHLFQREKVEVQLPEL-YH 162
Cdd:cd19085   102 QIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR------IDSNQLPYNLLWRAIEYEILPFCrEH 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVgaMTWSPLACGIISGKYGNG---VPESSRASLkcyqwlkeRIVSEEG--RKQQNKLKDLSPIAERLGCTLPQLAVA 237
Cdd:cd19085   176 GIGV--LAYSPLAQGLLTGKFSSAedfPPGDARTRL--------FRHFEPGaeEETFEALEKLKEIADELGVTMAQLALA 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034635487 238 WCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRN 285
Cdd:cd19085   246 WVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDEISDP 291
AKR_AKR11A1_11D1 cd19083
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ...
4-282 1.78e-42

AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).


Pssm-ID: 381309 [Multi-domain]  Cd Length: 307  Bit Score: 147.95  E-value: 1.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTK--LYWGGKaETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19083    42 ALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVVIATKgaHKFGGD-GSVLNNSPEFLRSAVEKSLKRLNTDYID 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  82 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAySVARQFNMIppvceQAEYHLFQREKVEVQLPELy 161
Cdd:cd19083   119 LYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC- 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGIISGKYGNGVpessraSLKCYQWLKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLAVAWC 239
Cdd:cd19083   192 VENNISFIPYFPLASGLLAGKYTKDT------KFPDNDLRNDKPLFKGERFSENldKVDKLKSIADEKGVTVAHLALAWY 265
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034635487 240 LRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNI 282
Cdd:cd19083   266 LTRPAIDVVIPGAKRAEQVIDNLKALDV--TLTEEEIAFIDAL 306
AKR_unchar cd19102
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
4-283 7.34e-42

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381328 [Multi-domain]  Cd Length: 302  Bit Score: 146.28  E-value: 7.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSsLVITTK--LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19102    35 ALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDR-PIVATKcgLLWDEEGRIRRSLKPASIRAECEASLRRLGVDVID 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  82 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEImeaysvaRQFNMIPPVCE-QAEYHLFQREKVEVQLPel 160
Cdd:cd19102   112 LYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQM-------KRCQAIHPIASlQPPYSLLRRGIEAEILP-- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 Y---HKIGVgaMTWSPLACGIISGKYGngvPESSrASLKCYQWLK-ERIVSEEGRKQQNKLKD-LSPIAERLGCTLPQLA 235
Cdd:cd19102   183 FcaeHGIGV--IVYSPMQSGLLTGKMT---PERV-ASLPADDWRRrSPFFQEPNLARNLALVDaLRPIAERHGRTVAQLA 256
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034635487 236 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNIL 283
Cdd:cd19102   257 IAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIEALL 302
AKR_AKR13C1_2 cd19078
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ...
4-283 9.40e-42

AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.


Pssm-ID: 381304 [Multi-domain]  Cd Length: 301  Bit Score: 145.84  E-value: 9.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW----GGKAETERGLSRKHIIEGLKGSLQRLQLEY 79
Cdd:cd19078    34 AVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGFkidgGKPGPLGLDSRPEHIRKAVEGSLKRLQTDY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  80 VDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLPE 159
Cdd:cd19078   111 IDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAVC------PVTAVQSEYSMMWREPEKEVLPT 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 160 LyHKIGVGAMTWSPLACGIISGKYGNGV---PESSRASLKCYqwlkerivSEEGRKQQNKLKDL-SPIAERLGCTLPQLA 235
Cdd:cd19078   185 L-EELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLPRF--------TPEALEANQALVDLlKEFAEEKGATPAQIA 255
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034635487 236 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNIL 283
Cdd:cd19078   256 LAWLLAKKPWIVPIPGTTKLSRLEENIGAADI--ELTPEELREIEDAL 301
AKR_AtPLR-like cd19093
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ...
3-264 9.79e-42

Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.


Pssm-ID: 381319 [Multi-domain]  Cd Length: 293  Bit Score: 145.45  E-value: 9.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   3 IAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKLywggkAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd19093    34 AALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF-----APLPWRLTRRSVVKALKASLERLGLDSIDL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  83 VFANRPDSN-TPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELY 161
Cdd:cd19093   108 YQLHWPGPWySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERG-VPLASNQVEYSLLYRDPEQNGLLPAC 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGIISGKYG--NGVPESSRASLKCYQWLKERIVseegrkqqnkLKDLSPIAERLGCTLPQLAVAWC 239
Cdd:cd19093   187 DELGITLIAYSPLAQGLLTGKYSpeNPPPGGRRRLFGRKNLEKVQPL----------LDALEEIAEKYGKTPAQVALNWL 256
                         250       260
                  ....*....|....*....|....*
gi 1034635487 240 LRNEGVssVLLGSSTPEQLIENLGA 264
Cdd:cd19093   257 IAKGVV--PIPGAKNAEQAEENAGA 279
AKR_AKR13A_13D cd19076
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ...
4-279 1.86e-40

AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.


Pssm-ID: 381302 [Multi-domain]  Cd Length: 303  Bit Score: 142.35  E-value: 1.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKlyWG---GKAETERGL--SRKHIIEGLKGSLQRLQLE 78
Cdd:cd19076    41 ALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEVVIATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  79 YVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLP 158
Cdd:cd19076   116 VIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTIRRAHAVH------PITAVQSEYSLWTRDIEDEVLP 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 159 ---ELyhkiGVGAMTWSPLACGIISGKYGNgvPESSRASLkcYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLA 235
Cdd:cd19076   190 tcrEL----GIGFVAYSPLGRGFLTGAIKS--PEDLPEDD--FRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLA 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034635487 236 VAWCL-RNEGVSSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEI 279
Cdd:cd19076   262 LAWVLaQGDDIVPI-PGTKRIKYLEENVGALDV--VLTPEELAEI 303
AKR_AKR11B2 cd19149
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ...
3-267 7.68e-40

Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.


Pssm-ID: 381375 [Multi-domain]  Cd Length: 315  Bit Score: 141.26  E-value: 7.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   3 IAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTK--LYWGGKAETE----------RGLSRKHIIEGLKG 70
Cdd:cd19149    41 AALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVVLATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  71 SLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEaYSVARQFNMIppvceQAEYHLFQR 150
Cdd:cd19149   118 SLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKE-YVKAGQLDII-----QEKYSMLDR 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 151 EKVEVQLPeLYHKIGVGAMTWSPLACGIISGKYGNG---VPESSRASLKCYQwlkerivsEEGRKQQNKLKD-LSPIAER 226
Cdd:cd19149   192 GIEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITPDrefDAGDARSGIPWFS--------PENREKVLALLEkWKPLCEK 262
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034635487 227 LGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19149   263 YGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI 303
AKR_AKR3F1-like cd19072
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ...
4-266 7.61e-39

Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381298 [Multi-domain]  Cd Length: 263  Bit Score: 137.36  E-value: 7.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19072    35 AIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS-------PDHLKYDDVIKAAKESLKRLGTDYIDLY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQfnmIPPVCEQAEYHLFQREkVEVQLPELYHK 163
Cdd:cd19072   106 LIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKK---GPIVANQVEYNLFDRE-EESGLLPYCQK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 164 IGVGAMTWSPLACGIISGKYGngvpessraslkcyqwlkerivseegrkqqnkLKDLSPIAERLGCTLPQLAVAWCLRNE 243
Cdd:cd19072   182 NGIAIIAYSPLEKGKLSNAKG--------------------------------SPLLDEIAKKYGKTPAQIALNWLISKP 229
                         250       260
                  ....*....|....*....|...
gi 1034635487 244 GVsSVLLGSSTPEQLIENLGAIQ 266
Cdd:cd19072   230 NV-IAIPKASNIEHLEENAGALG 251
AKR_AKR11C1 cd19086
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ...
4-264 5.46e-38

AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.


Pssm-ID: 381312 [Multi-domain]  Cd Length: 238  Bit Score: 134.14  E-value: 5.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKL--YWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19086    33 ALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRFDGGPERPQDFSPEYIREAVEASLKRLGTDYID 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  82 VVFA-NRPDSNTPMEEIVRAMTHVINQGMAMYWGTS---RWSAMEIMEAYSVArqfnmippvCEQAEYHLFQREKVEVQL 157
Cdd:cd19086   110 LYQLhNPPDEVLDNDELFEALEKLKQEGKIRAYGVSvgdPEEALAALRRGGID---------VVQVIYNLLDQRPEEELF 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 158 PELyHKIGVGAMTWSPLACGIISGKygngvpessraslkcyqwlkerivseegrkqqnklkdlspiaerlgctLPQLAVA 237
Cdd:cd19086   181 PLA-EEHGVGVIARVPLASGLLTGK------------------------------------------------LAQAALR 211
                         250       260
                  ....*....|....*....|....*..
gi 1034635487 238 WCLRNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19086   212 FILSHPAVSTVIPGARSPEQVEENAAA 238
AKR_AKR10A1_2 cd19082
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ...
5-264 9.73e-38

AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.


Pssm-ID: 381308 [Multi-domain]  Cd Length: 291  Bit Score: 134.99  E-value: 9.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   5 YESGVNLFDTAEVYAA----GKAEVILGSIIKKKGwRRSSLVITTKlywGG-----KAETERgLSRKHIIEGLKGSLQRL 75
Cdd:cd19082    27 VELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhpdleDMSRSR-LSPEDIRADLEESLERL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  76 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFqrEKVEV 155
Cdd:cd19082   102 GTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFAASSPQWSLA--RPNEP 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 156 QLP------------ELYHKIGVGAMTWSPLACGIISGKYGNGVpESSRASLKCYQwlkerivSEEGRKQQNKLKDLspi 223
Cdd:cd19082   180 PWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSKRAAGGA-EDDSELRRVYY-------SEENFERLERAKEL--- 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034635487 224 AERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19082   249 AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAA 289
AKR_AKR7A1-5 cd19075
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ...
5-282 6.80e-37

AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.


Pssm-ID: 381301 [Multi-domain]  Cd Length: 304  Bit Score: 133.07  E-value: 6.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   5 YESGVNLFDTAEVYAAGKAEVILGSIikkkGWRRSSLVITTKLY-WGGKaeterGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19075    30 LERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKANpGVGG-----GLSPENVRKQLETSLKRLKVDKVDVF 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQReKVEVQLPELYHK 163
Cdd:cd19075   101 YLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQGMYNAITR-QVETELFPCLRK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 164 IGVGAMTWSPLACGIISGKY--GNGVPESSR-----ASLKCYQ--WLKERIVSEegrkqqnkLKDLSPIAERLGCTLPQL 234
Cdd:cd19075   180 LGIRFYAYSPLAGGFLTGKYkySEDKAGGGRfdpnnALGKLYRdrYWKPSYFEA--------LEKVEEAAEKEGISLAEA 251
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034635487 235 AVAWC-----LRNEGVSSVLLGSSTPEQLIENLGAIQV--LPKmtsHVVNEIDNI 282
Cdd:cd19075   252 ALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKgpLPE---EVVKAIDEA 303
AKR_unchar cd19752
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
5-264 1.33e-31

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381391 [Multi-domain]  Cd Length: 291  Bit Score: 118.97  E-value: 1.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   5 YESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK-----LYWGGKAETERGLSRKHIIEGLKGSL 72
Cdd:cd19752    27 VAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKvgagpRDPDGGPESPEGLSAETIEQEIDKSL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  73 QRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQR-- 150
Cdd:cd19752   106 RRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHSYLRPrp 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 151 ---EKVEVQL-PEL-----YHKiGVGAMTWSPLacgiISGKYGNgvpeSSRASLKCYqwlkerivseEGRKQQNKLKDLS 221
Cdd:cd19752   186 gadFGVQRIVtDELldyasSRP-DLTLLAYSPL----LSGAYTR----PDRPLPEQY----------DGPDSDARLAVLE 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034635487 222 PIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19752   247 EVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAA 289
AKR_YeaE cd19138
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ...
6-280 1.69e-31

Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381364 [Multi-domain]  Cd Length: 266  Bit Score: 118.12  E-value: 1.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   6 ESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFA 85
Cdd:cd19138    40 DLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVL-------PSNASRQGTVRACERSLRRLGTDYLDLYLL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  86 NRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMippVCEQAEYHLFQReKVEVQLPELYHKIG 165
Cdd:cd19138   110 HWR-GGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNC---AANQVLYNLGSR-GIEYDLLPWCREHG 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 166 VGAMTWSPLACGiisGKYGNGVPESSraslkcyqwlkerivseegrkqqnklkDLSPIAERLGCTLPQLAVAWCLRNEGV 245
Cdd:cd19138   185 VPVMAYSPLAQG---GLLRRGLLENP---------------------------TLKEIAARHGATPAQVALAWVLRDGNV 234
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034635487 246 SSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 280
Cdd:cd19138   235 IAI-PKSGSPEHARENAAAADL--ELTEEDLAELD 266
AKR_AKR11B1 cd19148
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ...
2-258 2.48e-30

Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381374 [Multi-domain]  Cd Length: 302  Bit Score: 115.87  E-value: 2.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   2 TI--AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTK--LYWGGKAETERGLSRKHIIEGLKGSLQRLQL 77
Cdd:cd19148    30 TIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKvgLEWDEGGEVVRNSSPARIRKEVEDSLRRLQT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAmEIMEAY-SVARQFNMIPPvceqaeYHLFQREKVEVQ 156
Cdd:cd19148   109 DYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSP-EQMETFrKVAPLHTVQPP------YNLFEREIEKDV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 157 LP-ELYHKIGVgaMTWSPLACGIISGKYGngvPESS------RASLKCYQwlkerivseEGRKQQ-----NKLKDLSpiA 224
Cdd:cd19148   182 LPyARKHNIVT--LAYGALCRGLLSGKMT---KDTKfegddlRRTDPKFQ---------EPRFSQylaavEELDKLA--Q 245
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034635487 225 ERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQL 258
Cdd:cd19148   246 ERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQL 279
AKR_AKR3F1 cd19137
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ...
4-267 4.91e-30

Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.


Pssm-ID: 381363 [Multi-domain]  Cd Length: 260  Bit Score: 114.20  E-value: 4.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19137    35 AIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW-------PTNLRYDDLLRSLQNSLRRLDTDYIDLY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQfnmiPPVCEQAEYHLFQREKVEVQLPELYHK 163
Cdd:cd19137   106 LIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT----PIVCNQVKYNLEDRDPERDGLLEYCQK 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 164 IGVGAMTWSPLACGIIsgkygngvpessraslkcyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRNE 243
Cdd:cd19137   182 NGITVVAYSPLRRGLE---------------------KTNRTLEE--------------IAKNYGKTIAQIALAWLIQKP 226
                         250       260
                  ....*....|....*....|....
gi 1034635487 244 GVSSVLLgSSTPEQLIENLGAIQV 267
Cdd:cd19137   227 NVVAIPK-AGRVEHLKENLKATEI 249
AKR_PA4992-like cd19095
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ...
4-264 2.09e-29

Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381321 [Multi-domain]  Cd Length: 253  Bit Score: 111.94  E-value: 2.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaaGKAEVILGSIIKkkGWRRSSLVITTKL--YWGGkAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19095    29 ALDLGINLIDTAPAY--GRSEERLGRALA--GLRRDDLFIATKVgtHGEG-GRDRKDFSPAAIRASIERSLRRLGTDYID 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  82 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRwSAMEIMEAYSVARqFNMIppvceQAEYHLFQREKVEVqLPELY 161
Cdd:cd19095   104 LLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSG-DGEELEAAIASGV-FDVV-----QLPYNVLDREEEEL-LPLAA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 -HKIGVGAMtwSPLAcgiisgkygNGVPESSRASLKCYQWLKERivseegrkqqnklkdLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19095   176 eAGLGVIVN--RPLA---------NGRLRRRVRRRPLYADYARR---------------PEFAAEIGGATWAQAALRFVL 229
                         250       260
                  ....*....|....*....|....
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19095   230 SHPGVSSAIVGTTNPEHLEENLAA 253
AKR_BsYcsN_EcYdhF-like cd19092
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ...
4-272 2.82e-29

Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.


Pssm-ID: 381318 [Multi-domain]  Cd Length: 287  Bit Score: 112.65  E-value: 2.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK---LYWGGKAETERG---LSRKHIIEGLKGSLQRLQL 77
Cdd:cd19092    33 ALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRLGDDPRPGRIKhydTSKEHILASVEGSLKRLGT 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMeimeaysvarQFNM------IPPVCEQAEYHLFQRE 151
Cdd:cd19092   113 DYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPS----------QIELlqsyldQPLVTNQIELSLLHTE 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 152 KVEV----QLPELYHKIgvgaMTWSPLACGiisgkygngvpessraslkcyqwlkeRIVSEEGRKQQNKLKDLSPIAERL 227
Cdd:cd19092   183 AIDDgtldYCQLLDITP----MAWSPLGGG--------------------------RLFGGFDERFQRLRAALEELAEEY 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034635487 228 GCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMT 272
Cdd:cd19092   233 GVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI--ELT 275
ARA1 COG0656
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ...
4-264 8.90e-29

Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440421 [Multi-domain]  Cd Length: 259  Bit Score: 110.53  E-value: 8.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAeterglSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:COG0656    27 ALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDNH------GYDDTLAAFEESLERLGLDYLDLY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREkvevqlPEL--Y 161
Cdd:COG0656    97 LIHWP-GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG----VKPAVNQVELHPYLQQ------RELlaF 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HK-IGVGAMTWSPLAcgiisgkygngvpessRASLkcyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCL 240
Cdd:COG0656   166 CReHGIVVEAYSPLG----------------RGKL-----LDDPVLAE--------------IAEKHGKTPAQVVLRWHL 210
                         250       260
                  ....*....|....*....|....
gi 1034635487 241 RNeGVsSVLLGSSTPEQLIENLGA 264
Cdd:COG0656   211 QR-GV-VVIPKSVTPERIRENLDA 232
tas PRK10625
putative aldo-keto reductase; Provisional
4-284 1.46e-28

putative aldo-keto reductase; Provisional


Pssm-ID: 236727 [Multi-domain]  Cd Length: 346  Bit Score: 111.87  E-value: 1.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwRRSSLVITTKLywGGKAET-------ERGLSRKHIIEGLK 69
Cdd:PRK10625   39 AVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-SREKLIIASKV--SGPSRNndkgirpNQALDRKNIREALH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  70 GSLQRLQLEYVD---VVFANRP-----------DSNTP---MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQ 132
Cdd:PRK10625  116 DSLKRLQTDYLDlyqVHWPQRPtncfgklgyswTDSAPavsLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEK 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 133 FNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGV-PESSRASLKcyqwlkERIVSEEGR 211
Cdd:PRK10625  196 HDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCLAFGTLTGKYLNGAkPAGARNTLF------SRFTRYSGE 268
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034635487 212 KQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILR 284
Cdd:PRK10625  269 QTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIESLHL--TLSEEVLAEIEAVHQ 339
AKR_unchar cd19105
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
4-265 9.64e-28

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381331 [Multi-domain]  Cd Length: 250  Bit Score: 107.67  E-value: 9.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKLYWGGKAETerglsRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19105    34 ALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLATKASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 F---ANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME--IMEA-----YSVArqfnMIPpvceqaeY-HLFQREK 152
Cdd:cd19105   107 QlhgVDTPEERLLNEELLEALEKLKKEGKVRFIGFSTHDNMAevLQAAiesgwFDVI----MVA-------YnFLNQPAE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 153 VEVQLPELY-HKIGVGAMTwsPLACGIisgkygngvpessraslkcyqwlkerivSEEGRKQQNKLKDLSpiaerlgctL 231
Cdd:cd19105   176 LEEALAAAAeKGIGVVAMK--TLAGGY----------------------------LQPALLSVLKAKGFS---------L 216
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034635487 232 PQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 265
Cdd:cd19105   217 PQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
AKR_AKR8A1-2 cd19077
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ...
1-280 1.16e-27

AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).


Pssm-ID: 381303 [Multi-domain]  Cd Length: 302  Bit Score: 108.48  E-value: 1.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYAAGKAEV---ILGSIIKKKGWRRSSLVITTKlywGGKAET--ERGLSRKHIIEGLKGSLQRL 75
Cdd:cd19077    31 MKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSVK---GGLDPDtlRPDGSPEAVRKSIENILRAL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  76 -QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVE 154
Cdd:cd19077   108 gGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAVH------PIAAVEVEYSLFSREIEE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 155 VQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYqwlkERIVSEEGRKQQNKLKDLSPIAERLGCTLPQL 234
Cdd:cd19077   182 NGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHL----DRFNGENFEKNLKLVDALQELAEKKGCTPAQL 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034635487 235 AVAWCLRNEGVSSV-LLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 280
Cdd:cd19077   258 ALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTDEELKEIN 302
AKR_AKR15A-like cd19090
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ...
4-266 1.75e-27

AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).


Pssm-ID: 381316 [Multi-domain]  Cd Length: 278  Bit Score: 107.64  E-value: 1.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaaGKAEVILGSIIKkkGWRRSSLVITTKLywGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19090    29 ALDLGINYIDTAPAY--GDSEERLGLALA--ELPREPLVLSTKV--GRLPEDTADYSADRVRRSVEESLERLGRDRIDLL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNTPMEE-----IVRAMTHVINQGMAMYWGTSRWSAmEIMEAYSVARQFNMIPPVCeqaEYHLFQREKVEVQLP 158
Cdd:cd19090   103 MIHDPERVPWVDIlapggALEALLELKEEGLIKHIGLGGGPP-DLLRRAIETGDFDVVLTAN---RYTLLDQSAADELLP 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 159 ELYHKiGVGAMTWSPLACGIISGKYgngvPESSRASlkcYQWLKERivseegrkQQNKLKDLSPIAERLGCTLPQLAVAW 238
Cdd:cd19090   179 AAARH-GVGVINASPLGMGLLAGRP----PERVRYT---YRWLSPE--------LLDRAKRLYELCDEHGVPLPALALRF 242
                         250       260
                  ....*....|....*....|....*...
gi 1034635487 239 CLRNEGVSSVLLGSSTPEQLIENLGAIQ 266
Cdd:cd19090   243 LLRDPRISTVLVGASSPEELEQNVAAAE 270
AKR_AKR13D1 cd19145
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ...
4-279 1.18e-26

AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.


Pssm-ID: 381371 [Multi-domain]  Cd Length: 304  Bit Score: 105.98  E-value: 1.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKL---YWGGKAETERGlSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19145    42 AFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQLATKFgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREkVEVQLPEL 160
Cdd:cd19145   119 DLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRAHAVH------PITAVQLEWSLWTRD-IEEEIIPT 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKygnGVPESSRASLKCYQWLKeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19145   192 CRELGIGIVPYSPLGRGFFAGK---AKLEELLENSDVRKSHP-RFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVL 267
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034635487 241 -RNEGVSSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEI 279
Cdd:cd19145   268 hQGEDVVPI-PGTTKIKNLNQNIGALSV--KLTKEDLKEI 304
AKR_AKR13A1 cd19144
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ...
4-287 1.27e-26

AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.


Pssm-ID: 381370 [Multi-domain]  Cd Length: 323  Bit Score: 106.37  E-value: 1.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSLVITTKlyWGGKAETERGL-----SRKHIIEGLKGSLQRLQLE 78
Cdd:cd19144    43 AFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKIFLATK--FGIEKNVETGEysvdgSPEYVKKACETSLKRLGVD 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  79 YVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLF--QREKVEVQ 156
Cdd:cd19144   119 YIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHAVH------PIAAVQIEYSPFslDIERPEIG 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 157 LPELYHKIGVGAMTWSPLACGIISGKYgngvpeSSRASLKCYQWLKE--RIVSEEGRKQQNKLKDLSPIAERLGCTLPQL 234
Cdd:cd19144   193 VLDTCRELGVAIVAYSPLGRGFLTGAI------RSPDDFEEGDFRRMapRFQAENFPKNLELVDKIKAIAKKKNVTAGQL 266
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034635487 235 AVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKP 287
Cdd:cd19144   267 TLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV--KLTEEEEKEIREIAEEAE 317
AKR_AKR13B1 cd19088
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ...
4-264 4.66e-26

AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.


Pssm-ID: 381314 [Multi-domain]  Cd Length: 256  Bit Score: 103.45  E-value: 4.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW--GGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19088    33 ALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKGGLvrTGPGWWGPDGSPEYLRQAVEASLRRLGLDRID 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  82 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIppVCEQAEYHLFQREKVEVQlpELY 161
Cdd:cd19088   110 LYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR----I--VSVQNRYNLANRDDEGVL--DYC 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLAcgiisgkyGNGVPESSRaslkcyqwlkerivseegrkqqnklkDLSPIAERLGCTLPQLAVAWCLR 241
Cdd:cd19088   182 EAAGIAFIPWFPLG--------GGDLAQPGG--------------------------LLAEVAARLGATPAQVALAWLLA 227
                         250       260
                  ....*....|....*....|...
gi 1034635487 242 NEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19088   228 RSPVMLPIPGTSSVEHLEENLAA 250
YdhF COG4989
Predicted oxidoreductase YdhF [General function prediction only];
4-272 1.30e-25

Predicted oxidoreductase YdhF [General function prediction only];


Pssm-ID: 444013 [Multi-domain]  Cd Length: 299  Bit Score: 102.92  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK---LYWGGKAETERG---LSRKHIIEGLKGSLQRLQL 77
Cdd:COG4989    40 ALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQTKcgiRLPSEARDNRVKhydTSKEHIIASVEGSLRRLGT 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMeimeaysvarQFNMI------PPVCEQAEYHLFQRE 151
Cdd:COG4989   120 DYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNFTPS----------QFELLqsaldqPLVTNQIELSLLHTD 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 152 KVE------VQLpelyHKIGVgaMTWSPLACGIISGKYgngvpessraslkcyqwlkerivSEEGRKQQNKLKDlspIAE 225
Cdd:COG4989   190 AFDdgtldyCQL----NGITP--MAWSPLAGGRLFGGF-----------------------DEQFPRLRAALDE---LAE 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034635487 226 RLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMT 272
Cdd:COG4989   238 KYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDI--ELT 282
AKR_FDH cd19162
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ...
4-264 9.99e-23

D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.


Pssm-ID: 381388 [Multi-domain]  Cd Length: 290  Bit Score: 95.12  E-value: 9.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKL-------YWGGKAETER--GLSRKHIIEGLKGSLQR 74
Cdd:cd19162    28 AWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAGRPAGADRrfDFSADGIRRSIEASLER 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  75 LQLEYVDVVFANRPDS--NTPMEEIVRAMTHVINQGM--AMYWGTSRWSAmeimeAYSVARQFN----MIPpvceqAEYH 146
Cdd:cd19162   106 LGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVvgAIGVGVTDWAA-----LLRAARRADvdvvMVA-----GRYT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 147 LFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGkygnGVPESSRASlkcYQWLKERIVSeegRKQQnklkdLSPIAER 226
Cdd:cd19162   176 LLDRRAATELLPLCAAK-GVAVVAAGVFNSGILAT----DDPAGDRYD---YRPATPEVLA---RARR-----LAAVCRR 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034635487 227 LGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19162   240 YGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
AKR_unchar cd19104
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
4-282 1.87e-22

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381330 [Multi-domain]  Cd Length: 321  Bit Score: 95.02  E-value: 1.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKgwrRSSLVITTKlywGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19104    41 ALDLGINFFDTAPSYGDGKSEENLGRALKGL---PAGPYITTK---VRLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FA-NRPDSNTP--------------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIppvceQAEYHL- 147
Cdd:cd19104   115 QLhNRIGDERDkpvggtlsttdvlgLGGVADAFERLRSEGKIRFIGITGLGNPPAIRELLDSGKFDAV-----QVYYNLl 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 148 -----FQREKVEV-----QLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRAslkcyqwlkERIVSEEGRKQqnkl 217
Cdd:cd19104   190 npsaaEARPRGWSaqdygGIIDAAAEHGVGVMGIRVLAAGALTTSLDRGREAPPTS---------DSDVAIDFRRA---- 256
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034635487 218 KDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPkMTSHVVNEIDNI 282
Cdd:cd19104   257 AAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAEAAGP-LPAENLARLEAL 320
AKR_AKR9A1-2 cd19146
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ...
5-283 4.14e-22

Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.


Pssm-ID: 381372 [Multi-domain]  Cd Length: 326  Bit Score: 94.03  E-value: 4.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   5 YESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL---YWGGKAETER----GLSRKHIIEGLKGSLQRLQL 77
Cdd:cd19146    45 YEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKYttgYRRGGPIKIKsnyqGNHAKSLRLSVEASLKKLQT 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHL----FQREKV 153
Cdd:cd19146   124 SYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDIL 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 154 EVQLPElyhkiGVGAMTWSPLAcgiiSGKYGNGVPESSRASLKCYQWLKerivSEEGRKQQNKLKDlspIAERLGCTLPQ 233
Cdd:cd19146   204 PMCEAE-----GMALAPWGVLG----QGQFRTEEEFKRRGRSGRKGGPQ----TEKERKVSEKLEK---VAEEKGTAITS 267
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034635487 234 LAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNIL 283
Cdd:cd19146   268 VALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI--SLSDEEIQEIEDAY 315
AKR_AKR1-5-like cd19071
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ...
4-262 1.99e-20

AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.


Pssm-ID: 381297 [Multi-domain]  Cd Length: 251  Bit Score: 87.92  E-value: 1.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGgkaeteRGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19071    23 ALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKL-WP------TDHGYERVREALEESLKDLGLDYLDLY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 -----FANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLF--QREKVEv 155
Cdd:cd19071    93 lihwpVPGKEgGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR----IKPAVNQIELHPYlqQKELVE- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 156 qlpelY-HKIGVGAMTWSPLACGiisgkygngvpesSRASLKCyqwlkerivseegrkqqnklKDLSPIAERLGCTLPQL 234
Cdd:cd19071   168 -----FcKEHGIVVQAYSPLGRG-------------RRPLLDD--------------------PVLKEIAKKYGKTPAQV 209
                         250       260
                  ....*....|....*....|....*...
gi 1034635487 235 AVAWCLRNeGVsSVLLGSSTPEQLIENL 262
Cdd:cd19071   210 LLRWALQR-GV-VVIPKSSNPERIKENL 235
AKR_AKR3F2_3 cd19073
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ...
4-264 3.77e-20

Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.


Pssm-ID: 381299 [Multi-domain]  Cd Length: 243  Bit Score: 86.94  E-value: 3.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGkaetergLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19073    23 ALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------LRPEDLKKSVDRSLEKLGTDYVDLL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREKVEVQLPely 161
Cdd:cd19073    93 LIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIAVNQVEFHpfLYQAELLEYCRE--- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAmtWSPLACGiisgkygnGVPESSRaslkcyqwLKErivseegrkqqnklkdlspIAERLGCTLPQLAVAWCLR 241
Cdd:cd19073   166 NDIVITA--YSPLARG--------EVLRDPV--------IQE-------------------IAEKYDKTPAQVALRWLVQ 208
                         250       260
                  ....*....|....*....|...
gi 1034635487 242 nEGVsSVLLGSSTPEQLIENLGA 264
Cdd:cd19073   209 -KGI-VVIPKASSEDHLKENLAI 229
AKR_unchar cd19097
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
4-270 1.84e-19

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381323 [Multi-domain]  Cd Length: 267  Bit Score: 85.66  E-value: 1.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaaGKAEVILGSIIKKKgwrrSSLVITTKLywgGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19097    35 ALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL---PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSvARQFNMIppvceQAEYHLF-QREKVEVQLPELy 161
Cdd:cd19097   106 LLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALE-SFKIDII-----QLPFNILdQRFLKSGLLAKL- 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGIIsgkygngVPESSRASLKCYQWlkerivseegrkqQNKLKDLSPIAERLGCTLPQLAVAWCLR 241
Cdd:cd19097   179 KKKGIEIHARSVFLQGLL-------LMEPDKLPAKFAPA-------------KPLLKKLHELAKKLGLSPLELALGFVLS 238
                         250       260
                  ....*....|....*....|....*....
gi 1034635487 242 NEGVSSVLLGSSTPEQLIENLGAIQVLPK 270
Cdd:cd19097   239 LPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
AKR_Fe-S_oxidoreductase cd19096
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ...
4-264 1.11e-18

Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381322 [Multi-domain]  Cd Length: 255  Bit Score: 83.38  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGgkaeteRGLSRKHIIEGLKGSLQRLQLEYVDvV 83
Cdd:cd19096    30 AIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW------SVKSAEDFRRILEESLKRLGVDYID-F 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FA----NRPD------SNTPMEEIVRAMT-----HVinqGMamywgTSRWSA---MEIMEAYsvarQFNMIppvceQAEY 145
Cdd:cd19096   101 YLlhglNSPEwlekarKGGLLEFLEKAKKeglirHI---GF-----SFHDSPellKEILDSY----DFDFV-----QLQY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 146 HLFQREKVEVQ-LPELYHKIGVGAMTWSPLACGIISgkygngvpessraslkcyqwlkerivseegrkqqNKLKDLSPIA 224
Cdd:cd19096   164 NYLDQENQAGRpGIEYAAKKGMGVIIMEPLKGGGLA----------------------------------NNPPEALAIL 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034635487 225 ERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19096   210 CGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAA 249
AKR_AKR3F3 cd19140
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ...
4-262 1.11e-18

Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.


Pssm-ID: 381366 [Multi-domain]  Cd Length: 253  Bit Score: 83.08  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWGGkaetergLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19140    30 ALELGYRHIDTAQMYG-NEAQV--GEAIAASGVPRDELFLTTKVWPDN-------YSPDDFLASVEESLRKLRTDYVDLL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQRekvevQLPELY 161
Cdd:cd19140   100 LLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE----APLFTNQVEYHpyLDQR-----KLLDAA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLR 241
Cdd:cd19140   171 REHGIALTAYSPLARG---------------------EVLKDPVLQE--------------IGRKHGKTPAQVALRWLLQ 215
                         250       260
                  ....*....|....*....|.
gi 1034635487 242 NEGVsSVLLGSSTPEQLIENL 262
Cdd:cd19140   216 QEGV-AAIPKATNPERLEENL 235
AKR_galDH cd19163
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ...
4-265 4.46e-17

L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).


Pssm-ID: 381389 [Multi-domain]  Cd Length: 293  Bit Score: 79.52  E-value: 4.46e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKL--YwGGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19163    42 ALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSYYLATKVgrY-GLDPDKMFDFSAERITKSVEESLKRLGLDYID 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  82 VV------FAnrPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSaMEIMeAYSVARQFNMIPPVCEQAEYHLFQREKVEv 155
Cdd:cd19163   119 IIqvhdieFA--PSLDQILNETLPALQKLKEEGKVRFIGITGYP-LDVL-KEVLERSPVKIDTVLSYCHYTLNDTSLLE- 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 156 qLPELYHKIGVGAMTWSPLACGIISGKygnGVPESSRASlkcyQWLKERIvseegrkqqnklKDLSPIAERLGCTLPQLA 235
Cdd:cd19163   194 -LLPFFKEKGVGVINASPLSMGLLTER---GPPDWHPAS----PEIKEAC------------AKAAAYCKSRGVDISKLA 253
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034635487 236 VAWCLRNEGVSSVLLGSSTPEQLIENLGAI 265
Cdd:cd19163   254 LQFALSNPDIATTLVGTASPENLRKNLEAA 283
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
4-262 1.59e-16

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];


Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 78.71  E-value: 1.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVITTKLYWGGKaeterglSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:COG1453    38 AIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVILATKLPPWVR-------DPEDMRKDLEESLKRLQTDYIDLY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FanrpdsntpmeeIvramtHVINQGMAMYWGTSRWSAMEIMEAysvARQ----------FNMIPPVCEQA-E-------- 144
Cdd:COG1453   106 L------------I-----HGLNTEEDLEKVLKPGGALEALEK---AKAegkirhigfsTHGSLEVIKEAiDtgdfdfvq 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 145 ---YHLFQREKVEVQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyqwlkerivseegrkqqnKLKDLS 221
Cdd:COG1453   166 lqyNYLDQDNQAGEEALEAAAEKGIGVIIMKPLKGG--------------------------------------RLANPP 207
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034635487 222 PIAERLGC---TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENL 262
Cdd:COG1453   208 EKLVELLCpplSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENL 251
AKR_AKR1G1_CeAKR cd19154
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ...
1-262 3.05e-16

Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.


Pssm-ID: 381380 [Multi-domain]  Cd Length: 303  Bit Score: 77.07  E-value: 3.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITTKLYWGGkaetergLSRKHIIEGLKGSLQR 74
Cdd:cd19154    31 VRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITTKLWTHE-------HAPEDVEEALRESLKK 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  75 LQLEYVDVVFANRP-------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnm 135
Cdd:cd19154    99 LQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNAR---- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 136 IPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASLKCYQWlkerivseegrKQQN 215
Cdd:cd19154   175 VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL-----------GSPGRANFTKSTGVS-----------PAPN 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034635487 216 KLKD--LSPIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 262
Cdd:cd19154   230 LLQDpiVKAIAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENF 276
AKR_AKR3C2-3 cd19120
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ...
1-288 4.68e-16

Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.


Pssm-ID: 381346 [Multi-domain]  Cd Length: 269  Bit Score: 76.12  E-value: 4.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGKaeterglsrkHIIEGLKGSLQRLQLEYV 80
Cdd:cd19120    31 VKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK----------DPREALRKSLAKLGVDYV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  81 DVVFANRP----DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFqrekVEVQ 156
Cdd:cd19120    98 DLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK----IKPAVNQIEFHPY----LYPQ 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 157 LPEL--YHKigvgamtwsplACGIISGKYGNGVPessraslkcyqwlkerIVSEEGRKQQNKLKDlspIAERLGCTLPQL 234
Cdd:cd19120   170 QPALleYCR-----------EHGIVVSAYSPLSP----------------LTRDAGGPLDPVLEK---IAEKYGVTPAQV 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034635487 235 AVAWCLRNEGVssVLLGSSTPEQLIENLGAIqvLPKMTSHVVNEIDNILRNKPY 288
Cdd:cd19120   220 LLRWALQKGIV--VVTTSSKEERMKEYLEAF--DFELTEEEVEEIDKAGKQKHF 269
AKR_unchar cd19099
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
4-262 5.02e-16

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381325 [Multi-domain]  Cd Length: 316  Bit Score: 76.97  E-value: 5.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILG----SIIKKKGWRRSSLVITTKlywGG----------------KAETERGLSRKH 63
Cdd:cd19099    30 ALDSGINVIDTAINYRGGRSERLIGkalrELIEKGGIKRDEVVIVTK---AGyipgdgdeplrplkylEEKLGRGLIDVA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  64 IIEG-------------LKGSLQRLQLEYVDVVFANRP----------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 120
Cdd:cd19099   107 DSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPeeqllelgeeEFYDRLEEAFEALEEAVAEGKIRYYGISTWDG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 121 meiMEAYSVARQFNMIPPVCE---------------QAEYHLFQREKVEVQ---------LPELYHKIGVGAMTWSPLAc 176
Cdd:cd19099   187 ---FRAPPALPGHLSLEKLVAaaeevggdnhhfkviQLPLNLLEPEALTEKntvkgealsLLEAAKELGLGVIASRPLN- 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 177 giiSGKYGNGVPESSRAslkcyqwlkerivseegrkqqnklkdlspiAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPE 256
Cdd:cd19099   263 ---QGQLLGELRLADLL------------------------------ALPGGATLAQRALQFARSTPGVDSALVGMRRPE 309

                  ....*.
gi 1034635487 257 QLIENL 262
Cdd:cd19099   310 HVDENL 315
AKR_unchar cd19103
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
4-240 7.29e-16

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381329 [Multi-domain]  Cd Length: 299  Bit Score: 76.22  E-value: 7.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGGkaeteRGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19103    41 AMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI-----AGQSADPVADMLEGSLARLGTDYIDIY 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDsntpmeEIVRAMTHVI---NQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19103   114 WIHNPA------DVERWTPELIpllKSGKVKHVGVSNHNLAEIKRANEILAKAG-VSLSAVQNHYSLLYRSSEEAGILDY 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYG--NGVPESSraslkcyqwlkERIVSEEGRKQQnkLKDLSP----IAERLGCTLPQL 234
Cdd:cd19103   187 CKENGITFFAYMVLEQGALSGKYDtkHPLPEGS-----------GRAETYNPLLPQ--LEELTAvmaeIGAKHGASIAQV 253

                  ....*.
gi 1034635487 235 AVAWCL 240
Cdd:cd19103   254 AIAWAI 259
AKR_AKR15A cd19152
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ...
4-267 2.46e-15

AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.


Pssm-ID: 381378 [Multi-domain]  Cd Length: 308  Bit Score: 74.57  E-value: 2.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKLYWGGKAETERGLSRKHIIEGLKG------------- 70
Cdd:cd19152    29 AWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQEVEPTFEPGFWNPLPfdavfdysydgil 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  71 -----SLQRLQLEYVDVVFANRPDSNTP-----------MEEIVRAMTHVINQGMAMYW--GTSRWS-AMEIME-----A 126
Cdd:cd19152   107 rsiedSLQRLGLSRIDLLSIHDPDEDLAgaesdehfaqaIKGAFRALEELREEGVIKAIglGVNDWEvILRILEeadldW 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 127 YSVARQFNMIppvcEQAEYHLFqrekvevqLPELyHKIGVGAmtwsplacgIISGKYGNGVpessRASLKCYQWLKERIV 206
Cdd:cd19152   187 VMLAGRYTLL----DHSAAREL--------LPEC-EKRGVKV---------VNAGPFNSGF----LAGGDNFDYYEYGPA 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034635487 207 SEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19152   241 PPE---LIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLAT 298
AKR_unchar cd19101
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
5-264 2.85e-15

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381327 [Multi-domain]  Cd Length: 304  Bit Score: 74.55  E-value: 2.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   5 YESGVNLFDTAEVYaaGKAEVILGSIIKKKGW---RRSSLVITTKLYWGGKAETergLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19101    33 VDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIHTKWVPDPGELT---MTRAYVEAAIDRSLKRLGVDRLD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  82 VV-FANRPDSNTPMEEIVRAMTHVINQGMAMYWG-----TSRWSamEIMEAysvarqfnMIPPVCEQAEYHLFQReKVEV 155
Cdd:cd19101   108 LVqFHWWDYSDPGYLDAAKHLAELQEEGKIRHLGltnfdTERLR--EILDA--------GVPIVSNQVQYSLLDR-RPEN 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 156 QLPELYHKIGVGAMTWSPLACGIISGKYgNGVPESSR-----ASLKCYQwlkeRIVSEEG--RKQQNKLKDLSPIAERLG 228
Cdd:cd19101   177 GMAALCEDHGIKLLAYGTLAGGLLSEKY-LGVPEPTGpaletRSLQKYK----LMIDEWGgwDLFQELLRTLKAIADKHG 251
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034635487 229 CTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19101   252 VSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRA 287
AKR_galDH-like cd19153
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ...
4-268 2.94e-15

L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).


Pssm-ID: 381379 [Multi-domain]  Cd Length: 294  Bit Score: 74.49  E-value: 2.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETErgLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19153    42 AFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVGRYRDSEFD--YSAERVRASVATSLERLHTTYLDVV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANR---PDSNTPMEEIVRAMTHVINQGMAMYWGTSRWsAMEIMEaySVARQFNMIPPVCEQAEYHL-FQREKVEVQLPE 159
Cdd:cd19153   120 YLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY-PLDTLT--RATRRCSPGSLDAVLSYCHLtLQDARLESDAPG 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 160 LYHKIGVGAMTWSPLACGIISGKygnGVPE----------SSRASLKcyqWLKERIVSeegrkqqnklkdlspiaerlgc 229
Cdd:cd19153   197 LVRGAGPHVINASPLSMGLLTSQ---GPPPwhpasgelrhYAAAADA---VCASVEAS---------------------- 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034635487 230 tLPQLAVAWCLRNE-GVSSVLLGSSTPEQLIENLGAIQVL 268
Cdd:cd19153   249 -LPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVDAV 287
AKR_AKR3G1 cd19123
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ...
3-288 7.32e-15

AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.


Pssm-ID: 381349 [Multi-domain]  Cd Length: 297  Bit Score: 73.21  E-value: 7.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   3 IAYESGVNLFDTAEVYAaGKAEV--ILGSIIKKKGWRRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRLQLEYV 80
Cdd:cd19123    33 QALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKL-WNNSHAPE------DVLPALEKTLADLQLDYL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  81 D-------VVF---ANRPDSNT--------PMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQ 142
Cdd:cd19123   105 DlylmhwpVALkkgVGFPESGEdllslspiPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLATAR----IKPAVNQ 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 143 AEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkyGNGVPESSRASLKCYQWLKERIVSEegrkqqnklkdlsp 222
Cdd:cd19123   181 VELHPYLQQP---ELLAFCRDNGIHLTAYSPL---------GSGDRPAAMKAEGEPVLLEDPVINK-------------- 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034635487 223 IAERLGCTLPQLAVAWCL-RNegvSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKPY 288
Cdd:cd19123   235 IAEKHGASPAQVLIAWAIqRG---TVVIPKSVNPERIQQNLEAAEV--ELDASDMATIAALDRHHRY 296
AKR_AKR5F1 cd19133
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ...
4-262 2.97e-14

the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).


Pssm-ID: 381359 [Multi-domain]  Cd Length: 255  Bit Score: 71.07  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19133    32 AIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKL-WIQDAGYEK------AKKAFERSLKRLGLDYLDLY 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNTP-----MEEIVRAmthvinqGMAMYWGTSRWSAMEIMEAYSvarqFNMIPPVCEQAEYHLFQREKVEVqlp 158
Cdd:cd19133   102 LIHQPFGDVYgawraMEELYKE-------GKIRAIGVSNFYPDRLVDLIL----HNEVKPAVNQIETHPFNQQIEAV--- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 159 ELYHKIGVGAMTWSPLAcgiisgkygngvpessraslkcyqwlkerivseEGRKQ--QNKLkdLSPIAERLGCTLPQLAV 236
Cdd:cd19133   168 EFLKKYGVQIEAWGPFA---------------------------------EGRNNlfENPV--LTEIAEKYGKSVAQVIL 212
                         250       260
                  ....*....|....*....|....*.
gi 1034635487 237 AWcLRNEGVsSVLLGSSTPEQLIENL 262
Cdd:cd19133   213 RW-LIQRGI-VVIPKSVRPERIAENF 236
PLN02587 PLN02587
L-galactose dehydrogenase
4-283 3.38e-14

L-galactose dehydrogenase


Pssm-ID: 178198 [Multi-domain]  Cd Length: 314  Bit Score: 71.35  E-value: 3.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLywgGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:PLN02587   40 AFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVSTKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDIL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANR---PDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSaMEIMEaYSVARqfnmIPP-----VCEQAEYHLFQREKVEV 155
Cdd:PLN02587  117 HCHDiefGSLDQIVNETIPALQKLKESGKVRFIGITGLP-LAIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 156 qLPELYHKiGVGAMTWSPLACGIISgkyGNGVPESSRASLKcyqwLKE--RIVSEEGRKQqnklkdlspiaerlGCTLPQ 233
Cdd:PLN02587  191 -LPYLKSK-GVGVISASPLAMGLLT---ENGPPEWHPAPPE----LKSacAAAATHCKEK--------------GKNISK 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034635487 234 LAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPK--MTSHVVNEIDNIL 283
Cdd:PLN02587  248 LALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETsgIDEELLSEVEAIL 299
AKR_GlAR-like cd19128
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ...
3-262 2.20e-13

Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.


Pssm-ID: 381354 [Multi-domain]  Cd Length: 277  Bit Score: 68.70  E-value: 2.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   3 IAYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLE 78
Cdd:cd19128    22 NAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQPEN------VKEQLLITLQDLQLE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  79 YVDVVFANRP-------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 139
Cdd:cd19128    92 YLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNYCK----IKPF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 140 CEQAEYHL-FQREKVeVQLPeLYHKIGVGAmtWSPLAcgiisGKYGNGvpesSRASLKCyqwlkerivseegrkqqnklK 218
Cdd:cd19128   168 MNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYGDG----NLTFLND--------------------S 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034635487 219 DLSPIAERLGCTLPQLAVAWCL-RNEGVSSVLLGSSTPEQLIENL 262
Cdd:cd19128   215 ELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
AKR_AKR5C2 cd19131
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ...
4-262 5.47e-13

Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.


Pssm-ID: 381357 [Multi-domain]  Cd Length: 256  Bit Score: 67.40  E-value: 5.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLsrkhiiEGLKGSLQRLQLEYVDVV 83
Cdd:cd19131    32 ALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL------RAFDESLRKLGLDYVDLY 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPdsnTPME----EIVRAMTHVINQGMAMYWGTSRWSA---MEIMEAYSVArqfnmipPVCEQAEYH-LFQREkvev 155
Cdd:cd19131   102 LIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIehlQRLIDETGVV-------PVVNQIELHpRFQQR---- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 156 QLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLA 235
Cdd:cd19131   168 ELRAFHAKHGIQTESWSPLGQG---------------------GLLSDPVIGE--------------IAEKHGKTPAQVV 212
                         250       260
                  ....*....|....*....|....*..
gi 1034635487 236 VAWCLRNEGVssVLLGSSTPEQLIENL 262
Cdd:cd19131   213 IRWHLQNGLV--VIPKSVTPSRIAENF 237
AKR_CeZK1290-like cd19135
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ...
6-261 5.57e-13

Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.


Pssm-ID: 381361 [Multi-domain]  Cd Length: 265  Bit Score: 67.35  E-value: 5.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   6 ESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLEYVDVVFA 85
Cdd:cd19135    37 ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKL-WPSDYGYES------TKQAFEASLKRLGVDYLDLYLL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  86 NRPDSNTP-------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEaysvARQFNMIPPVCEQAEYHLFQREKvevQLP 158
Cdd:cd19135   107 HWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQ----LLEDCSVVPHVNQVEFHPFQNPV---ELI 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 159 ELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAW 238
Cdd:cd19135   180 EYCRDNNIVFEGYCPLAKG---------------------KALEEPTVTE--------------LAKKYQKTPAQILIRW 224
                         250       260
                  ....*....|....*....|...
gi 1034635487 239 CLRNEGVssVLLGSSTPEQLIEN 261
Cdd:cd19135   225 SIQNGVV--TIPKSTKEERIKEN 245
AKR_AKR4A_4B cd19124
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ...
4-262 9.26e-13

AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.


Pssm-ID: 381350 [Multi-domain]  Cd Length: 281  Bit Score: 66.91  E-value: 9.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAgkaEVILGSIIK---KKG--WRRSSLVITTKLyWGGKAEterglsRKHIIEGLKGSLQRLQLE 78
Cdd:cd19124    29 AIEVGYRHFDTAAAYGT---EEALGEALAealRLGlvKSRDELFVTSKL-WCSDAH------PDLVLPALKKSLRNLQLE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  79 YVDVVFANRPDSNTP----------------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQ 142
Cdd:cd19124    99 YVDLYLIHWPVSLKPgkfsfpieeedflpfdIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSFAT----IPPAVNQ 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 143 AEYH-LFQREKvevqLPELYHKIGVGAMTWSPLacGIISGKYG-NGVPESsraslkcyQWLKErivseegrkqqnklkdl 220
Cdd:cd19124   175 VEMNpAWQQKK----LREFCKANGIHVTAYSPL--GAPGTKWGsNAVMES--------DVLKE----------------- 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034635487 221 spIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENL 262
Cdd:cd19124   224 --IAAAKGKTVAQVSLRW-VYEQGV-SLVVKSFNKERMKQNL 261
AKR_AKR2E1-5 cd19116
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ...
4-285 1.71e-12

AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.


Pssm-ID: 381342 [Multi-domain]  Cd Length: 292  Bit Score: 66.15  E-value: 1.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGGKAEterglsRKHIIEGLKGSLQRLQLEY 79
Cdd:cd19116    34 AIEAGYRHIDTAYLY---GNEAEVGEAIREKiaegVVKREDLFITTKL-WNSYHE------REQVEPALRESLKRLGLDY 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  80 VDVVFANRP-------DSNTPME---------EIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQA 143
Cdd:cd19116   104 VDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNCN----IKPAVNQI 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 144 EYHL-FQREKvevqLPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASLkcyqwlkerivsEEGRKQQNKLKDlsp 222
Cdd:cd19116   180 EVHPtLTQEK----LVAYCQSNGIVVMAYSPF-----------GRLVPRGQTN------------PPPRLDDPTLVA--- 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034635487 223 IAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENlgaIQVLP-KMTSHVVNEIDNILRN 285
Cdd:cd19116   230 IAKKYGKTTAQIVLRY-LIDRGV-VPIPKSSNKKRIKEN---IDIFDfQLTPEEVAALNSFNTN 288
AKR_AKR1G1_1I cd19111
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ...
4-288 1.93e-12

Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.


Pssm-ID: 381337 [Multi-domain]  Cd Length: 286  Bit Score: 65.98  E-value: 1.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQL 77
Cdd:cd19111    26 ALFVGYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKLP-------PVYLEFKDTEKSLEKSLENLKL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  78 EYVDVVFAN-------------RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAE 144
Cdd:cd19111    94 PYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK----VKPSNLQLE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 145 YHLF--QREKVEVQLPelyHKIGVGAmtWSPLacgiisgkygnGVPesSRASLkcYQWLKERIVSEEgrkqQNKLKdlsp 222
Cdd:cd19111   170 CHAYlqQRELRKFCNK---KNIVVTA--YAPL-----------GSP--GRANQ--SLWPDQPDLLED----PTVLA---- 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034635487 223 IAERLGCTLPQLAVAWCL-RNEGvssVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKPY 288
Cdd:cd19111   222 IAKELDKTPAQVLLRFVLqRGTG---VLPKSTNKERIEENFEVFDF--ELTEEHFKKLKTLDRNMKY 283
AKR_AKR15A1 cd19161
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ...
4-270 3.83e-12

Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.


Pssm-ID: 381387 [Multi-domain]  Cd Length: 310  Bit Score: 65.42  E-value: 3.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKLywgGK----AETERGL-----------------SRK 62
Cdd:cd19161    29 AWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRllkpAREGSVPdpngfvdplpfeivydySYD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  63 HIIEGLKGSLQRLQLEYVDVVF---------ANRPDSN---TPMEEIVRAMTHVINQGM--AMYWGTSRWSAM-EIMEAY 127
Cdd:cd19161   104 GIMRSFEDSLQRLGLNRIDILYvhdigvythGDRKERHhfaQLMSGGFKALEELKKAGVikAFGLGVNEVQIClEALDEA 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 128 SVarQFNMIppvceQAEYHLFQREKVEVQLPELyHKIGVGAmtwsplacgIISGKYGNGVPESSRASLKCYQWlkeRIVS 207
Cdd:cd19161   184 DL--DCFLL-----AGRYSLLDQSAEEEFLPRC-EQRGTSL---------VIGGVFNSGILATGTKSGAKFNY---GDAP 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034635487 208 EEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ-VLPK 270
Cdd:cd19161   244 AE---IISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQtDIPE 304
AKR_AKR3F2 cd19139
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ...
4-267 7.19e-12

Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).


Pssm-ID: 381365 [Multi-domain]  Cd Length: 248  Bit Score: 63.91  E-value: 7.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWggkaeteRGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19139    23 ALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNLSKDKLLPSLEESLEKLRTDYVDLT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYhlFQREKVEVQLPEly 161
Cdd:cd19139    93 LIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIELSPY--LQNRKLVAHCKQ-- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAmtWSPLAcgiisgkygngvpessraslkcyqwlkerivseEGRKQQNKLkdLSPIAERLGCTLPQLAVAWCLr 241
Cdd:cd19139   169 HGIHVTS--YMTLA---------------------------------YGKVLDDPV--LAAIAERHGATPAQIALAWAM- 210
                         250       260
                  ....*....|....*....|....*.
gi 1034635487 242 NEGVsSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19139   211 ARGY-AVIPSSTKREHLRSNLLALDL 235
AKR_AKR4C1-15 cd19125
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ...
13-262 1.16e-11

AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.


Pssm-ID: 381351 [Multi-domain]  Cd Length: 287  Bit Score: 63.90  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  13 DTAEVYAAGKaEV--ILGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLEYVDVV-----FA 85
Cdd:cd19125    42 DCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKL-WCTDHAPED------VPPALEKTLKDLQLDYLDLYlihwpVR 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  86 NRPDSNTP---------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQ 156
Cdd:cd19125   114 LKKGAHMPepeevlppdIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---K 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 157 LPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASLKCyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAV 236
Cdd:cd19125   187 LHEFCKSKGIHLSAYSPL-----------GSPGTTWVKKNV---LKDPIVTK--------------VAEKLGKTPAQVAL 238
                         250       260
                  ....*....|....*....|....*.
gi 1034635487 237 AWCLRnEGvSSVLLGSSTPEQLIENL 262
Cdd:cd19125   239 RWGLQ-RG-TSVLPKSTNEERIKENI 262
AKR_DrGR-like cd19136
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ...
4-262 7.34e-11

Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).


Pssm-ID: 381362 [Multi-domain]  Cd Length: 262  Bit Score: 61.11  E-value: 7.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIK----KKGWRRSSLVITTKL--YWGGKAETErglsrkhiiEGLKGSLQRLQL 77
Cdd:cd19136    24 ALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKLapKDQGYEKAR---------AACLGSLERLGT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  78 EYVDVVFANRP-----DSNTPMEEIVR-----AMTHVINQGMAMYWGTSRW--SAMEIMEAYSvarqfnMIPPVCEQAEY 145
Cdd:cd19136    92 DYLDLYLIHWPgvqglKPSDPRNAELRreswrALEDLYKEGKLRAIGVSNYtvRHLEELLKYC------EVPPAVNQVEF 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 146 H--LFQREkvevqLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkCYQWLKERIVSEegrkqqnklkdlspI 223
Cdd:cd19136   166 HphLVQKE-----LLKFCKDHGIHLQAYSSLGSG-------------------DLRLLEDPTVLA--------------I 207
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034635487 224 AERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 262
Cdd:cd19136   208 AKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENI 244
AKR_AKR5H1 cd19134
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ...
4-262 9.75e-11

AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.


Pssm-ID: 381360 [Multi-domain]  Cd Length: 263  Bit Score: 61.03  E-value: 9.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAgkaEVILGSIIKKKGWRRSSLVITTKLywggkAETERGLSRKhiIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19134    33 ALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKL-----ATPDQGFTAS--QAACRASLERLGLDYVDLY 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNT-PMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnMIPPVCEQAEYH--LFQREkvevqLPEL 160
Cdd:cd19134   103 LIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----FFTPAVNQIELHplLNQAE-----LRKV 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKygngvPESSRaslkcyqwlkerivseegrkqqnklkdlspIAERLGCTLPQLAVAWCL 240
Cdd:cd19134   174 NAQHGIVTQAYSPLGVGRLLDN-----PAVTA------------------------------IAAAHGRTPAQVLLRWSL 218
                         250       260
                  ....*....|....*....|..
gi 1034635487 241 RNEGVssVLLGSSTPEQLIENL 262
Cdd:cd19134   219 QLGNV--VISRSSNPERIASNL 238
AKR_ARA2 cd19164
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ...
2-84 1.11e-10

D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).


Pssm-ID: 381390 [Multi-domain]  Cd Length: 298  Bit Score: 61.14  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   2 TIAYESGVNLFDTAEVYaaGKAEVILGSIIKK--KGWRRSSLVITTKLywGGKAETERGLSRKHIIEGLKGSLQRLQLEY 79
Cdd:cd19164    41 RRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIITKV--GRYGPDDFDYSPEWIRASVERSLRRLHTDY 116

                  ....*
gi 1034635487  80 VDVVF 84
Cdd:cd19164   117 LDLVY 121
AKR_AKR5A_5G cd19126
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ...
4-184 1.13e-10

AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.


Pssm-ID: 381352 [Multi-domain]  Cd Length: 254  Bit Score: 60.53  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLSrkhiieGLKGSLQRLQLEYVDVV 83
Cdd:cd19126    32 ALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQRARRTED------AFQESLDRLGLDYVDLY 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNTpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH-LFQREKVEVQLPElyH 162
Cdd:cd19126   102 LIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD----VVPAVNQVEFHpYLTQKELRGYCKS--K 174
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034635487 163 KIGVGAmtWSPLACGI---------ISGKYG 184
Cdd:cd19126   175 GIVVEA--WSPLGQGGllsnpvlaaIGEKYG 203
dkgB PRK11172
2,5-didehydrogluconate reductase DkgB;
4-264 1.25e-10

2,5-didehydrogluconate reductase DkgB;


Pssm-ID: 183012 [Multi-domain]  Cd Length: 267  Bit Score: 60.81  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLyWggkaeTERgLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:PRK11172   25 ALELGYRAIDTAQIYD-NEAAV--GQAIAESGVPRDELFITTKI-W-----IDN-LAKDKLIPSLKESLQKLRTDYVDLT 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWS------AMEIMEAYSVARQfnmippvceQAEYH-LFQREKVE 154
Cdd:PRK11172   95 LIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTialmkqAIAAVGAENIATN---------QIELSpYLQNRKVV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 155 VQLPElyHKIGVGA-MTwspLAcgiisgkYGngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQ 233
Cdd:PRK11172  166 AFAKE--HGIHVTSyMT---LA-------YG--------------KVLKDPVIAR--------------IAAKHNATPAQ 205
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034635487 234 LAVAWCLRnEGvSSVLLGSSTPEQLIENLGA 264
Cdd:PRK11172  206 VILAWAMQ-LG-YSVIPSSTKRENLASNLLA 234
AKR_unchar cd19100
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
4-262 1.51e-10

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381326 [Multi-domain]  Cd Length: 238  Bit Score: 60.19  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVITTKLYWGGKAETERGLSRkhiieglkgSLQRLQLEYVDVV 83
Cdd:cd19100    36 ALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATKTGARDYEGAKRDLER---------SLKRLGTDYIDLY 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 F----ANRPDSNTPMEE--IVRAMTHVINQGMAMYWGTS--RWSAM-EIMEAYsvarQFNMIPPVCEQAEYHlfQREKVE 154
Cdd:cd19100   102 QlhavDTEEDLDQVFGPggALEALLEAKEEGKIRFIGISghSPEVLlRALETG----EFDVVLFPINPAGDH--IDSFRE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 155 VQLPELY-HKIGVGAMtwSPLACGiisgkygngvpessraslkcyQWLKERIVSeegrkqqnklkdlspiaerlgctlPQ 233
Cdd:cd19100   176 ELLPLAReKGVGVIAM--KVLAGG---------------------RLLSGDPLD------------------------PE 208
                         250       260
                  ....*....|....*....|....*....
gi 1034635487 234 LAVAWCLRNEGVSSVLLGSSTPEQLIENL 262
Cdd:cd19100   209 QALRYALSLPPVDVVIVGMDSPEELDENL 237
AKR_AKR9A3_9B1-4 cd19147
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ...
5-280 3.16e-10

Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.


Pssm-ID: 381373 [Multi-domain]  Cd Length: 319  Bit Score: 59.84  E-value: 3.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   5 YESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKLYW--------GGKAETERGLSRKHIIEGLKGSLQRLQ 76
Cdd:cd19147    44 YEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATKFTTdykayevgKGKAVNYCGNHKRSLHVSVRDSLRKLQ 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  77 LEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQ 156
Cdd:cd19147   123 TDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDI 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 157 LPELYHkIGVGAMTWSPLacgiisgkyGNGVPESSRAslkcyqwLKERIVSEEGRK------QQNKL-----KDLSPIAE 225
Cdd:cd19147   203 IPMARH-FGMALAPWDVL---------GGGKFQSKKA-------VEERKKNGEGLRsfvggtEQTPEevkisEALEKVAE 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034635487 226 RLGC-TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 280
Cdd:cd19147   266 EHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSI--KLTPEEIEYLE 319
AKR_BaDH-like cd19129
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ...
4-279 4.16e-10

Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.


Pssm-ID: 381355 [Multi-domain]  Cd Length: 295  Bit Score: 59.39  E-value: 4.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLEY 79
Cdd:cd19129    28 ALEAGFRHFDCAERYrneaEVGEA---MQEVFKAGKIRREDLFVTTKL-WNTNHRPER------VKPAFEASLKRLQLDY 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  80 VDVV-----FANRP---------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 139
Cdd:cd19129    98 LDLYlihtpFAFQPgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIFEAAR----IKPA 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 140 CEQAEYHLFQRekvEVQLPELYHKIGVGAMTWSPLACGIisgkygngvpessraslkcyqwlkerivseegrkQQNKLKD 219
Cdd:cd19129   174 VVQVESHPYLP---EWELLDFCKNHGIVLQAFAPLGHGM----------------------------------EPKLLED 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034635487 220 --LSPIAERLGCTLPQLAVAWCLRNEGvsSVLLGSSTPEQLIENLGaIQVLPKMTSHVVNEI 279
Cdd:cd19129   217 pvITAIARRVNKTPAQVLLAWAIQRGT--ALLTTSKTPSRIRENFD-ISTLPEDAMREINEG 275
AKR_AKR5B1 cd19127
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ...
2-262 4.42e-10

AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.


Pssm-ID: 381353 [Multi-domain]  Cd Length: 268  Bit Score: 58.96  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   2 TIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWG--GKAETERGLSRkhiieglkgSLQRLQLEY 79
Cdd:cd19127    29 ATALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyGYDKALRGFDA---------SLRRLGLDY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  80 VDVVFANRPdsnTPME-----EIVRAMTHVINQGMAMYWGTSRWSA---MEIMEAYSVarqfnmIPPVcEQAEYHLFQRE 151
Cdd:cd19127    97 VDLYLLHWP---VPNDfdrtiQAYKALEKLLAEGRVRAIGVSNFTPehlERLIDATTV------VPAV-NQVELHPYFSQ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 152 KvevQLPELYHKIGVGAMTWSPLAcGIIsgKYGNGVPESSRASLKCYQwlkerivseegrkqqnklkdLSPIAERLGCTL 231
Cdd:cd19127   167 K---DLRAFHRRLGIVTQAWSPIG-GVM--RYGASGPTGPGDVLQDPT--------------------ITGLAEKYGKTP 220
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034635487 232 PQLAVAWCLRNeGVSSVlLGSSTPEQLIENL 262
Cdd:cd19127   221 AQIVLRWHLQN-GVSAI-PKSVHPERIAENI 249
AKR_AKR1I_CgAKR1 cd19155
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ...
4-262 6.22e-10

Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.


Pssm-ID: 381381 [Multi-domain]  Cd Length: 307  Bit Score: 59.08  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGKAeviLGSIIKKkgW------RRSSLVITTKLYWGGkaeterglSRKHIIEG-LKGSLQRLQ 76
Cdd:cd19155    34 ALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKLPPGG--------NRREKVEKfLLKSLEKLQ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  77 LEYVDVVFANRP---------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnm 135
Cdd:cd19155   101 LDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARILKNAR---- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 136 IPPVCEQAEYHLFQREKVEVQLPElYHKIGVGAmtWSPLAC-GIISGKYGNGVPESSRASLkcyqwLKERIVSEegrkqq 214
Cdd:cd19155   177 IKPANLQVELHVYLQQKDLVDFCS-THSITVTA--YAPLGSpGAAHFSPGTGSPSGSSPDL-----LQDPVVKA------ 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034635487 215 nklkdlspIAERLGCTLPQLAVAWCLrNEGVsSVLLGSSTPEQLIENL 262
Cdd:cd19155   243 --------IAERHGKSPAQVLLRWLM-QRGV-VVIPKSTNAARIKENF 280
AKR_AKR2A1-2 cd19112
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ...
4-262 2.21e-09

AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.


Pssm-ID: 381338 [Multi-domain]  Cd Length: 308  Bit Score: 57.50  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIK---KKGW-RRSSLVITTKLYwggkaETERGlsrkHIIEGLKGSLQRLQLEY 79
Cdd:cd19112    33 AIKIGYRHFDCAADY---KNEKEVGEALAeafKTGLvKREDLFITTKLW-----NSDHG----HVIEACKDSLKKLQLDY 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  80 VDVVFANRP-----------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA--MEIMEAYSvarqfn 134
Cdd:cd19112   101 LDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLVSAGLVRSIGISNYDIflTRDCLAYS------ 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 135 MIPPVCEQAEYH-LFQREKVeVQLPeLYHKIGVGAMTwsPLACGIISGKYGNGVpessraslkcyqwlkerivseegrkq 213
Cdd:cd19112   175 KIKPAVNQIETHpYFQRDSL-VKFC-QKHGISVTAHT--PLGGAAANAEWFGSV-------------------------- 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034635487 214 qNKLKD--LSPIAERLGCTLPQLAVAWCL-RNegvSSVLLGSSTPEQLIENL 262
Cdd:cd19112   225 -SPLDDpvLKDLAKKYGKSAAQIVLRWGIqRN---TAVIPKSSKPERLKENI 272
AKR_AKR5D1_E1 cd19132
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ...
1-262 2.82e-09

AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).


Pssm-ID: 381358 [Multi-domain]  Cd Length: 255  Bit Score: 56.51  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   1 MTIAYESGVNLFDTAEVYAAgkaEVILGSIIKKKGWRRSSLVITTKLywggkaeteRGlsRKH----IIEGLKGSLQRLQ 76
Cdd:cd19132    26 VVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL---------PG--RHHgyeeALRTIEESLYRLG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  77 LEYVDVVFANRPD-SNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM---EIMEAYSVArqfnmipPVCEQAEYH-LFQRE 151
Cdd:cd19132    92 LDYVDLYLIHWPNpSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEhldRLIDETGVT-------PAVNQIELHpYFPQA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 152 KVEVqlpelYHK-IGVGAMTWSPLacgiisGKyGNGVpessraslkcyqwLKERIVSEegrkqqnklkdlspIAERLGCT 230
Cdd:cd19132   165 EQRA-----YHReHGIVTQSWSPL------GR-GSGL-------------LDEPVIKA--------------IAEKHGKT 205
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034635487 231 LPQLAVAWCLRnEGVsSVLLGSSTPEQLIENL 262
Cdd:cd19132   206 PAQVVLRWHVQ-LGV-VPIPKSANPERQRENL 235
dkgA PRK11565
2,5-didehydrogluconate reductase DkgA;
4-187 3.06e-09

2,5-didehydrogluconate reductase DkgA;


Pssm-ID: 183203 [Multi-domain]  Cd Length: 275  Bit Score: 56.62  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKaeterglsRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:PRK11565   37 ALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD--------HKRPREALEESLKKLQLDYVDLY 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSntPMEEIVRAMTHVIN---QGMAMYWGTSRWSA---MEIMEAYSVArqfnmipPVCEQAEYH-LFQREkvEVQ 156
Cdd:PRK11565  105 LMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIhhlQRLIDETGVT-------PVINQIELHpLMQQR--QLH 173
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034635487 157 LPELYHKIGVGAmtWSPLACGiisgkyGNGV 187
Cdd:PRK11565  174 AWNATHKIQTES--WSPLAQG------GKGV 196
AKR_AKR5A1_2 cd19156
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ...
4-184 6.41e-09

AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.


Pssm-ID: 381382 [Multi-domain]  Cd Length: 266  Bit Score: 55.60  E-value: 6.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLSrkhiieGLKGSLQRLQLEYVDVV 83
Cdd:cd19156    32 AIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSDQGYESTLA------AFEESLEKLGLDYVDLY 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPDSNTpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH-LFQREKVEVQLPElyH 162
Cdd:cd19156   102 LIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK----VAPMVNQIELHpLLTQEPLRKFCKE--K 174
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034635487 163 KIGVGAmtWSPLACG---------IISGKYG 184
Cdd:cd19156   175 NIAVEA--WSPLGQGkllsnpvlkAIGKKYG 203
AKR_AKR3E1 cd19122
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ...
37-267 2.26e-08

AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.


Pssm-ID: 381348 [Multi-domain]  Cd Length: 291  Bit Score: 54.17  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  37 RRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRLQLEYVDV------VFANRPDSNTPM---------------- 94
Cdd:cd19122    68 KREDLFICTKV-WNHLHEPE------DVKWSIDNSLKNLKLDYIDLflvhwpIAAEKNDQRSPKlgpdgkyvilkdlten 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  95 -EEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSP 173
Cdd:cd19122   141 pEPTWRAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSP 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 174 LACGiisgkygNGVPESSraslkcyqwlkERIvseegrkqqNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSS 253
Cdd:cd19122   214 LGSQ-------NQVPSTG-----------ERV---------SENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSS 264
                         250
                  ....*....|....
gi 1034635487 254 TPEQLIENLGAIQV 267
Cdd:cd19122   265 TPSRIESNFKSIEL 278
AKR_AKR1A1-4 cd19106
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ...
4-285 8.89e-08

AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.


Pssm-ID: 381332 [Multi-domain]  Cd Length: 305  Bit Score: 52.39  E-value: 8.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAaGKAEVilGSIIKK-----KGWRRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRLQLE 78
Cdd:cd19106    29 ALDAGYRHIDCAAVYG-NEQEV--GEALKEkvgpgKAVPREDLFVTSKL-WNTKHHPE------DVEPALRKTLKDLQLD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  79 YVDV--------------VFANRPD-----SNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 139
Cdd:cd19106    99 YLDLylihwpyafergdnPFPKNPDgtiryDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVAR----IKPA 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 140 CEQAEYHLFQrekVEVQLPELYHKIGVGAMTWSPLacgiisgkygnGVPEssRAslkcyqWLK--ERIVSEEGRkqqnkl 217
Cdd:cd19106   175 VLQVECHPYL---AQNELIAHCKARGLVVTAYSPL-----------GSPD--RP------WAKpdEPVLLEEPK------ 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034635487 218 kdLSPIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENlgaIQVLP-KMTSHVVNEIDNILRN 285
Cdd:cd19106   227 --VKALAKKYNKSPAQILLRW-QVQRGV-VVIPKSVTPSRIKQN---IQVFDfTLSPEEMKQLDALNRN 288
AKR_AKR5G1-3 cd19157
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ...
4-263 1.85e-07

AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.


Pssm-ID: 381383 [Multi-domain]  Cd Length: 265  Bit Score: 51.24  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLsrkhiiEGLKGSLQRLQLEYVDVV 83
Cdd:cd19157    33 ALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNADQGYDSTL------KAFEASLERLGLDYLDLY 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  84 FANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREkvevqLPELY 161
Cdd:cd19157   103 LIHWP-VKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE----IVPMVNQVEFHprLTQKE-----LRDYC 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLR 241
Cdd:cd19157   173 KKQGIQLEAWSPLMQG---------------------QLLDNPVLKE--------------IAEKYNKSVAQVILRWDLQ 217
                         250       260
                  ....*....|....*....|..
gi 1034635487 242 NEGVssVLLGSSTPEQLIENLG 263
Cdd:cd19157   218 NGVV--TIPKSIKEHRIIENAD 237
AKR_AKR3A1-2 cd19117
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ...
3-282 8.35e-07

AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.


Pssm-ID: 381343 [Multi-domain]  Cd Length: 284  Bit Score: 49.42  E-value: 8.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   3 IAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLyWGgkaeTERglsrKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd19117    35 AALKAGYRHIDTAAIYG-NEEEV--GQGIKDSGVPREEIFITTKL-WC----TWH----RRVEEALDQSLKKLGLDYVDL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  83 VFANRP-------DSNTPMEEIVRA--------------MTHVINQGMAMYWGTSRWSAMEIMEAysVARQFNMIPPVCE 141
Cdd:cd19117   103 YLMHWPvpldpdgNDFLFKKDDGTKdhepdwdfiktwelMQKLPATGKVKAIGVSNFSIKNLEKL--LASPSAKIVPAVN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 142 QAEYHLFQREKvevQLPELYHKIGVGAMTWSPLAcgiisgkygngvpeSSRASLkcyqwLKERIVSEegrkqqnklkdls 221
Cdd:cd19117   181 QIELHPLLPQP---KLVDFCKSKGIHATAYSPLG--------------STNAPL-----LKEPVIIK------------- 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034635487 222 pIAERLGCTLPQLAVAWCLRnEGVsSVLLGSSTPEQLIENLGAIQvlpkMTSHVVNEIDNI 282
Cdd:cd19117   226 -IAKKHGKTPAQVIISWGLQ-RGY-SVLPKSVTPSRIESNFKLFT----LSDEEFKEIDEL 279
PRK10376 PRK10376
putative oxidoreductase; Provisional
4-282 1.17e-06

putative oxidoreductase; Provisional


Pssm-ID: 236676 [Multi-domain]  Cd Length: 290  Bit Score: 48.81  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAGkaevILGSIIkkkgwR------RSSLVITTKLywgGKAETERG-----LSRKHIIEGLKGSL 72
Cdd:PRK10376   49 AVALGVNHIDTSDFYGPH----VTNQLI-----RealhpyPDDLTIVTKV---GARRGEDGswlpaFSPAELRRAVHDNL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  73 QRLQLEYVDVV------FANRPDSNtPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYH 146
Cdd:PRK10376  117 RNLGLDVLDVVnlrlmgDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA------EIVCVQNHYN 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 147 LFQREkvEVQLPELYHKIGVGAMTWSPLacgiisgkyGNGVPESSRAslkcyqwlkerivseegrkqqnklkdLSPIAER 226
Cdd:PRK10376  190 LAHRA--DDALIDALARDGIAYVPFFPL---------GGFTPLQSST--------------------------LSDVAAS 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034635487 227 LGCTLPQLAVAWCLRNEgvSSVLL--GSSTPEQLIENLGAIQ-VLPkmtSHVVNEIDNI 282
Cdd:PRK10376  233 LGATPMQVALAWLLQRS--PNILLipGTSSVAHLRENLAAAElVLS---EEVLAELDGI 286
AKR_unchar cd19098
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
4-267 2.05e-06

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381324 [Multi-domain]  Cd Length: 318  Bit Score: 48.49  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSLVITTKlyWG----------GKAETERGLSRKHIIEGLKGSLQ 73
Cdd:cd19098    44 AWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadwqvdAAVHEVKDHSLARLLKQWEETRS 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  74 RLQlEYVDV-----------VFANrpdsntpmEEIVRAMTHVINQGMAMYWGTSRWS-------AMEImeAYSVARQFNm 135
Cdd:cd19098   120 LLG-KHLDLyqihsatlesgVLED--------ADVLAALAELKAEGVKIGLSLSGPQqaetlrrALEI--EIDGARLFD- 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 136 ippvCEQAEYHLFQREKVEvQLpELYHKIGVGAmtwsplacgIISGKYGNGvpessRaslkcyqwLKERIVSEEGRKqqn 215
Cdd:cd19098   188 ----SVQATWNLLEQSAGE-AL-EEAHEAGMGV---------IVKEALANG-----R--------LTDRNPSPELAP--- 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034635487 216 KLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19098   237 LMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
AKR_AKR2D1 cd19115
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ...
4-154 3.73e-05

AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.


Pssm-ID: 381341 [Multi-domain]  Cd Length: 311  Bit Score: 44.33  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYA----AGK--AEVILGSIIKkkgwrRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRLQL 77
Cdd:cd19115    35 AIKAGYRLFDGACDYGneveAGQgvARAIKEGIVK-----REDLFIVSKL-WNTFHDGE------RVEPICRKQLADWGI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  78 EYVDVVFANRP------------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 133
Cdd:cd19115   103 DYFDLFLIHFPialkyvdpavryppgwfydgkkveFSNAPIQETWTAMEKLVDKGLARSIGVSNFSAQLLMDLLRYAR-- 180
                         170       180
                  ....*....|....*....|...
gi 1034635487 134 nmIPPVCEQAEYH--LFQREKVE 154
Cdd:cd19115   181 --IRPATLQIEHHpyLTQPRLVK 201
AKR_AKR1C1-35 cd19108
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ...
3-148 1.04e-04

AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.


Pssm-ID: 381334 [Multi-domain]  Cd Length: 303  Bit Score: 42.99  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   3 IAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGGKAETErgLSRKhiieGLKGSLQRLQLE 78
Cdd:cd19108    35 LAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WCTFHRPE--LVRP----ALEKSLKKLQLD 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  79 YVDVVFANRPDSNTPMEEIVRAMTHvinqGMAMYWGT---SRWSAME------IMEAYSVA----RQFNMI---P----- 137
Cdd:cd19108   105 YVDLYLIHFPVALKPGEELFPKDEN----GKLIFDTVdlcATWEAMEkckdagLAKSIGVSnfnrRQLEMIlnkPglkyk 180
                         170
                  ....*....|.
gi 1034635487 138 PVCEQAEYHLF 148
Cdd:cd19108   181 PVCNQVECHPY 191
AKR_AKR2C1 cd19114
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ...
4-152 1.20e-03

AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.


Pssm-ID: 381340 [Multi-domain]  Cd Length: 302  Bit Score: 39.85  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487   4 AYESGVNLFDTAEVYAAgkaEVILGSIIKK---KGW-RRSSLVITTKLyWGGKAeterglSRKHIIEGLKGSLQRLQLEY 79
Cdd:cd19114    26 AIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-WNNFH------GKDHVREAFDRQLKDYGLDY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487  80 VDVVFANRPDS-------------------------NTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfn 134
Cdd:cd19114    96 IDLYLIHFPIPaayvdpaenypflwkdkelkkfpleQSPMQECWREMEKLVDAGLVRNIGIANFNVQLILDLLTYAK--- 172
                         170
                  ....*....|....*....
gi 1034635487 135 mIPPVCEQAEYHLF-QREK 152
Cdd:cd19114   173 -IKPAVLQIEHHPYlQQKR 190
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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