|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
60-360 |
6.57e-166 |
|
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: 465.55 E-value: 6.57e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 60 VTKLGIGAWSWGDTTYWNefqWDDRKLKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQKEqvEV 139
Cdd:cd19093 2 VSPLGLGTWQWGDRLWWG---YGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTG-----RSERLLGRFLKELGDRD--EV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 140 AIATKFAALPWRLGRGSVISALKDSLSRLGVSSVELYQLHWPGIWG--NEGYLDGLGDAYEQGLVKAVGVSNYSEKRLRD 217
Cdd:cd19093 72 VIATKFAPLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYsqIEALMDGLADAVEEGLVRAVGVSNYSADQLRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 218 AYERLKKRGVPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGKYTPNNPPTGPRGRIYTPEFLTKLQ 297
Cdd:cd19093 152 AHKALKERGVPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKNLEKVQ 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002286311 298 PLINRIKEIGGSYEKTPTQVVLNWLICQGnVVPIPGAKNAEQAREFAGALGWSLTDQEVEELR 360
Cdd:cd19093 232 PLLDALEEIAEKYGKTPAQVALNWLIAKG-VVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
50-368 |
4.38e-88 |
|
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: 268.59 E-value: 4.38e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 50 KVRLGGSDVAVTKLGIGAWSWGDTtywnefqWDDRKLKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIK 129
Cdd:COG0667 3 YRRLGRSGLKVSRLGLGTMTFGGP-------WGGVDEAEAIAILDAALDAGINFFDTADVYGPG-----RSEELLGEALK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 130 ERQQKEqveVAIATKFA------ALPWRLGRGSVISALKDSLSRLGVSSVELYQLHWPGI-WGNEGYLDGLGDAYEQGLV 202
Cdd:COG0667 71 GRPRDD---VVIATKVGrrmgpgPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPdTPIEETLGALDELVREGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 203 KAVGVSNYSEKRLRDAYERLKKRgVPLASNQVNYSLIYRNPEEnGVKAACDELGITLIAYSPIAQGVLTGKYTPNNP-PT 281
Cdd:COG0667 148 RYIGVSNYSAEQLRRALAIAEGL-PPIVAVQNEYSLLDRSAEE-ELLPAARELGVGVLAYSPLAGGLLTGKYRRGATfPE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 282 GPRGRIY--TPEFLTKLQPLINRIKEIGGSYEKTPTQVVLNWLICQGNV-VPIPGAKNAEQAREFAGALGWSLTDQEVEE 358
Cdd:COG0667 226 GDRAATNfvQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVtSVIPGARSPEQLEENLAAADLELSAEDLAA 305
|
330
....*....|
gi 1002286311 359 LRSMAREIKP 368
Cdd:COG0667 306 LDAALAAVPA 315
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
57-360 |
1.77e-76 |
|
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: 238.19 E-value: 1.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 57 DVAVTKLGIGAWSWGDTtYWNEFQWDD--RKLKAAkgafdasVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQK 134
Cdd:cd19084 1 DLKVSRIGLGTWAIGGT-WWGEVDDQEsiEAIKAA-------IDLGINFFDTAPVYGFG-----HSEEILGKALKGRRDD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 135 eqveVAIATKFAaLPWR--------LGRGSVISALKDSLSRLGVSSVELYQLHWP-GIWGNEGYLDGLGDAYEQGLVKAV 205
Cdd:cd19084 68 ----VVIATKCG-LRWDggkgvtkdLSPESIRKEVEQSLRRLQTDYIDLYQIHWPdPNTPIEETAEALEKLKKEGKIRYI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 206 GVSNYSEKRLRDAyerlkKRGVPLASNQVNYSLIYRNPEENgVKAACDELGITLIAYSPIAQGVLTGKYTPNN--PPTGP 283
Cdd:cd19084 143 GVSNFSVEQLEEA-----RKYGPIVSLQPPYSMLEREIEEE-LLPYCRENGIGVLPYGPLAQGLLTGKYKKEPtfPPDDR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 284 RGRI--YTPEFLTKLQPLINRIKEIGGSYEKTPTQVVLNWLICQGNV-VPIPGAKNAEQAREFAGALGWSLTDQEVEELR 360
Cdd:cd19084 217 RSRFpfFRGENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVtSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
60-366 |
7.06e-73 |
|
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: 228.63 E-value: 7.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 60 VTKLGIGAWSWGDTTYWNefqwdDRKLKAAKGAFDASVDCGITFFDTAEVYGAGISgainsESLLGRFIKERQQkeqvEV 139
Cdd:cd19085 1 VSRLGLGCWQFGGGYWWG-----DQDDEESIATIHAALDAGINFFDTAEAYGDGHS-----EEVLGKALKGRRD----DV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 140 AIATKFAalPWRLGRGSVISALKDSLSRLGVSSVELYQLHWPgiwgNEG-----YLDGLGDAYEQGLVKAVGVSNYSEKR 214
Cdd:cd19085 67 VIATKVS--PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWP----SSDvpleeTMEALEKLKEEGKIRAIGVSNFGPAQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 215 LRDAyerlKKRGvPLASNQVNYSLIYRNPEeNGVKAACDELGITLIAYSPIAQGVLTGKYTPN--NPPTGPRGRIYT--- 289
Cdd:cd19085 141 LEEA----LDAG-RIDSNQLPYNLLWRAIE-YEILPFCREHGIGVLAYSPLAQGLLTGKFSSAedFPPGDARTRLFRhfe 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002286311 290 PEFLTKLQPLINRIKEIGGSYEKTPTQVVLNWLICQGNVV-PIPGAKNAEQAREFAGALGWSLTDQEVEELRSMAREI 366
Cdd:cd19085 215 PGAEEETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDPL 292
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
63-361 |
4.43e-72 |
|
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: 226.81 E-value: 4.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 63 LGIGAWSWGDTtyWNEFQWDDrklkaAKGAFDASVDCGITFFDTAEVYGAGISgainsESLLGRFIKERQQKEQvEVAIA 142
Cdd:pfam00248 1 IGLGTWQLGGG--WGPISKEE-----ALEALRAALEAGINFIDTAEVYGDGKS-----EELLGEALKDYPVKRD-KVVIA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 143 TKF----AALPWRLGRGSVISALKDSLSRLGVSSVELYQLHWP-GIWGNEGYLDGLGDAYEQGLVKAVGVSNYSEKRLRD 217
Cdd:pfam00248 68 TKVpdgdGPWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPdPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 218 AyerLKKRGVPLASNQVNYSLIYRNPEEnGVKAACDELGITLIAYSPIAQGVLTGKYTPNNPPTGPRGRIYTPEFLTKLQ 297
Cdd:pfam00248 148 A---LTKGKIPIVAVQVEYNLLRRRQEE-ELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGTPLNL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002286311 298 PLINRIKEIGGSYEKTPTQVVLNWLICQ-GNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRS 361
Cdd:pfam00248 224 EALEALEEIAKEHGVSPAQVALRWALSKpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDE 288
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
57-360 |
9.35e-68 |
|
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: 214.40 E-value: 9.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 57 DVAVTKLGIGawSWGDTTYWNEFQWDDRK-LKAAKGAFDAsvdcGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQKE 135
Cdd:cd19072 1 GEEVPVLGLG--TWGIGGGMSKDYSDDKKaIEALRYAIEL----GINLIDTAEMYGGG-----HAEELVGKAIKGFDRED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 136 qveVAIATKFaaLPWRLGRGSVISALKDSLSRLGVSSVELYQLHWPGIWGN-EGYLDGLGDAYEQGLVKAVGVSNYSEKR 214
Cdd:cd19072 70 ---LFITTKV--SPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPiEETLRAMEELVEEGKIRYIGVSNFSLEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 215 LRDAYERLKKrgVPLASNQVNYSLIYRNpEENGVKAACDELGITLIAYSPIAQGVLTGKytpnnpptgprgriytpeflt 294
Cdd:cd19072 145 LEEAQSYLKK--GPIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNA--------------------- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286311 295 klqPLINRIKEIGGSYEKTPTQVVLNWLICQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELR 360
Cdd:cd19072 201 ---KGSPLLDEIAKKYGKTPAQIALNWLISKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
61-342 |
2.18e-59 |
|
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: 191.96 E-value: 2.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 61 TKLGIGAWSWGDttywnefqwdDRKLKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQKEQVevA 140
Cdd:cd06660 1 SRLGLGTMTFGG----------DGDEEEAFALLDAALEAGGNFFDTADVYGDG-----RSERLLGRWLKGRGNRDDV--V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 141 IATKFAALPW------RLGRGSVISALKDSLSRLGVSSVELYQLHWPGI-WGNEGYLDGLGDAYEQGLVKAVGVSNYSEK 213
Cdd:cd06660 64 IATKGGHPPGgdpsrsRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPsTPVEETLEALNELVREGKIRYIGVSNWSAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 214 RLRDAYERLKKRG-VPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGvltgkytpnnpptgprgriytpef 292
Cdd:cd06660 144 RLAEALAYAKAHGlPGFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG------------------------ 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1002286311 293 ltklqplinrikeiggsyektPTQVVLNWLICQ-GNVVPIPGAKNAEQARE 342
Cdd:cd06660 200 ---------------------PAQLALAWLLSQpFVTVPIVGARSPEQLEE 229
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
62-363 |
9.67e-57 |
|
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: 187.54 E-value: 9.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 62 KLGIGAWSWG------DTTYWNEFQWDDrkLKAAkgaFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQKE 135
Cdd:cd19103 6 KIALGTWSWGsggaggDQVFGNHLDEDT--LKAV---FDKAMAAGLNLWDTAAVYGMG-----ASEKILGEFLKRYPRED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 136 qveVAIATKFAALPWRLGRGSVISALKDSLSRLGVSSVELYQLHWPGiwGNEGYLDGLGDAYEQGLVKAVGVSNYSEKRL 215
Cdd:cd19103 76 ---YIISTKFTPQIAGQSADPVADMLEGSLARLGTDYIDIYWIHNPA--DVERWTPELIPLLKSGKVKHVGVSNHNLAEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 216 RDAYERLKKRGVPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGKYTPNNP-PTGP-RGRIYTPeFL 293
Cdd:cd19103 151 KRANEILAKAGVSLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKHPlPEGSgRAETYNP-LL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 294 TKLQPLINRIKEIGGSYEKTPTQVVLNWLICQGnVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSMA 363
Cdd:cd19103 230 PQLEELTAVMAEIGAKHGASIAQVAIAWAIAKG-TTPIIGVTKPHHVEDAARAASITLTDDEIKELEQLA 298
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
50-361 |
1.87e-56 |
|
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: 187.09 E-value: 1.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 50 KVRLGGSDVAVTKLGIGAWSWGDTTYWNEFqwDDRKlkaAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIK 129
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAIGGGPWWGGS--DDNE---SIRTIHAALDLGINLIDTAPAYGFG-----HSEEIVGKAIK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 130 ERQQKeqveVAIATKFAaLPWRLGRG------------------SVISALKDSLSRLGVSSVELYQLHWPG----IWGNE 187
Cdd:cd19149 71 GRRDK----VVLATKCG-LRWDREGGsfffvrdgvtvyknlspeSIREEVEQSLKRLGTDYIDLYQTHWQDvetpIEETM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 188 GYLDGLgdaYEQGLVKAVGVSNYSEKRLrDAYERlkkrGVPLASNQVNYSLIYRNPEENgVKAACDELGITLIAYSPIAQ 267
Cdd:cd19149 146 EALEEL---KRQGKIRAIGASNVSVEQI-KEYVK----AGQLDIIQEKYSMLDRGIEKE-LLPYCKKNNIAFQAYSPLEQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 268 GVLTGKYTP--NNPPTGPRGRI--YTPEFLTKLQPLINRIKEIGGSYEKTPTQVVLNWLICQ-GNVVPIPGAKNAEQARE 342
Cdd:cd19149 217 GLLTGKITPdrEFDAGDARSGIpwFSPENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQpGITSALCGARKPEQAEE 296
|
330
....*....|....*....
gi 1002286311 343 FAGALGWSLTDQEVEELRS 361
Cdd:cd19149 297 NAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
52-359 |
2.16e-56 |
|
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: 186.65 E-value: 2.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 52 RLGGSDVAVTKLGIGAWSWGDTTywnefqwdDRKlkAAKGAFDASVDCGITFFDTAEVYGAGISGAIN--SESLLGRFIK 129
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVFGWTA--------DEE--TSFALLDAFVDAGGNFIDTADVYSAWVPGNAGgeSETIIGRWLK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 130 ERQQKEQVevAIATKFAALPWR----LGRGSVISALKDSLSRLGVSSVELYQLHWpgiWGN----EGYLDGLGDAYEQGL 201
Cdd:cd19081 71 SRGKRDRV--VIATKVGFPMGPngpgLSRKHIRRAVEASLRRLQTDYIDLYQAHW---DDPatplEETLGALNDLIRQGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 202 VKAVGVSNYSEKRLRDAYERLKKRGVP-LASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGKYTPNNPP 280
Cdd:cd19081 146 VRYIGASNYSAWRLQEALELSRQHGLPrYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 281 TG--PRGRIY----TPEFLTKLQPLinriKEIGGSYEKTPTQVVLNWLICQGNV-VPIPGAKNAEQAREFAGALGWSLTD 353
Cdd:cd19081 226 PGstRRGEAAkrylNERGLRILDAL----DEVAAEHGATPAQVALAWLLARPGVtAPIAGARTVEQLEDLLAAAGLRLTD 301
|
....*.
gi 1002286311 354 QEVEEL 359
Cdd:cd19081 302 EEVARL 307
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
60-359 |
7.28e-56 |
|
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: 185.18 E-value: 7.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 60 VTKLGIGAWSWG--DTTYWNEFQWDDRKLKAAKGAFDAsvdcGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQkeqv 137
Cdd:cd19102 1 LTTIGLGTWAIGggGWGGGWGPQDDRDSIAAIRAALDL----GINWIDTAAVYGLG-----HSEEVVGRALKGLRD---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 138 EVAIATKFAALP-------WRLGRGSVISALKDSLSRLGVSSVELYQLHWPGiwGNEGYLDG---LGDAYEQGLVKAVGV 207
Cdd:cd19102 68 RPIVATKCGLLWdeegrirRSLKPASIRAECEASLRRLGVDVIDLYQIHWPD--PDEPIEEAwgaLAELKEEGKVRAIGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 208 SNYSEkrlrDAYERLKKRGvPLASNQVNYSLIYRnPEENGVKAACDELGITLIAYSPIAQGVLTGKYTP----NNPPTG- 282
Cdd:cd19102 146 SNFSV----DQMKRCQAIH-PIASLQPPYSLLRR-GIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPervaSLPADDw 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286311 283 -PRGRIYTPEFLTKLQPLINRIKEIGGSYEKTPTQVVLNWLICQGNVV-PIPGAKNAEQAREFAGALGWSLTDQEVEEL 359
Cdd:cd19102 220 rRRSPFFQEPNLARNLALVDALRPIAERHGRTVAQLAIAWVLRRPEVTsAIVGARRPDQIDETVGAADLRLTPEELAEI 298
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
97-364 |
2.16e-55 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 182.56 E-value: 2.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 97 VDCGITFFDTAEVYGAgisgainsESLLGRFIKE----RQqkeqvEVAIATKFaaLPWRLGRGSVISALKDSLSRLGVSS 172
Cdd:COG0656 28 LEAGYRHIDTAAMYGN--------EEGVGEAIAAsgvpRE-----ELFVTTKV--WNDNHGYDDTLAAFEESLERLGLDY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 173 VELYQLHWPGIWGNEGYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAYERLkkrGVPLASNQVNYSLIYRNPEengVKAAC 252
Cdd:COG0656 93 LDLYLIHWPGPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAET---GVKPAVNQVELHPYLQQRE---LLAFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 253 DELGITLIAYSPIAQG-VLtgkytpNNPPtgprgriytpefltklqplinrIKEIGGSYEKTPTQVVLNWLIcQGNVVPI 331
Cdd:COG0656 167 REHGIVVEAYSPLGRGkLL------DDPV----------------------LAEIAEKHGKTPAQVVLRWHL-QRGVVVI 217
|
250 260 270
....*....|....*....|....*....|...
gi 1002286311 332 PGAKNAEQAREFAGALGWSLTDQEVEELRSMAR 364
Cdd:COG0656 218 PKSVTPERIRENLDAFDFELSDEDMAAIDALDR 250
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
51-359 |
3.56e-54 |
|
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: 181.24 E-value: 3.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 51 VRLGGSDVAVTKLGIGAWSWGDTTY--WNEFQWDDRKLkaakgaFDASVDCGITFFDTAEVYGAGIsgainSESLLGRFI 128
Cdd:cd19079 3 VRLGNSGLKVSRLCLGCMSFGDPKWrpWVLDEEESRPI------IKRALDLGINFFDTANVYSGGA-----SEEILGRAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 129 KERQQKEqvEVAIATKFAAlPWR-------LGRGSVISALKDSLSRLGVSSVELYQLHWpgiWGN----EGYLDGLGDAY 197
Cdd:cd19079 72 KEFAPRD--EVVIATKVYF-PMGdgpngrgLSRKHIMAEVDASLKRLGTDYIDLYQIHR---WDYetpiEETLEALHDVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 198 EQGLVKAVGVSNYSEKRLRDAYERLKKRG-VPLASNQVNYSLIYRNpEENGVKAACDELGITLIAYSPIAQGVLTGKYTP 276
Cdd:cd19079 146 KSGKVRYIGASSMYAWQFAKALHLAEKNGwTKFVSMQNHYNLLYRE-EEREMIPLCEEEGIGVIPWSPLARGRLARPWGD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 277 NN------PPTGPRGRIYTPEfltKLQPLINRIKEIGGSYEKTPTQVVLNWLICQGNVV-PIPGAKNAEQAREFAGALGW 349
Cdd:cd19079 225 TTerrrstTDTAKLKYDYFTE---ADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTaPIVGATKLEHLEDAVAALDI 301
|
330
....*....|
gi 1002286311 350 SLTDQEVEEL 359
Cdd:cd19079 302 KLSEEEIKYL 311
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
52-359 |
1.16e-53 |
|
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: 180.12 E-value: 1.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 52 RLGGSDVAVTKLGIGAWSWGDTTYWNEfQWDDRKLKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKER 131
Cdd:cd19091 5 TLGRSGLKVSELALGTMTFGGGGGFFG-AWGGVDQEEADRLVDIALDAGINFFDTADVYSEG-----ESEEILGKALKGR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 132 QQKeqveVAIATKFAALPWR------LGRGSVISALKDSLSRLGVSSVELYQLH-WPGIWGNEGYLDGLGDAYEQGLVKA 204
Cdd:cd19091 79 RDD----VLIATKVRGRMGEgpndvgLSRHHIIRAVEASLKRLGTDYIDLYQLHgFDALTPLEETLRALDDLVRQGKVRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 205 VGVSNYSEKRLRDAYERLKKRG-VPLASNQVNYSLIYRNpEENGVKAACDELGITLIAYSPIAQGVLTGKYTPNNP-PTG 282
Cdd:cd19091 155 IGVSNFSAWQIMKALGISERRGlARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPaPEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 283 PRGRIYTPEFL----TKLQPLINRIKEIGGSYEKTPTQVVLNWLICQGNVVP-IPGAKNAEQAREFAGALGWSLTDQEVE 357
Cdd:cd19091 234 SRLRRTGFDFPpvdrERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSvIIGARNEEQLEDNLGAAGLSLTPEEIA 313
|
..
gi 1002286311 358 EL 359
Cdd:cd19091 314 RL 315
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
50-359 |
5.59e-52 |
|
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: 175.10 E-value: 5.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 50 KVRLGGSDVAVTKLGIGA----WSWGDTtywnefqwDDrklKAAKGAFDASVDCGITFFDTAEVYGAGISgainsESLLG 125
Cdd:cd19076 2 TRKLGTQGLEVSALGLGCmgmsAFYGPA--------DE---EESIATLHRALELGVTFLDTADMYGPGTN-----EELLG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 126 RFIKERQQKeqveVAIATKFAALpWRLGRGSVI---------SALKDSLSRLGVSSVELYQLH-------WPGIWGnegy 189
Cdd:cd19076 66 KALKDRRDE----VVIATKFGIV-RDPGSGFRGvdgrpeyvrAACEASLKRLGTDVIDLYYQHrvdpnvpIEETVG---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 190 ldGLGDAYEQGLVKAVGVSNYSEKRLRDAYerlkkRGVPLASNQVNYSLIYRNPEEnGVKAACDELGITLIAYSPIAQGV 269
Cdd:cd19076 137 --AMAELVEEGKVRYIGLSEASADTIRRAH-----AVHPITAVQSEYSLWTRDIED-EVLPTCRELGIGFVAYSPLGRGF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 270 LTGKYT-PNNPPTGPRGRI---YTPEFLTKLQPLINRIKEIGGSYEKTPTQVVLNWLICQG-NVVPIPGAKNAEQAREFA 344
Cdd:cd19076 209 LTGAIKsPEDLPEDDFRRNnprFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQGdDIVPIPGTKRIKYLEENV 288
|
330
....*....|....*
gi 1002286311 345 GALGWSLTDQEVEEL 359
Cdd:cd19076 289 GALDVVLTPEELAEI 303
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
50-359 |
3.75e-48 |
|
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: 163.96 E-value: 3.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 50 KVRLGgSDVAVTKLGIGAWSWGDttywnefqwDDRKLKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIK 129
Cdd:cd19138 2 TVTLP-DGTKVPALGQGTWYMGE---------DPAKRAQEIEALRAGIDLGMTLIDTAEMYGDG-----GSEELVGEAIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 130 ERQQKeqveVAIATKfaALPWRLGRGSVISALKDSLSRLGVSSVELYQLHWPGIWGNEGYLDGLGDAYEQGLVKAVGVSN 209
Cdd:cd19138 67 GRRDK----VFLVSK--VLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEELKKEGKIRAWGVSN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 210 YSEKRLRDAYERLKkrGVPLASNQVNYSLIYRNPEeNGVKAACDELGITLIAYSPIAQGVLTGKYTPNNPptgprgriyt 289
Cdd:cd19138 141 FDTDDMEELWAVPG--GGNCAANQVLYNLGSRGIE-YDLLPWCREHGVPVMAYSPLAQGGLLRRGLLENP---------- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 290 pefltklqplinRIKEIGGSYEKTPTQVVLNWLICQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEEL 359
Cdd:cd19138 208 ------------TLKEIAARHGATPAQVALAWVLRDGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
58-359 |
4.23e-48 |
|
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: 163.90 E-value: 4.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 58 VAVTKLGIGAWSWGDTTYwNEFQWDDRKLKAAKgafdASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKE-RQQKeq 136
Cdd:cd19137 2 EKIPALGLGTWGIGGFLT-PDYSRDEEMVELLK----TAIELGYTHIDTAEMYGGG-----HTEELVGKAIKDfPRED-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 137 veVAIATKfaALPWRLGRGSVISALKDSLSRLGVSSVELYQLHWPG--IWGNEGyLDGLGDAYEQGLVKAVGVSNYSEKR 214
Cdd:cd19137 70 --LFIVTK--VWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNpnIPLEET-LSAMAEGVRQGLIRYIGVSNFNRRL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 215 LRDAYERLKKrgvPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLtgkytpnnpptgprgriytpeflt 294
Cdd:cd19137 145 LEEAISKSQT---PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLE------------------------ 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286311 295 klqpLINR-IKEIGGSYEKTPTQVVLNWLICQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEEL 359
Cdd:cd19137 198 ----KTNRtLEEIAKNYGKTIAQIALAWLIQKPNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
60-346 |
2.05e-45 |
|
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: 156.10 E-value: 2.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 60 VTKLGIGAWSWGdTTYWNEFqwDDRKlkaAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQKeqveV 139
Cdd:cd19086 3 VSEIGFGTWGLG-GDWWGDV--DDAE---AIRALRAALDLGINFFDTADVYGDG-----HSERLLGKALKGRRDK----V 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 140 AIATKF-------AALPWRLGRGSVISALKDSLSRLGVSSVELYQLH-WPGIW-GNEGYLDGLGDAYEQGLVKAVGVSNy 210
Cdd:cd19086 68 VIATKFgnrfdggPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVlDNDELFEALEKLKQEGKIRAYGVSV- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 211 seKRLRDAYERLKKRGVplASNQVNYSLIYRNPEEnGVKAACDELGITLIAYSPIAQGVLTGKytpnnpptgprgriytp 290
Cdd:cd19086 147 --GDPEEALAALRRGGI--DVVQVIYNLLDQRPEE-ELFPLAEEHGVGVIARVPLASGLLTGK----------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002286311 291 efltklqplinrikeiggsyektPTQVVLNWLICQGNV-VPIPGAKNAEQAREFAGA 346
Cdd:cd19086 205 -----------------------LAQAALRFILSHPAVsTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
97-359 |
2.33e-45 |
|
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: 157.78 E-value: 2.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 97 VDCGITFFDTAEVYGAgisgaINSESLLGRFIKERQQKeqveVAIATKF-----AALPWRLGRGS----VISALKDSLSR 167
Cdd:cd19078 35 VELGITFFDTAEVYGP-----YTNEELVGEALKPFRDQ----VVIATKFgfkidGGKPGPLGLDSrpehIRKAVEGSLKR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 168 LGVSSVELYQLHW--PGIwGNEGYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAYERLkkrgvPLASNQVNYSLIYRNPEE 245
Cdd:cd19078 106 LQTDYIDLYYQHRvdPNV-PIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAVC-----PVTAVQSEYSMMWREPEK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 246 nGVKAACDELGITLIAYSPIAQGVLTGKYTPNN--PPTGPRGRI--YTPEFLTKLQPLINRIKEIGGSYEKTPTQVVLNW 321
Cdd:cd19078 180 -EVLPTLEELGIGFVPFSPLGKGFLTGKIDENTkfDEGDDRASLprFTPEALEANQALVDLLKEFAEEKGATPAQIALAW 258
|
250 260 270
....*....|....*....|....*....|....*....
gi 1002286311 322 LICQG-NVVPIPGAKNAEQAREFAGALGWSLTDQEVEEL 359
Cdd:cd19078 259 LLAKKpWIVPIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
81-361 |
7.25e-44 |
|
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: 153.90 E-value: 7.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 81 WDDRKLKAAKGAFDASVDCGITFFDTAEVYGagisgaiNSESLLGRFIKERQQKEQV--EVAIATKFAALPWRLG--RGS 156
Cdd:cd19101 17 GGIRDEDAAVRAMAAYVDAGLTTFDCADIYG-------PAEELIGEFRKRLRRERDAadDVQIHTKWVPDPGELTmtRAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 157 VISALKDSLSRLGVSSVELYQLHWpgiW--GNEGYLDGLGDAYE---QGLVKAVGVSNYSEKRLRDAYERlkkrGVPLAS 231
Cdd:cd19101 90 VEAAIDRSLKRLGVDRLDLVQFHW---WdySDPGYLDAAKHLAElqeEGKIRHLGLTNFDTERLREILDA----GVPIVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 232 NQVNYSLIYRNPeENGVKAACDELGITLIAYSPIAQGVLTGKYTPNNPPTGPRGriyTPEFLTK-------------LQP 298
Cdd:cd19101 163 NQVQYSLLDRRP-ENGMAALCEDHGIKLLAYGTLAGGLLSEKYLGVPEPTGPAL---ETRSLQKyklmidewggwdlFQE 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286311 299 LINRIKEIGGSYEKTPTQVVLNWLICQGNVV-PIPGAKNAEQAREFAGALGWSLTDQEVEELRS 361
Cdd:cd19101 239 LLRTLKAIADKHGVSIANVAVRWVLDQPGVAgVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
51-369 |
1.44e-43 |
|
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: 153.75 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 51 VRLGGSDVAVTKLGIGAWswGDTTYWNEFQWDDRKLKAakgaFDASVDCGITFFDTAEVYGagisgaiNSESLLGRFIKE 130
Cdd:cd19144 4 RTLGRNGPSVPALGFGAM--GLSAFYGPPKPDEERFAV----LDAAFELGCTFWDTADIYG-------DSEELIGRWFKQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 131 RQQKEQvEVAIATKFA-ALPWRLGRGSVIS-------ALKDSLSRLGVSSVELYQLH-WPGIWGNEGYLDGLGDAYEQGL 201
Cdd:cd19144 71 NPGKRE-KIFLATKFGiEKNVETGEYSVDGspeyvkkACETSLKRLGVDYIDLYYQHrVDGKTPIEKTVAAMAELVQEGK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 202 VKAVGVSNYSEKRLRDAYERLkkrgvPLASNQVNYSLIYRNPEEN--GVKAACDELGITLIAYSPIAQGVLTGKYT-PNN 278
Cdd:cd19144 150 IKHIGLSECSAETLRRAHAVH-----PIAAVQIEYSPFSLDIERPeiGVLDTCRELGVAIVAYSPLGRGFLTGAIRsPDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 279 PPTG------PRgriYTPEFLTKLQPLINRIKEIGGSYEKTPTQVVLNWLICQGN-VVPIPGAKNAEQAREFAGALGWSL 351
Cdd:cd19144 225 FEEGdfrrmaPR---FQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDdIIPIPGTTKLKRLEENLGALKVKL 301
|
330
....*....|....*...
gi 1002286311 352 TDQEVEELRSMAREIKPV 369
Cdd:cd19144 302 TEEEEKEIREIAEEAEVV 319
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
89-359 |
2.29e-43 |
|
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: 151.10 E-value: 2.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 89 AKGAFDASVDCGITFFDTAEVYG--AGISGAINsESLLGRfikerqqkeqVEVAIATKFAalPWRLGRGSVISALKDSLS 166
Cdd:cd19071 16 TAEAVLAALEAGYRHIDTAAAYGneAEVGEAIR-ESGVPR----------EELFITTKLW--PTDHGYERVREALEESLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 167 RLGVSSVELYQLHWPGIWGNEG----YLD---GLGDAYEQGLVKAVGVSNYSEKRLrdayERLKK-RGVPLASNQVNYSL 238
Cdd:cd19071 83 DLGLDYLDLYLIHWPVPGKEGGskeaRLEtwrALEELVDEGLVRSIGVSNFNVEHL----EELLAaARIKPAVNQIELHP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 239 IYRNPEengVKAACDELGITLIAYSPIAQGVLTGKytpNNPptgprgriytpefltklqplinRIKEIGGSYEKTPTQVV 318
Cdd:cd19071 159 YLQQKE---LVEFCKEHGIVVQAYSPLGRGRRPLL---DDP----------------------VLKEIAKKYGKTPAQVL 210
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1002286311 319 LNWLIcQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEEL 359
Cdd:cd19071 211 LRWAL-QRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
76-360 |
2.39e-43 |
|
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: 152.39 E-value: 2.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 76 WNEFQWDDrklKAAKGAFDASVDCGITFFDTAEVYGagISGAINSESLLGRFIKERQQKEQvEVAIATKFAALPWRLGRG 155
Cdd:cd19077 17 WRPNPTPD---EEAFETMKAALDAGSNLWNGGEFYG--PPDPHANLKLLARFFRKYPEYAD-KVVLSVKGGLDPDTLRPD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 156 SVISALKDS----LSRLG-VSSVELYQL-----HWPgIwgnEGYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAYerlkkR 225
Cdd:cd19077 91 GSPEAVRKSieniLRALGgTKKIDIFEParvdpNVP-I---EETIKALKELVKEGKIRGIGLSEVSAETIRRAH-----A 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 226 GVPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGKYTPNNPPTGPRGRIYTPEF----LTKLQPLIN 301
Cdd:cd19077 162 VHPIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHLDRFngenFEKNLKLVD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002286311 302 RIKEIGGSYEKTPTQVVLNWLICQGN--VVPIPGAKNAEQAREFAGALGWSLTDQEVEELR 360
Cdd:cd19077 242 ALQELAEKKGCTPAQLALAWILAQSGpkIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
51-359 |
9.51e-43 |
|
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: 151.19 E-value: 9.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 51 VRLGGSDVAVTKLGIGAWSWGDTTywnefqwdDRKlkAAKGAFDASVDCGITFFDTAEVYGAGISgainsESLLGRFIKE 130
Cdd:cd19087 4 RTLGRTGLKVSRLCLGTMNFGGRT--------DEE--TSFAIMDRALDAGINFFDTADVYGGGRS-----EEIIGRWIAG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 131 RQQkeqvEVAIATKF----AALPWRLG--RGSVISALKDSLSRLGVSSVELYQLH-------WpgiwgnEGYLDGLGDAY 197
Cdd:cd19087 69 RRD----DIVLATKVfgpmGDDPNDRGlsRRHIRRAVEASLRRLQTDYIDLYQMHhfdrdtpL------EETLRALDDLV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 198 EQGLVKAVGVSNYSEKRLRDAYERLKKRGV-PLASNQVNYSLIYRNPEeNGVKAACDELGITLIAYSPIAQGVLTGKYTP 276
Cdd:cd19087 139 RQGKIRYIGVSNFAAWQIAKAQGIAARRGLlRFVSEQPMYNLLKRQAE-LEILPAARAYGLGVIPYSPLAGGLLTGKYGK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 277 NNPPTGprGRIYTPEfLTKLQPLINRIKEIGGSYEK-------TPTQVVLNWLICQGNVV-PIPGAKNAEQAREFAGALG 348
Cdd:cd19087 218 GKRPES--GRLVERA-RYQARYGLEEYRDIAERFEAlaaeaglTPASLALAWVLSHPAVTsPIIGPRTLEQLEDSLAALE 294
|
330
....*....|.
gi 1002286311 349 WSLTDQEVEEL 359
Cdd:cd19087 295 ITLTPELLAEI 305
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
93-347 |
3.30e-42 |
|
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: 149.24 E-value: 3.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 93 FDASVDCGITFFDTAEVYGAGIsGAINSESLLGRFIKERQQKEqvEVAIATKFA------ALPWRLGRGSVISALKDSLS 166
Cdd:cd19082 23 LDAFVELGGNFIDTARVYGDWV-ERGASERVIGEWLKSRGNRD--KVVIATKGGhpdledMSRSRLSPEDIRADLEESLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 167 RLGVSSVELYQLHW-----PGiwgnEGYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAYERLKKRG-VPLASNQVNYSLIY 240
Cdd:cd19082 100 RLGTDYIDLYFLHRddpsvPV----GEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGlPGFAASSPQWSLAR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 241 RNPE--ENGVKAACD--------ELGITLIAYSPIAQGVLTGKYTPNNPPTGP-RGRIYTPEFLTKLQplinRIKEIGGS 309
Cdd:cd19082 176 PNEPpwPGPTLVAMDeemrawheENQLPVFAYSSQARGFFSKRAAGGAEDDSElRRVYYSEENFERLE----RAKELAEE 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 1002286311 310 YEKTPTQVVLNWLICQG-NVVPIPGAKNAEQAREFAGAL 347
Cdd:cd19082 252 KGVSPTQIALAYVLNQPfPTVPIIGPRTPEQLRDSLAAA 290
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
56-358 |
7.65e-42 |
|
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: 148.61 E-value: 7.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 56 SDVAVTKLGIGAWSWGDTtywnefqwDDrklKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQKE 135
Cdd:cd19148 5 SRIALGTWAIGGWMWGGT--------DE---KEAIETIHKALDLGINLIDTAPVYGFG-----LSEEIVGKALKEYGKRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 136 QveVAIATKfAALPWRLG--------RGSVISALKDSLSRLGVSSVELYQLHWPG----IwgnEGYLDGLGDAYEQGLVK 203
Cdd:cd19148 69 R--VVIATK-VGLEWDEGgevvrnssPARIRKEVEDSLRRLQTDYIDLYQVHWPDplvpI---EETAEALKELLDEGKIR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 204 AVGVSNYSEKRLrdayERLKKrGVPLASNQVNYSLIYRNPEEnGVKAACDELGITLIAYSPIAQGVLTGKYTPNNPPTGP 283
Cdd:cd19148 143 AIGVSNFSPEQM----ETFRK-VAPLHTVQPPYNLFEREIEK-DVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 284 RGRIYTPEF-----------LTKLQPLINRikeiggSYEKTPTQVVLNWLICQGNV-VPIPGAKNAEQAREFAGALGWSL 351
Cdd:cd19148 217 DLRRTDPKFqeprfsqylaaVEELDKLAQE------RYGKSVIHLAVRWLLDQPGVsIALWGARKPEQLDAVDEVFGWSL 290
|
....*..
gi 1002286311 352 TDQEVEE 358
Cdd:cd19148 291 NDEDMKE 297
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
60-353 |
1.54e-41 |
|
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: 147.74 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 60 VTKLGIGAWswgdTTYWNEFqwddrKLKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQKEQVev 139
Cdd:cd19074 4 VSELSLGTW----LTFGGQV-----DDEDAKACVRKAYDLGINFFDTADVYAAG-----QAEEVLGKALKGWPRESYV-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 140 aIATK--FAALPWRLGRG----SVISALKDSLSRLGVSSVELYQLHWPG----IwgnEGYLDGLGDAYEQGLVKAVGVSN 209
Cdd:cd19074 68 -ISTKvfWPTGPGPNDRGlsrkHIFESIHASLKRLQLDYVDIYYCHRYDpetpL---EETVRAMDDLIRQGKILYWGTSE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 210 YSEKRLRDAYERLKKRG-VPLASNQVNYSLIYRNPEENgVKAACDELGITLIAYSPIAQGVLTGKYTPNNPPtGPRGRIY 288
Cdd:cd19074 144 WSAEQIAEAHDLARQFGlIPPVVEQPQYNMLWREIEEE-VIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPP-PSRSRAT 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286311 289 TPEFLTKLQPLINR--------IKEIGGSYEKTPTQVVLNWLICQGNVV-PIPGAKNAEQAREFAGALGWSLTD 353
Cdd:cd19074 222 DEDNRDKKRRLLTDenlekvkkLKPIADELGLTLAQLALAWCLRNPAVSsAIIGASRPEQLEENVKASGVKLSP 295
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
50-356 |
7.16e-41 |
|
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: 146.02 E-value: 7.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 50 KVRLGGSDVAVTKLGIGA-WSWGDTTYWNEFQWDDRKL-KAAkgafdasVDCGITFFDTAEVYGAGisgaiNSESLLGRF 127
Cdd:cd19083 1 KVKLGKSDIDVNPIGLGTnAVGGHNLYPNLDEEEGKDLvREA-------LDNGVNLLDTAFIYGLG-----RSEELVGEV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 128 IKERQQKEqveVAIATKFAALpwRLGRGSVI--------SALKDSLSRLGVSSVELYQLHWP-GIWGNEGYLDGLGDAYE 198
Cdd:cd19083 69 LKEYNRNE---VVIATKGAHK--FGGDGSVLnnspeflrSAVEKSLKRLNTDYIDLYYIHFPdGETPKAEAVGALQELKD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 199 QGLVKAVGVSNYSEKRLRDAyerlKKRGVpLASNQVNYSLIYRNPEEnGVKAACDELGITLIAYSPIAQGVLTGKYTPNN 278
Cdd:cd19083 144 EGKIRAIGVSNFSLEQLKEA----NKDGY-VDVLQGEYNLLQREAEE-DILPYCVENNISFIPYFPLASGLLAGKYTKDT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 279 --PPTGPRGRI---YTPEFLTKLQPlINRIKEIGGSYEKTPTQVVLNWLICQGNV-VPIPGAKNAEQAREFAGALGWSLT 352
Cdd:cd19083 218 kfPDNDLRNDKplfKGERFSENLDK-VDKLKSIADEKGVTVAHLALAWYLTRPAIdVVIPGAKRAEQVIDNLKALDVTLT 296
|
....
gi 1002286311 353 DQEV 356
Cdd:cd19083 297 EEEI 300
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
53-359 |
2.47e-40 |
|
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: 144.67 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 53 LGGSDVAVTKLGIGAWSWGDTTYWNefqWDDrklKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQ 132
Cdd:cd19080 3 LGRSGLRVSPLALGTMTFGTEWGWG---ADR---EEARAMFDAYVEAGGNFIDTANNYTNG-----TSERLLGEFIAGNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 133 QkeqvEVAIATKF-----AALPWRLG--RGSVISALKDSLSRLGVSSVELYQLH-WPGIWGNEGYLDGLGDAYEQGLVKA 204
Cdd:cd19080 72 D----RIVLATKYtmnrrPGDPNAGGnhRKNLRRSVEASLRRLQTDYIDLLYVHaWDFTTPVEEVMRALDDLVRAGKVLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 205 VGVSNYSEKRLRDAYERLKKRGV-PLASNQVNYSLIYRNPEENGVKAAcDELGITLIAYSPIAQGVLTGKYTPNNPPTGP 283
Cdd:cd19080 148 VGISDTPAWVVARANTLAELRGWsPFVALQIEYSLLERTPERELLPMA-RALGLGVTPWSPLGGGLLTGKYQRGEEGRAG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 284 RGRIYTPEFltklQPLINRIKEIGGSYEK-------TPTQVVLNWLICQ-GNVVPIPGAKNAEQAREFAGALGWSLTDQE 355
Cdd:cd19080 227 EAKGVTVGF----GKLTERNWAIVDVVAAvaeelgrSAAQVALAWVRQKpGVVIPIIGARTLEQLKDNLGALDLTLSPEQ 302
|
....
gi 1002286311 356 VEEL 359
Cdd:cd19080 303 LARL 306
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
100-360 |
7.00e-40 |
|
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: 141.64 E-value: 7.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 100 GITFFDTAEVYgagisgaiNSESLLGRFIKErQQKEQVEVAIATKFaalpWR--LGRGSVISALKDSLSRLGVSSVELYQ 177
Cdd:cd19073 27 GYRHIDTAEIY--------NNEAEVGEAIAE-SGVPREDLFITTKV----WRdhLRPEDLKKSVDRSLEKLGTDYVDLLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 178 LHWPgiwgNEGY-----LDGLGDAYEQGLVKAVGVSNYSEKRLRDAyerLKKRGVPLASNQVNYSlIYRNPEEngVKAAC 252
Cdd:cd19073 94 IHWP----NPTVpleetLGALKELKEAGKVKSIGVSNFTIELLEEA---LDISPLPIAVNQVEFH-PFLYQAE--LLEYC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 253 DELGITLIAYSPIAQGVLtgkytPNNPPtgprgriytpefltklqplinrIKEIGGSYEKTPTQVVLNWLICQGnVVPIP 332
Cdd:cd19073 164 RENDIVITAYSPLARGEV-----LRDPV----------------------IQEIAEKYDKTPAQVALRWLVQKG-IVVIP 215
|
250 260
....*....|....*....|....*...
gi 1002286311 333 GAKNAEQAREFAGALGWSLTDQEVEELR 360
Cdd:cd19073 216 KASSEDHLKENLAIFDWELTSEDVAKID 243
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
93-358 |
3.99e-37 |
|
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: 136.54 E-value: 3.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 93 FDASVDCGITFFDTAEVY---------GAgisgainSESLLGRFIKERQQKEqvEVAIATKFA----ALPW------RLG 153
Cdd:cd19094 24 LDYAFDEGVNFIDTAEMYpvppspetqGR-------TEEIIGSWLKKKGNRD--KVVLATKVAgpgeGITWprgggtRLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 154 RGSVISALKDSLSRLGVSSVELYQLHWP----GIWGNEGY---------------LDGLGDAYEQGLVKAVGVSNYSEKR 214
Cdd:cd19094 95 RENIREAVEGSLKRLGTDYIDLYQLHWPdrytPLFGGGYYtepseeedsvsfeeqLEALGELVKAGKIRHIGLSNETPWG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 215 LRDAYERLKKRGVP-LASNQVNYSLIYRNPEEnGVKAACDELGITLIAYSPIAQGVLTGKYT-PNNPPTGPRGRIYtPEF 292
Cdd:cd19094 175 VMKFLELAEQLGLPrIVSIQNPYSLLNRNFEE-GLAEACHRENVGLLAYSPLAGGVLTGKYLdGAARPEGGRLNLF-PGY 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002286311 293 LT-KLQPL----INRIKEIGGSYEKTPTQVVLNWLICQGNVVP-IPGAKNAEQAREFAGALGWSLTDqEVEE 358
Cdd:cd19094 253 MArYRSPQaleaVAEYVKLARKHGLSPAQLALAWVRSRPFVTStIIGATTLEQLKENIDAFDVPLSD-ELLA 323
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
55-355 |
1.15e-35 |
|
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: 131.52 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 55 GSDVAVTKLGIGAWSWGDttyWNEfqwDDRKLKAAkgaFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQK 134
Cdd:cd19092 1 PEGLEVSRLVLGCMRLAD---WGE---SAEELLSL---IEAALELGITTFDHADIYGGG-----KCEELFGEALALNPGL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 135 -EQVEV----AIATKFAALPWRLGR-----GSVISALKDSLSRLGVSSVELYQLHWPgiwgnegylDGLGDAYE------ 198
Cdd:cd19092 67 rEKIEIqtkcGIRLGDDPRPGRIKHydtskEHILASVEGSLKRLGTDYLDLLLLHRP---------DPLMDPEEvaeafd 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 199 ----QGLVKAVGVSNYSEKRLrdayERLKKR-GVPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGk 273
Cdd:cd19092 138 elvkSGKVRYFGVSNFTPSQI----ELLQSYlDQPLVTNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFG- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 274 ytpnnpptgprgriytpEFLTKLQPLINRIKEIGGSYEKTPTQVVLNWLICQ-GNVVPIPGAKNAEQAREFAGALGWSLT 352
Cdd:cd19092 213 -----------------GFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHpARIQPILGTTNPERIRSAVKALDIELT 275
|
...
gi 1002286311 353 DQE 355
Cdd:cd19092 276 REE 278
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
60-352 |
2.14e-35 |
|
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: 130.03 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 60 VTKLGIGAWSWGDTTYWNEfqwdDRKLKAAKGAFDASVDCGITFFDTAEVYGAGISgainsESLLGRFIKERQQKeqveV 139
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWGP----PADREEAIAVLRRALELGVNFIDTADSYGPDVN-----ERLIAEALHPYPDD----V 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 140 AIATKFAAL-----PW-RLGR-GSVISALKDSLSRLGVSSVELYQLHWPGIWGN-EGYLDGLGDAYEQGLVKAVGVSNYS 211
Cdd:cd19088 68 VIATKGGLVrtgpgWWgPDGSpEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPfEEQLGALAELQDEGLIRHIGLSNVT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 212 EKRLRDAyerlkKRGVPLASNQVNYSLIYRNPEenGVKAACDELGITLIAYSPIAQGvltgkytpnnPPTGPRGriytpe 291
Cdd:cd19088 148 VAQIEEA-----RAIVRIVSVQNRYNLANRDDE--GVLDYCEAAGIAFIPWFPLGGG----------DLAQPGG------ 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002286311 292 fltklqplinRIKEIGGSYEKTPTQVVLNWLICQG-NVVPIPGAKNAEQAREFAGALGWSLT 352
Cdd:cd19088 205 ----------LLAEVAARLGATPAQVALAWLLARSpVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
87-362 |
4.39e-35 |
|
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: 129.30 E-value: 4.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 87 KAAKGAFDASVDCGITFFDTAEVYGagisgainSESLLGRFIKE----RQqkeqvEVAIATKfaALPWRLGRGSVISALK 162
Cdd:cd19140 21 EECTRAVEHALELGYRHIDTAQMYG--------NEAQVGEAIAAsgvpRD-----ELFLTTK--VWPDNYSPDDFLASVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 163 DSLSRLGVSSVELYQLHWPGIWG-NEGYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAYERLkkrGVPLASNQVNYSlIYR 241
Cdd:cd19140 86 ESLRKLRTDYVDLLLLHWPNKDVpLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELS---EAPLFTNQVEYH-PYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 242 NPEEngVKAACDELGITLIAYSPIAQGVLtgkytPNNPptgprgriytpefltklqplinRIKEIGGSYEKTPTQVVLNW 321
Cdd:cd19140 162 DQRK--LLDAAREHGIALTAYSPLARGEV-----LKDP----------------------VLQEIGRKHGKTPAQVALRW 212
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1002286311 322 LICQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSM 362
Cdd:cd19140 213 LLQQEGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
63-362 |
3.56e-33 |
|
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: 124.36 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 63 LGIGAWSWGDttywnefQWDDRKLKAAKgafdasvDCGITFFDTAEVYGagisgainSESLLGRFIKERQQKEQvEVAIA 142
Cdd:cd19135 16 LGLGTSHSGG-------YSHEAVVYALK-------ECGYRHIDTAKRYG--------CEELLGKAIKESGVPRE-DLFLT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 143 TKFaaLPWRLGRGSVISALKDSLSRLGVSSVELYQLHWPG--IWGN------EGYLDGLGDAYEQGLVKAVGVSNYSEKR 214
Cdd:cd19135 73 TKL--WPSDYGYESTKQAFEASLKRLGVDYLDLYLLHWPDcpSSGKnvketrAETWRALEELYDEGLCRAIGVSNFLIEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 215 LRDAYERLkkrGVPLASNQVNYSlIYRNPEEngVKAACDELGITLIAYSPIAQGvltgkytpnnpptgprgriytpeflt 294
Cdd:cd19135 151 LEQLLEDC---SVVPHVNQVEFH-PFQNPVE--LIEYCRDNNIVFEGYCPLAKG-------------------------- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286311 295 klQPLIN-RIKEIGGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSM 362
Cdd:cd19135 199 --KALEEpTVTELAKKYQKTPAQILIRWSI-QNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
63-361 |
5.19e-33 |
|
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: 124.70 E-value: 5.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 63 LGIGAWSWGDttywnefqwDDRKLKAAKGAFDAsvdcGITFFDTAEVYGagisgainSESLLGRFIKERQQKEQV---EV 139
Cdd:cd19116 14 IALGTWKLKD---------DEGVRQAVKHAIEA----GYRHIDTAYLYG--------NEAEVGEAIREKIAEGVVkreDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 140 AIATKFaalpWRL--GRGSVISALKDSLSRLGVSSVELYQLHWP--------------GIWGNEGYLD---GLGDAYEQG 200
Cdd:cd19116 73 FITTKL----WNSyhEREQVEPALRESLKRLGLDYVDLYLIHWPvafkenndsesngdGSLSDIDYLEtwrGMEDLVKLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 201 LVKAVGVSNYSEKRLRDAYERLKkrgVPLASNQVNYSLIYRNPEengVKAACDELGITLIAYSPIAQGVLTGKytPNNPP 280
Cdd:cd19116 149 LTRSIGVSNFNSEQINRLLSNCN---IKPAVNQIEVHPTLTQEK---LVAYCQSNGIVVMAYSPFGRLVPRGQ--TNPPP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 281 tgprgRIYTPefltklqplinRIKEIGGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELR 360
Cdd:cd19116 221 -----RLDDP-----------TLVAIAKKYGKTTAQIVLRYLI-DRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALN 283
|
.
gi 1002286311 361 S 361
Cdd:cd19116 284 S 284
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
49-359 |
5.71e-33 |
|
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: 124.85 E-value: 5.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 49 GKVRLGGSDVAVTKLGIGAWswGDTTYWNEFQWDDRKLKAAKGAFDasvdCGITFFDTAEVYGAGisgaiNSESLLGRFI 128
Cdd:cd19145 1 PRVKLGSQGLEVSAQGLGCM--GLSGDYGAPKPEEEGIALIHHAFN----SGVTFLDTSDIYGPN-----TNEVLLGKAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 129 KErQQKEQVEvaIATKFAAL----PWRLGRGS---VISALKDSLSRLGVSSVELYQLHW-----PgIWGNEGYLDGLgda 196
Cdd:cd19145 70 KD-GPREKVQ--LATKFGIHeiggSGVEVRGDpayVRAACEASLKRLDVDYIDLYYQHRidttvP-IEITMGELKKL--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 197 YEQGLVKAVGVSNYSEKRLRDAYerlkkrGV-PLASNQVNYSLIYRNPEENgVKAACDELGITLIAYSPIAQGVLTGKYT 275
Cdd:cd19145 143 VEEGKIKYIGLSEASADTIRRAH------AVhPITAVQLEWSLWTRDIEEE-IIPTCRELGIGIVPYSPLGRGFFAGKAK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 276 PNNPPTGPRGRIYTPEF----LTKLQPLINRIKEIGGSYEKTPTQVVLNWLICQGN-VVPIPGAKNAEQAREFAGALGWS 350
Cdd:cd19145 216 LEELLENSDVRKSHPRFqgenLEKNKVLYERVEALAKKKGCTPAQLALAWVLHQGEdVVPIPGTTKIKNLNQNIGALSVK 295
|
....*....
gi 1002286311 351 LTDQEVEEL 359
Cdd:cd19145 296 LTKEDLKEI 304
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
84-362 |
2.67e-32 |
|
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: 121.97 E-value: 2.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 84 RKLKAAKGAFDASVDCGITFFDTAEVYGagisgainSESLLGRFIKERQQKEQV---EVAIATKFAalPWRLGRGSVISA 160
Cdd:cd19136 12 RGEEEVRQAVDAALKAGYRLIDTASVYR--------NEADIGKALRDLLPKYGLsreDIFITSKLA--PKDQGYEKARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 161 LKDSLSRLGVSSVELYQLHWPGIWG-------NEGYLDG----LGDAYEQGLVKAVGVSNYSEKRLRdayERLKKRGVPL 229
Cdd:cd19136 82 CLGSLERLGTDYLDLYLIHWPGVQGlkpsdprNAELRREswraLEDLYKEGKLRAIGVSNYTVRHLE---ELLKYCEVPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 230 ASNQVNYSLIYRNPEengVKAACDELGITLIAYSPIaqGVLTGKYTPNNPptgprgriytpefltklqplinrIKEIGGS 309
Cdd:cd19136 159 AVNQVEFHPHLVQKE---LLKFCKDHGIHLQAYSSL--GSGDLRLLEDPT-----------------------VLAIAKK 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1002286311 310 YEKTPTQVVLNWLICQGNVVpIPGAKNAEQAREFAGALGWSLTDQEVEELRSM 362
Cdd:cd19136 211 YGRTPAQVLLRWALQQGIGV-IPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
76-348 |
1.08e-31 |
|
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: 121.79 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 76 WNEFQwDDRKLKAAKGAFDASVDCGITFFDTAEVYGAGISGAinsESLLGRFIKERQQKEQVEVAIATK--FAALPWRLG 153
Cdd:cd19150 20 WHNFG-DDTPLETQRAILRTAFDLGITHFDLANNYGPPPGSA---EENFGRILREDFAGYRDELIISTKagYDMWPGPYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 154 ----RGSVISALKDSLSRLGVSSVELYQLH-----WPgiwgNEGYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAYERLKK 224
Cdd:cd19150 96 ewgsRKYLLASLDQSLKRMGLDYVDIFYSHrfdpdTP----LEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 225 RGVPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGKYTpNNPPTGPR---GRIYTPEFLTKLQ-PLI 300
Cdd:cd19150 172 LGTPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYL-NGIPEGSRaskERSLSPKMLTEANlNSI 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1002286311 301 NRIKEIGGSYEKTPTQVVLNWLICQGNVVP-IPGAKNAEQAREFAGALG 348
Cdd:cd19150 251 RALNEIAQKRGQSLAQMALAWVLRDGRVTSaLIGASRPEQLEENVGALD 299
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
50-364 |
1.55e-31 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 121.03 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 50 KVRLGGSDVAVTKLGIGAWSWGDTtywnefqwdDRKLKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIK 129
Cdd:COG4989 3 RIKLGASGLSVSRIVLGCMRLGEW---------DLSPAEAAALIEAALELGITTFDHADIYGGY-----TCEALFGEALK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 130 ERQQK-EQVEvaIATKF------AALPWRLG-----RGSVISALKDSLSRLGVSSVELYQLHWPgiwgnegylDGLGDA- 196
Cdd:COG4989 69 LSPSLrEKIE--LQTKCgirlpsEARDNRVKhydtsKEHIIASVEGSLRRLGTDYLDLLLLHRP---------DPLMDPe 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 197 ---------YEQGLVKAVGVSNYSekrlRDAYERLKKR-GVPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIA 266
Cdd:COG4989 138 evaeafdelKASGKVRHFGVSNFT----PSQFELLQSAlDQPLVTNQIELSLLHTDAFDDGTLDYCQLNGITPMAWSPLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 267 QGVLTGKYTPNNPptgprgriytpefltklqPLINRIKEIGGSYEKTPTQVVLNWLICQ-GNVVPIPGAKNAEQAREFAG 345
Cdd:COG4989 214 GGRLFGGFDEQFP------------------RLRAALDELAEKYGVSPEAIALAWLLRHpAGIQPVIGTTNPERIKAAAA 275
|
330
....*....|....*....
gi 1002286311 346 ALGWSLTDQEVEELRSMAR 364
Cdd:COG4989 276 ALDIELTREEWYELYEAAR 294
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
52-347 |
2.21e-31 |
|
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: 120.83 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 52 RLGGSDVAVTKLGIGAWS-WGDTTYWNEFqwddRKLkaAKGAFDAsvdcGITFFDTAEVYGaGISGAInsESLLGRFIKE 130
Cdd:cd19089 3 RCGRSGLHLPAISLGLWHnFGDYTSPEEA----REL--LRTAFDL----GITHFDLANNYG-PPPGSA--EENFGRILKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 131 RQQKEQVEVAIATK--FAALPWRLGRGS----VISALKDSLSRLGVSSVELYQLHWPGiwGN---EGYLDGLGDAYEQGL 201
Cdd:cd19089 70 DLRPYRDELVISTKagYGMWPGPYGDGGsrkyLLASLDQSLKRMGLDYVDIFYHHRYD--PDtplEETMTALADAVRSGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 202 VKAVGVSNYSEKRLRDAYERLKKRGVPLASNQVNYSLIYRNPEEnGVKAACDELGITLIAYSPIAQGVLTGKYTPNNPPT 281
Cdd:cd19089 148 ALYVGISNYPGAKARRAIALLRELGVPLIIHQPRYSLLDRWAED-GLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPD 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286311 282 GPRGRI--------YTPEFLTKLQplinRIKEIGGSYEKTPTQVVLNWLICQGNV--VPIpGAKNAEQAREFAGAL 347
Cdd:cd19089 227 SRRAAEskflteeaLTPEKLEQLR----KLNKIAAKRGQSLAQLALSWVLRDPRVtsVLI-GASSPSQLEDNVAAL 297
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
63-347 |
1.50e-29 |
|
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: 115.73 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 63 LGIGAWSWGDTTYWNEfqwddrklkAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFikerqQKEQVEVAIA 142
Cdd:cd19075 5 LGTMTFGSQGRFTTAE---------AAAELLDAFLERGHTEIDTARVYPDG-----TSEELLGEL-----GLGERGFKID 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 143 TKfaALPW---RLGRGSVISALKDSLSRLGVSSVELYQLHWPG----IwgnEGYLDGLGDAYEQGLVKAVGVSNYSEKRL 215
Cdd:cd19075 66 TK--ANPGvggGLSPENVRKQLETSLKRLKVDKVDVFYLHAPDrstpL---EETLAAIDELYKEGKFKEFGLSNYSAWEV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 216 RDAYERLKKRGVPLAS-NQVNYSLIYRNPEENgVKAACDELGITLIAYSPIAQGVLTGKYTP-NNPPTGPR-------GR 286
Cdd:cd19075 141 AEIVEICKENGWVLPTvYQGMYNAITRQVETE-LFPCLRKLGIRFYAYSPLAGGFLTGKYKYsEDKAGGGRfdpnnalGK 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286311 287 IYTPEFLTK-LQPLINRIKEIGGSYEKTPTQVVLNWLI-------CQGNVVpIPGAKNAEQAREFAGAL 347
Cdd:cd19075 220 LYRDRYWKPsYFEALEKVEEAAEKEGISLAEAALRWLYhhsaldgEKGDGV-ILGASSLEQLEENLAAL 287
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
62-362 |
2.78e-27 |
|
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: 108.29 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 62 KLGIGAWswgdttywnEFQWDDRKLKAAKGAfdasVDCGITFFDTAEVYgagisgaiNSESLLGRFIKERQQKEQvEVAI 141
Cdd:cd19126 11 WLGLGVF---------QTPDGDETERAVQTA----LENGYRSIDTAAIY--------KNEEGVGEAIRESGVPRE-ELFV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 142 ATKFAALPWRLGRGSviSALKDSLSRLGVSSVELYQLHWPGIWGNEGYLDGLGDAYEQGLVKAVGVSNYSEKRLRdayER 221
Cdd:cd19126 69 TTKLWNDDQRARRTE--DAFQESLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLE---EL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 222 LKKRGVPLASNQVNYSLIYRNPEengVKAACDELGITLIAYSPIAQGVLTgkytpNNPptgprgriytpefltklqplin 301
Cdd:cd19126 144 LAHADVVPAVNQVEFHPYLTQKE---LRGYCKSKGIVVEAWSPLGQGGLL-----SNP---------------------- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002286311 302 RIKEIGGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSM 362
Cdd:cd19126 194 VLAAIGEKYGKSAAQVVLRWDI-QHGVVTIPKSVHASRIKENADIFDFELSEDDMTAIDAL 253
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
94-348 |
3.21e-27 |
|
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: 108.96 E-value: 3.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 94 DASVDCGITFFDTAEVYGAGISGAI--NSESLLGRFIKERQQKEqvEVAIATKFAALPWR----------LGRGSVISAL 161
Cdd:cd19752 24 DRYVAAGGNFLDTANNYAFWTEGGVggESERLIGRWLKDRGNRD--DVVIATKVGAGPRDpdggpespegLSAETIEQEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 162 KDSLSRLGVSSVELYQLH-----WPgiwgNEGYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAYERLKKRGVPLASN-QVN 235
Cdd:cd19752 102 DKSLRRLGTDYIDLYYAHvddrdTP----LEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWAEFSAiQQR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 236 YSLIYRNP--EENGVKAACDEL--------GITLIAYSPIaqgvLTGKYTPNNPPTGPRGRiyTPEFLTKLQplinRIKE 305
Cdd:cd19752 178 HSYLRPRPgaDFGVQRIVTDELldyassrpDLTLLAYSPL----LSGAYTRPDRPLPEQYD--GPDSDARLA----VLEE 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1002286311 306 IGGSYEKTPTQVVLNWLICQ-GNVVPIPGAKNAEQAREFAGALG 348
Cdd:cd19752 248 VAGELGATPNQVVLAWLLHRtPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
52-360 |
1.16e-26 |
|
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: 107.87 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 52 RLGGSDVAVTKLGIGAW-SWGDTT-YWNEfqwddRKLkaAKGAFDAsvdcGITFFDTAEVYGAGISGAinsESLLGRFIK 129
Cdd:cd19151 4 RCGRSGLKLPAISLGLWhNFGDVDrYENS-----RAM--LRRAFDL----GITHFDLANNYGPPPGSA---EENFGRILK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 130 ERQQKEQVEVAIATKFAALPWRLGRGS------VISALKDSLSRLGVSSVELYQLHWPG----IwgnEGYLDGLGDAYEQ 199
Cdd:cd19151 70 EDLKPYRDELIISTKAGYTMWPGPYGDwgskkyLIASLDQSLKRMGLDYVDIFYHHRPDpetpL---EETMGALDQIVRQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 200 GLVKAVGVSNYSEKRLRDAYERLKKRGVPLASNQVNYSLIYRNPEEnGVKAACDELGITLIAYSPIAQGVLTGKY---TP 276
Cdd:cd19151 147 GKALYVGISNYPPEEAREAAAILKDLGTPCLIHQPKYSMFNRWVEE-GLLDVLEEEGIGCIAFSPLAQGLLTDRYlngIP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 277 NNPPTGPRGRIY-----TPEFLTKlqplINRIKEIGGSYEKTPTQVVLNWLICQGNVVP-IPGAKNAEQAREFAGALgwS 350
Cdd:cd19151 226 EDSRAAKGSSFLkpeqiTEEKLAK----VRRLNEIAQARGQKLAQMALAWVLRNKRVTSvLIGASKPSQIEDAVGAL--D 299
|
330
....*....|
gi 1002286311 351 LTDQEVEELR 360
Cdd:cd19151 300 NREFSEEELA 309
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
61-346 |
7.96e-26 |
|
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: 104.24 E-value: 7.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 61 TKLGIGAWSWGDTtywnefqWDDRKLKAAKGAFDASVDCGITFFDTAEVYGagisgaiNSESLLGRFIKERQQKEQVeva 140
Cdd:cd19095 1 SVLGLGTSGIGRV-------WGVPSEAEAARLLNTALDLGINLIDTAPAYG-------RSEERLGRALAGLRRDDLF--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 141 IATKfAALPWRLGRGS-------VISALKDSLSRLGVSSVELYQLHWPGIW-GNEGYLDGLGDAYEQGLVKAVGVSNYSE 212
Cdd:cd19095 64 IATK-VGTHGEGGRDRkdfspaaIRASIERSLRRLGTDYIDLLQLHGPSDDeLTGEVLETLEDLKAAGKVRYIGVSGDGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 213 kRLRDAyerlkkrgvpLASN-----QVNYSLIyrNPEENGVKAACDELGITLIAYSPIAQGVLTGKYTPNNPPTGPRGRi 287
Cdd:cd19095 143 -ELEAA----------IASGvfdvvQLPYNVL--DREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARR- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 288 ytPEFLTklqplinrikEIGGsyeKTPTQVVLNWLICQGNV-VPIPGAKNAEQAREFAGA 346
Cdd:cd19095 209 --PEFAA----------EIGG---ATWAQAALRFVLSHPGVsSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
105-359 |
1.99e-25 |
|
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: 103.20 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 105 DTAEVYGagisgainSESLLGRFIKERQQKEQvEVAIATKFaalpW--RLGRGSVISALKDSLSRLGVSSVELYQLHWPG 182
Cdd:cd19139 32 DTAQIYD--------NEAAVGQAIAESGVPRD-ELFITTKI----WidNLSKDKLLPSLEESLEKLRTDYVDLTLIHWPS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 183 IWGN---EGYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAYERLKKRGVplASNQVNYSLIYRNPeenGVKAACDELGITL 259
Cdd:cd19139 99 PNDEvpvEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAI--ATNQIELSPYLQNR---KLVAHCKQHGIHV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 260 IAYSPIAQGVLTGKytpnnpPTgprgriytpefltklqplinrIKEIGGSYEKTPTQVVLNWLICQGNVVpIPGAKNAEQ 339
Cdd:cd19139 174 TSYMTLAYGKVLDD------PV---------------------LAAIAERHGATPAQIALAWAMARGYAV-IPSSTKREH 225
|
250 260
....*....|....*....|
gi 1002286311 340 AREFAGALGWSLTDQEVEEL 359
Cdd:cd19139 226 LRSNLLALDLTLDADDMAAI 245
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
54-366 |
2.90e-25 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 104.69 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 54 GGSDVAVTKLGIGAW-SWGDTtywnefqwddRKLKAAKGAFDASVDCGITFFDTAEVYGAGISGAinsESLLGRFIKERQ 132
Cdd:PRK09912 19 GKSGLRLPALSLGLWhNFGHV----------NALESQRAILRKAFDLGITHFDLANNYGPPPGSA---EENFGRLLREDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 133 QKEQVEVAIATK--FAALPWRLGRGS----VISALKDSLSRLGVSSVELYQLHwpGIWGN---EGYLDGLGDAYEQGLVK 203
Cdd:PRK09912 86 AAYRDELIISTKagYDMWPGPYGSGGsrkyLLASLDQSLKRMGLEYVDIFYSH--RVDENtpmEETASALAHAVQSGKAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 204 AVGVSNYSEKRLRDAYERLKKRGVPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGKYTpNNPPTGP 283
Cdd:PRK09912 164 YVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYL-NGIPQDS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 284 R-------GRIYTPEFLTKLQ----PLINRIKEIGGsyeKTPTQVVLNWLICQGNVVPI-PGAKNAEQAREFAGALGwSL 351
Cdd:PRK09912 243 RmhregnkVRGLTPKMLTEANlnslRLLNEMAQQRG---QSMAQMALSWLLKDERVTSVlIGASRAEQLEENVQALN-NL 318
|
330
....*....|....*
gi 1002286311 352 TDQEvEELRSMAREI 366
Cdd:PRK09912 319 TFST-EELAQIDQHI 332
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
85-364 |
2.91e-25 |
|
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: 102.73 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 85 KLKAAKG--AFDASVDCGITFFDTAEVYGagisgainSESLLGRFIKeRQQKEQVEVAIATKfaaLPWRL-GRGSVISAL 161
Cdd:cd19132 16 PLKGDEGveAVVAALQAGYRLLDTAFNYE--------NEGAVGEAVR-RSGVPREELFVTTK---LPGRHhGYEEALRTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 162 KDSLSRLGVSSVELYQLHWPGIwGNEGYLD---GLGDAYEQGLVKAVGVSNYSEKRLrdayERL-KKRGVPLASNQVNYS 237
Cdd:cd19132 84 EESLYRLGLDYVDLYLIHWPNP-SRDLYVEawqALIEAREEGLVRSIGVSNFLPEHL----DRLiDETGVTPAVNQIELH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 238 lIYRNPEEngVKAACDELGITLIAYSPIAQG--VLtgkytpNNPPtgprgriytpefltklqplinrIKEIGGSYEKTPT 315
Cdd:cd19132 159 -PYFPQAE--QRAYHREHGIVTQSWSPLGRGsgLL------DEPV----------------------IKAIAEKHGKTPA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1002286311 316 QVVLNWLICQGnVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSMAR 364
Cdd:cd19132 208 QVVLRWHVQLG-VVPIPKSANPERQRENLAIFDFELSDEDMAAIAALDR 255
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
70-365 |
3.63e-25 |
|
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: 103.08 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 70 WGDTTYWNEFQWD--DRKL-KAAKGAFDAsvdcGITFFDTAEVYGagisgainSESLLGRFIKERQQKEQvEVAIATKfa 146
Cdd:cd19120 9 FGTGTAWYKSGDDdiQRDLvDSVKLALKA----GFRHIDTAEMYG--------NEKEVGEALKESGVPRE-DLFITTK-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 147 alpWRLGRGSVISALKDSLSRLGVSSVELYQLHWPGIWGNEGY-LDG----LGDAYEQGLVKAVGVSNYsekRLRDAYER 221
Cdd:cd19120 74 ---VSPGIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEGGPtLAEawaeLEALKDAGLVRSIGVSNF---RIEDLEEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 222 LKKRGVPLASNQVNYSlIYRNPEENGVKAACDELGITLIAYSPIAqgvltgkytpnnPPTGPRGRiytpefltklqPLIN 301
Cdd:cd19120 148 LDTAKIKPAVNQIEFH-PYLYPQQPALLEYCREHGIVVSAYSPLS------------PLTRDAGG-----------PLDP 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286311 302 RIKEIGGSYEKTPTQVVLNWLICQGnVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSMARE 365
Cdd:cd19120 204 VLEKIAEKYGVTPAQVLLRWALQKG-IVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQ 266
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
58-362 |
4.50e-25 |
|
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: 102.45 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 58 VAVTKLGIGAWswgdttywnefQWDDRKlkaAKGAFDASVDCGITFFDTAEVYGagisgainSESLLGRFIKERQQKEQv 137
Cdd:cd19131 8 NTIPQLGLGVW-----------QVSNDE---AASAVREALEVGYRSIDTAAIYG--------NEEGVGKAIRASGVPRE- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 138 EVAIATKFaalpWR--LGRGSVISALKDSLSRLGVSSVELYQLHWPgIWGNEGYLD---GLGDAYEQGLVKAVGVSNYSE 212
Cdd:cd19131 65 ELFITTKL----WNsdQGYDSTLRAFDESLRKLGLDYVDLYLIHWP-VPAQDKYVEtwkALIELKKEGRVKSIGVSNFTI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 213 KRLrdayERLKKR-GVPLASNQVNYSLIYRNPEengVKAACDELGITLIAYSPIAQGVLTgkytpNNPptgprgriytpe 291
Cdd:cd19131 140 EHL----QRLIDEtGVVPVVNQIELHPRFQQRE---LRAFHAKHGIQTESWSPLGQGGLL-----SDP------------ 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002286311 292 fltklqplinRIKEIGGSYEKTPTQVVLNWLICQGNVVpIPGAKNAEQAREFAGALGWSLTDQEVEELRSM 362
Cdd:cd19131 196 ----------VIGEIAEKHGKTPAQVVIRWHLQNGLVV-IPKSVTPSRIAENFDVFDFELDADDMQAIAGL 255
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
87-342 |
9.68e-25 |
|
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: 101.84 E-value: 9.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 87 KAAKGAFDASVDCGITFFDTAEVYGagisgaiNSESLLGRFIKERQQkeqveVAIATKFAALPWRLGRG--SVISALKDS 164
Cdd:cd19097 26 KEAKKILEYALKAGINTLDTAPAYG-------DSEKVLGKFLKRLDK-----FKIITKLPPLKEDKKEDeaAIEASVEAS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 165 LSRLGVSSVELYQLHWPGIW--GNEGYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAYERLKKRGVplasnQVNYSLIYRN 242
Cdd:cd19097 94 LKRLKVDSLDGLLLHNPDDLlkHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDII-----QLPFNILDQR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 243 PEENGVKAACDELGITLIAYSPIAQGVLTGKytPNNPptgprgriytPEFLTKLQPLINRIKEIGGSYEKTPTQVVLNWL 322
Cdd:cd19097 169 FLKSGLLAKLKKKGIEIHARSVFLQGLLLME--PDKL----------PAKFAPAKPLLKKLHELAKKLGLSPLELALGFV 236
|
250 260
....*....|....*....|....
gi 1002286311 323 ICQGN----VVpipGAKNAEQARE 342
Cdd:cd19097 237 LSLPEidkiVV---GVDSLEQLKE 257
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
50-273 |
9.84e-25 |
|
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: 101.02 E-value: 9.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 50 KVRLGGSDVAVTKLGIGAWSWGDTTYwnefqwddrklKAAKGAFDASVDCGITFFDTAEVYGagisgaiNSESLLGRFIK 129
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRLSQ-----------EEAAAIIRRALDLGINYFDTAPSYG-------DSEEKIGKALK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 130 ERQQKeqveVAIATKFAAlpwrLGRGSVISALKDSLSRLGVSSVELYQLH-------WPGIWGNEGYLDGLGDAYEQGLV 202
Cdd:cd19100 63 GRRDK----VFLATKTGA----RDYEGAKRDLERSLKRLGTDYIDLYQLHavdteedLDQVFGPGGALEALLEAKEEGKI 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002286311 203 KAVGVSNYSEKRLRDAYERLkkrgvPLASNQ--VNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGK 273
Cdd:cd19100 135 RFIGISGHSPEVLLRALETG-----EFDVVLfpINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSG 202
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
52-361 |
5.67e-24 |
|
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: 100.75 E-value: 5.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 52 RLGGSDVAVTKLGIGAW-SWGDTTywnefqwddrKLKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKE 130
Cdd:cd19143 5 RLGRSGLKVSALSFGSWvTFGNQV----------DVDEAKECMKAAYDAGVNFFDNAEVYANG-----QSEEIMGQAIKE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 131 RQQKEQvEVAIATKF---AALPWR----LGRGSVISALKDSLSRLGVSSVELYQLHWPGIWGN-EGYLDGLGDAYEQGLV 202
Cdd:cd19143 70 LGWPRS-DYVVSTKIfwgGGGPPPndrgLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPiEETVRAMNDLIDQGKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 203 KAVGVSNYSEKRLRDAYERLKKRG-VPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGKYTpNNPPT 281
Cdd:cd19143 149 FYWGTSEWSAQQIEEAHEIADRLGlIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYN-NGIPE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 282 GPRGRIYTPEFLTKLQPL--------INRIKEIGGSYEKTPTQVVLNWLICQGNV--VpIPGAKNAEQAREFAGALGW-- 349
Cdd:cd19143 228 GSRLALPGYEWLKDRKEElgqekiekVRKLKPIAEELGCSLAQLAIAWCLKNPNVstV-ITGATKVEQLEENLKALEVlp 306
|
330
....*....|..
gi 1002286311 350 SLTDQEVEELRS 361
Cdd:cd19143 307 KLTPEVMEKIEA 318
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
105-362 |
1.23e-22 |
|
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: 95.92 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 105 DTAEVYGagisgainSESLLGRFIKErQQKEQVEVAIATKFaalpWR--LGRGSVISALKDSLSRLGVSSVELYQLHWPG 182
Cdd:cd19157 42 DTAAIYG--------NEEGVGKGIKE-SGIPREELFITSKV----WNadQGYDSTLKAFEASLERLGLDYLDLYLIHWPV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 183 IWGNEGYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAyerLKKRGVPLASNQVNYSLIYRNPEengVKAACDELGITLIAY 262
Cdd:cd19157 109 KGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDL---LADAEIVPMVNQVEFHPRLTQKE---LRDYCKKQGIQLEAW 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 263 SPIAQGVLTGKYTpnnpptgprgriytpefltklqplinrIKEIGGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEQARE 342
Cdd:cd19157 183 SPLMQGQLLDNPV---------------------------LKEIAEKYNKSVAQVILRWDL-QNGVVTIPKSIKEHRIIE 234
|
250 260
....*....|....*....|
gi 1002286311 343 FAGALGWSLTDQEVEELRSM 362
Cdd:cd19157 235 NADVFDFELSQEDMDKIDAL 254
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
91-356 |
5.65e-22 |
|
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: 94.01 E-value: 5.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 91 GAFDASVDCGITFFDTAEVYGagisgainSESLLGRFIKeRQQKEQVEVAIATKFaalpW--RLGRGSVISALKDSLSRL 168
Cdd:cd19127 26 DAVATALADGYRLIDTAAAYG--------NEREVGEGIR-RSGVDRSDIFVTTKL----WisDYGYDKALRGFDASLRRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 169 GVSSVELYQLHWP--GIWGN--EGYLDgLGDAYEQGLVKAVGVSNYSEKRLrdayERLKKR-GVPLASNQVNYSLIYRNP 243
Cdd:cd19127 93 GLDYVDLYLLHWPvpNDFDRtiQAYKA-LEKLLAEGRVRAIGVSNFTPEHL----ERLIDAtTVVPAVNQVELHPYFSQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 244 EengVKAACDELGITLIAYSPIAqGVLTgkYTPNNPPTGPRgriytpefltklqPLINR-IKEIGGSYEKTPTQVVLNWL 322
Cdd:cd19127 168 D---LRAFHRRLGIVTQAWSPIG-GVMR--YGASGPTGPGD-------------VLQDPtITGLAEKYGKTPAQIVLRWH 228
|
250 260 270
....*....|....*....|....*....|....
gi 1002286311 323 ICQGnVVPIPGAKNAEQAREFAGALGWSLTDQEV 356
Cdd:cd19127 229 LQNG-VSAIPKSVHPERIAENIDIFDFALSAEDM 261
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
104-360 |
6.80e-22 |
|
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: 94.26 E-value: 6.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 104 FDTAEVYGagisgainSESLLGRFIKERQQKEQV----EVAIATKfaalPW--RLGRGSVISALKDSLSRLGVSSVELYQ 177
Cdd:cd19124 37 FDTAAAYG--------TEEALGEALAEALRLGLVksrdELFVTSK----LWcsDAHPDLVLPALKKSLRNLQLEYVDLYL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 178 LHWP-----------------------GIWgnegylDGLGDAYEQGLVKAVGVSNYSEKRLRDAYERLKkrgVPLASNQV 234
Cdd:cd19124 105 IHWPvslkpgkfsfpieeedflpfdikGVW------EAMEECQRLGLTKAIGVSNFSCKKLQELLSFAT---IPPAVNQV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 235 NYSLIYRNPEengVKAACDELGITLIAYSPiaqgvLTGKYTpnnpPTGPRGRIYTPefltklqplinRIKEIGGSYEKTP 314
Cdd:cd19124 176 EMNPAWQQKK---LREFCKANGIHVTAYSP-----LGAPGT----KWGSNAVMESD-----------VLKEIAAAKGKTV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1002286311 315 TQVVLNWLICQGNVVpIPGAKNAEQAREFAGALGWSLTDQEVEELR 360
Cdd:cd19124 233 AQVSLRWVYEQGVSL-VVKSFNKERMKQNLDIFDWELTEEDLEKIS 277
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
85-364 |
9.34e-22 |
|
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: 94.02 E-value: 9.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 85 KLKAAKG--AFDASVDCGITFFDTAEVYgagisgaiNSESLLGRFIKERQQKEQV---EVAIATKFAalPWRLGRGSVIS 159
Cdd:cd19154 21 QSKGAEGitAVRTALKAGYRLIDTAFLY--------QNEEAIGEALAELLEEGVVkreDLFITTKLW--THEHAPEDVEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 160 ALKDSLSRLGVSSVELYQLHWPgiWG----------NEGYLD------------GLGDAYEQGLVKAVGVSNYSEKRLRD 217
Cdd:cd19154 91 ALRESLKKLQLEYVDLYLIHAP--AAfkddegesgtMENGMSihdavdvedvwrGMEKVYDEGLTKAIGVSNFNNDQIQR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 218 AYERLKkrgVPLASNQVNYSLIYRNPEengVKAACDELGITLIAYSPIaqgvltGKYTPNNPPTgPRGRIYTPEFLtkLQ 297
Cdd:cd19154 169 ILDNAR---VKPHNNQVECHLYFPQKE---LVEFCKKHNISVTSYATL------GSPGRANFTK-STGVSPAPNLL--QD 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002286311 298 PLinrIKEIGGSYEKTPTQVVLNWLICQGNVVpIPGAKNAEQAREFAGALGWSLTDQEVEELRSMAR 364
Cdd:cd19154 234 PI---VKAIAEKHGKTPAQVLLRYLLQRGIAV-IPKSATPSRIKENFNIFDFSLSEEDMATLEEIEK 296
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
58-362 |
1.17e-21 |
|
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: 93.35 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 58 VAVTKLGIGAWSWGDttywnefqwDDRKLKAAKGAFDAsvdcGITFFDTAEVYGagisgaiNSESLlGRFIKERQQKEQv 137
Cdd:cd19156 7 VEMPRLGLGVWRVQD---------GAEAENAVKWAIEA----GYRHIDTAAIYK-------NEEGV-GQGIRESGVPRE- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 138 EVAIATKFaalpWRLGRG--SVISALKDSLSRLGVSSVELYQLHWPgiwGNEGYLD---GLGDAYEQGLVKAVGVSNYSE 212
Cdd:cd19156 65 EVFVTTKL----WNSDQGyeSTLAAFEESLEKLGLDYVDLYLIHWP---VKGKFKDtwkAFEKLYKEKKVRAIGVSNFHE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 213 KRLRDAYERLKKRgvPLAsNQVN-YSLIYRNPeengVKAACDELGITLIAYSPIAQGVLTgkytpNNPptgprgriytpe 291
Cdd:cd19156 138 HHLEELLKSCKVA--PMV-NQIElHPLLTQEP----LRKFCKEKNIAVEAWSPLGQGKLL-----SNP------------ 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002286311 292 fltklqplinRIKEIGGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSM 362
Cdd:cd19156 194 ----------VLKAIGKKYGKSAAQVIIRWDI-QHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGL 253
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
61-351 |
1.28e-21 |
|
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: 93.39 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 61 TKLGIGAWSWGDTtywnefqWDDRKLKAAKGAFDASVDCGITFFDTAEVYGagisgaiNSESLLGRFIKERQQKEQVeva 140
Cdd:cd19090 1 SALGLGTAGLGGV-------FGGVDDDEAVATIRAALDLGINYIDTAPAYG-------DSEERLGLALAELPREPLV--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 141 IATKFAALP---WRLGRGSVISALKDSLSRLGVSSVELYQLH------WPGIWGNEGYLDGLGDAYEQGLVKAVGVSNYS 211
Cdd:cd19090 64 LSTKVGRLPedtADYSADRVRRSVEESLERLGRDRIDLLMIHdpervpWVDILAPGGALEALLELKEEGLIKHIGLGGGP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 212 EKRLRDAyerlkkrgvpLASNQV-------NYSLIYRNPEENgVKAACDELGITLIAYSPIAQGVLTGKYtPNNPPTGPR 284
Cdd:cd19090 144 PDLLRRA----------IETGDFdvvltanRYTLLDQSAADE-LLPAAARHGVGVINASPLGMGLLAGRP-PERVRYTYR 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002286311 285 GRiyTPEFLTKLQplinRIKEIGGSYEKTPTQVVLNWLICQGNV-VPIPGAKNAEQAREFAGALGWSL 351
Cdd:cd19090 212 WL--SPELLDRAK----RLYELCDEHGVPLPALALRFLLRDPRIsTVLVGASSPEELEQNVAAAEGPL 273
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
89-362 |
2.12e-21 |
|
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: 92.79 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 89 AKGAFDASVDCGITFFDTAEVYGAGIS-GAINSESLLGRFIKERqqkeqvEVAIATKFaalpWR--LGRGSVISALKDSL 165
Cdd:cd19125 26 VGNAVKTAIKEGYRHIDCAAIYGNEKEiGKALKKLFEDGVVKRE------DLFITSKL----WCtdHAPEDVPPALEKTL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 166 SRLGVSSVELYQLHWP-------GIWGNEGYLD--------GLGDAYEQGLVKAVGVSNYSEKRLRDAyerLKKRGVPLA 230
Cdd:cd19125 96 KDLQLDYLDLYLIHWPvrlkkgaHMPEPEEVLPpdipstwkAMEKLVDSGKVRAIGVSNFSVKKLEDL---LAVARVPPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 231 SNQVNYSLIYRNpeeNGVKAACDELGITLIAYSPIaqgvltgkytpnnpptGPRGRIYTPEFLTKLqPLINRIKEiggSY 310
Cdd:cd19125 173 VNQVECHPGWQQ---DKLHEFCKSKGIHLSAYSPL----------------GSPGTTWVKKNVLKD-PIVTKVAE---KL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1002286311 311 EKTPTQVVLNWLICQGNVVpIPGAKNAEQAREFAGALGWSLTDQEVEELRSM 362
Cdd:cd19125 230 GKTPAQVALRWGLQRGTSV-LPKSTNEERIKENIDVFDWSIPEEDFAKFSSI 280
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
63-359 |
3.25e-21 |
|
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: 91.84 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 63 LGIGAWSWGDTTywnefqwddrklkaAKGAFDASVDCGITFFDTAEVYGagisgainSESLLGRFIKeRQQKEQVEVAIA 142
Cdd:cd19134 14 IGLGVGELSDDE--------------AERSVSAALEAGYRLIDTAAAYG--------NEAAVGRAIA-ASGIPRGELFVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 143 TKFAALPwrLGRGSVISALKDSLSRLGVSSVELYQLHWPGiwGNEG-YLD---GLGDAYEQGLVKAVGVSNYSEKRLRDA 218
Cdd:cd19134 71 TKLATPD--QGFTASQAACRASLERLGLDYVDLYLIHWPA--GREGkYVDswgGLMKLREEGLARSIGVSNFTAEHLENL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 219 yerLKKRGVPLASNQVNYSLIYRNPEENGVKAacdELGITLIAYSPIAQGVLTgkytpNNPptgprgriytpefltklqp 298
Cdd:cd19134 147 ---IDLTFFTPAVNQIELHPLLNQAELRKVNA---QHGIVTQAYSPLGVGRLL-----DNP------------------- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002286311 299 linRIKEIGGSYEKTPTQVVLNWLICQGNVVpIPGAKNAEQAREFAGALGWSLTDQEVEEL 359
Cdd:cd19134 197 ---AVTAIAAAHGRTPAQVLLRWSLQLGNVV-ISRSSNPERIASNLDVFDFELTADHMDAL 253
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
52-347 |
5.57e-21 |
|
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: 90.72 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 52 RLGGSDVAVTKLGIGAWSWGDTtywnefqwDDRKLKAAkgafdasVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKER 131
Cdd:cd19105 5 TLGKTGLKVSRLGFGGGGLPRE--------SPELLRRA-------LDLGINYFDTAEGYGNG-----NSEEIIGEALKGL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 132 QQKeqvEVAIATKFAALPWRLGRGSVISALKDSLSRLGVSSVELYQLHWPG----IWGNEGYLDGLGDAYEQGLVKAVGV 207
Cdd:cd19105 65 RRD---KVFLATKASPRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDtpeeRLLNEELLEALEKLKKEGKVRFIGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 208 S--NYSEKRLRDAyerLKKRGVPLAsnQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQgvltgkytpnnpptGPRG 285
Cdd:cd19105 142 SthDNMAEVLQAA---IESGWFDVI--MVAYNFLNQPAELEEALAAAAEKGIGVVAMKTLAG--------------GYLQ 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002286311 286 RIYTPEFLTKlqplinrikeiggsyEKTPTQVVLNWLICQGNV-VPIPGAKNAEQAREFAGAL 347
Cdd:cd19105 203 PALLSVLKAK---------------GFSLPQAALKWVLSNPRVdTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
87-362 |
6.73e-21 |
|
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: 90.71 E-value: 6.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 87 KAAKGAFDAsvdcGITFFDTAEVYGagisgaiNSESLlGRFIKERQQKEQvEVAIATKFaalpW--RLGRGSVISALKDS 164
Cdd:cd19133 27 RAVLEAIKA----GYRLIDTAAAYG-------NEEAV-GRAIKKSGIPRE-ELFITTKL----WiqDAGYEKAKKAFERS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 165 LSRLGVSSVELYQLHWPgiWGN-EGYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAYERLKkrgVPLASNQVNYSLIYrnp 243
Cdd:cd19133 90 LKRLGLDYLDLYLIHQP--FGDvYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNE---VKPAVNQIETHPFN--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 244 EENGVKAACDELGITLIAYSPIAQGvltgkytpnnpptgpRGRIYTPEFLTklqplinrikEIGGSYEKTPTQVVLNWLI 323
Cdd:cd19133 162 QQIEAVEFLKKYGVQIEAWGPFAEG---------------RNNLFENPVLT----------EIAEKYGKSVAQVILRWLI 216
|
250 260 270
....*....|....*....|....*....|....*....
gi 1002286311 324 cQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSM 362
Cdd:cd19133 217 -QRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAAL 254
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
92-367 |
1.38e-20 |
|
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: 91.05 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 92 AFDASVDCGITFFDTAEVYGagisgainSESLLGRFIKERQQKEQV---EVAIATKFAALPWRlgRGSVISALKDSLSRL 168
Cdd:cd19155 30 AVDTALEAGYRHIDTAYVYR--------NEAAIGNVLKKWIDSGKVkreELFIVTKLPPGGNR--REKVEKFLLKSLEKL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 169 GVSSVELYQLHWP-GIWGNE---GYLD------------------GLGDAYEQGLVKAVGVSNYSEKRLRdayERLKKRG 226
Cdd:cd19155 100 QLDYVDLYLIHFPvGSLSKEddsGKLDptgehkqdyttdlldiwkAMEAQVDQGLTRSIGLSNFNREQMA---RILKNAR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 227 VPLASNQVNYSlIYRNPEEngVKAACDELGITLIAYSPIAQGVLTGKYTPNNPPTGPrgriyTPEFLTklqplINRIKEI 306
Cdd:cd19155 177 IKPANLQVELH-VYLQQKD--LVDFCSTHSITVTAYAPLGSPGAAHFSPGTGSPSGS-----SPDLLQ-----DPVVKAI 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002286311 307 GGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSMAREIK 367
Cdd:cd19155 244 AERHGKSPAQVLLRWLM-QRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIR 303
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
52-289 |
2.47e-20 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 91.07 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 52 RLGGSDVAVTKLGIGAWSWGDTTYWNEfqwddrklkaAKGAFDASVDCGITFFDTAEVYGA-------GISgainsESLL 124
Cdd:PRK10625 5 RIPHSSLEVSTLGLGTMTFGEQNSEAD----------AHAQLDYAVAQGINLIDVAEMYPVpprpetqGLT-----ETYI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 125 GRFIKERQQKEQVevAIATKFAAlPWR-----------LGRGSVISALKDSLSRLGVSSVELYQLHWP----GIWGNEGY 189
Cdd:PRK10625 70 GNWLAKRGSREKL--IIASKVSG-PSRnndkgirpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHWPqrptNCFGKLGY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 190 --------------LDGLGDAYEQGLVKAVGVSNYSEKRLRDAYERLKKRGVP-LASNQVNYSLIYRNpEENGVKAACDE 254
Cdd:PRK10625 147 swtdsapavslletLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPrIVTIQNPYSLLNRS-FEVGLAEVSQY 225
|
250 260 270
....*....|....*....|....*....|....*
gi 1002286311 255 LGITLIAYSPIAQGVLTGKYTPNNPPTGPRGRIYT 289
Cdd:PRK10625 226 EGVELLAYSCLAFGTLTGKYLNGAKPAGARNTLFS 260
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
52-362 |
2.47e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 87.71 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 52 RLGGSDVAVTKLGIG----AWSWGDTTywnefqwDDRKLKAAKGAFDAsvdcGITFFDTAEVYGAGIsgainSESLLGRF 127
Cdd:cd19104 4 RFGRTGLKVSELTFGgggiGGLMGRTT-------REEQIAAVRRALDL----GINFFDTAPSYGDGK-----SEENLGRA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 128 IKERQQKeqveVAIATKFAALPWRLGR--GSVISALKDSLSRLGVSSVELYQLH--------WPG--------IWGNEGY 189
Cdd:cd19104 68 LKGLPAG----PYITTKVRLDPDDLGDigGQIERSVEKSLKRLKRDSVDLLQLHnrigderdKPVggtlsttdVLGLGGV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 190 LDGLGDAYEQGLVKAVGVSNYSEKrlrDAYERLKKRGVPlASNQVNYSLI-----------YRNPEENGVKAACDELGIT 258
Cdd:cd19104 144 ADAFERLRSEGKIRFIGITGLGNP---PAIRELLDSGKF-DAVQVYYNLLnpsaaearprgWSAQDYGGIIDAAAEHGVG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 259 LIAYSPIAQGVLTGkyTPNNPPTGP--RGRIYTPEFlTKLQPLINRIKEIGGsyekTPTQVVLNWLICQGNVVP-IPGAK 335
Cdd:cd19104 220 VMGIRVLAAGALTT--SLDRGREAPptSDSDVAIDF-RRAAAFRALAREWGE----TLAQLAHRFALSNPGVSTvLVGVK 292
|
330 340
....*....|....*....|....*....
gi 1002286311 336 NAEQAREF--AGALGwSLTDQEVEELRSM 362
Cdd:cd19104 293 NREELEEAvaAEAAG-PLPAENLARLEAL 320
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
92-367 |
4.71e-19 |
|
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: 86.40 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 92 AFDASVDCGITFFDTAEVYG--AGISGAINsesllgRFIKERQQKEQvEVAIATKfaALPWRLGRGSVISALKDSLSRLG 169
Cdd:cd19111 22 AVDYALFVGYRHIDTALSYQneKAIGEALK------WWLKNGKLKRE-EVFITTK--LPPVYLEFKDTEKSLEKSLENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 170 VSSVELYQLHWPgiWGNEGYLDG----------------LGDAYEQGLVKAVGVSNYSEKRLRDAyerLKKRGVPLASNQ 233
Cdd:cd19111 93 LPYVDLYLIHHP--CGFVNKKDKgerelassdvtsvwraMEALVSEGKVKSIGLSNFNPRQINKI---LAYAKVKPSNLQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 234 VNYSLIYrnpEENGVKAACDELGITLIAYSPIAQGVLTGKYTPnnPPTgprgriytPEFLTklQPLINRI-KEIGgsyeK 312
Cdd:cd19111 168 LECHAYL---QQRELRKFCNKKNIVVTAYAPLGSPGRANQSLW--PDQ--------PDLLE--DPTVLAIaKELD----K 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1002286311 313 TPTQVVLNWLIcQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSMAREIK 367
Cdd:cd19111 229 TPAQVLLRFVL-QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
105-364 |
5.13e-18 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 82.76 E-value: 5.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 105 DTAEVYGagisgainSESLLGRFIKERQQKEQvEVAIATKFaalpW--RLGRGSVISALKDSLSRLGVSSVELYQLHWPG 182
Cdd:PRK11172 34 DTAQIYD--------NEAAVGQAIAESGVPRD-ELFITTKI----WidNLAKDKLIPSLKESLQKLRTDYVDLTLIHWPS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 183 IwGNE----GYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAYERLKKRGVplASNQVNYSLIYRNPEengVKAACDELGIT 258
Cdd:PRK11172 101 P-NDEvsveEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENI--ATNQIELSPYLQNRK---VVAFAKEHGIH 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 259 LIAYSPIAQG-VLTgkytpnnpptgprgriytpefltklQPLinrIKEIGGSYEKTPTQVVLNWLICQGNVVpIPGAKNA 337
Cdd:PRK11172 175 VTSYMTLAYGkVLK-------------------------DPV---IARIAAKHNATPAQVILAWAMQLGYSV-IPSSTKR 225
|
250 260
....*....|....*....|....*..
gi 1002286311 338 EQAREFAGALGWSLTDQEVEELRSMAR 364
Cdd:PRK11172 226 ENLASNLLAQDLQLDAEDMAAIAALDR 252
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
81-339 |
1.48e-17 |
|
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: 81.45 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 81 WDDRK-LKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQKeqvEVAIATKfaaLPWrlgrGSVIS 159
Cdd:cd19096 14 DDDSIdEEKAIEMIRYAIDAGINYFDTAYGYGGG-----KSEEILGEALKEGPRE---KFYLATK---LPP----WSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 160 A------LKDSLSRLGVSSVELYQLH------WPGIWGNEGYLDGLGDAYEQGLVKAVGVS---NYSE-KRLRDAYerlk 223
Cdd:cd19096 79 AedfrriLEESLKRLGVDYIDFYLLHglnspeWLEKARKGGLLEFLEKAKKEGLIRHIGFSfhdSPELlKEILDSY---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 224 krgvPLASNQVNYSLIYRNPEEN--GVKAACdELGITLIAYSPIAQGVLtgkytPNNPptgprgriytPEFLTKLqplin 301
Cdd:cd19096 155 ----DFDFVQLQYNYLDQENQAGrpGIEYAA-KKGMGVIIMEPLKGGGL-----ANNP----------PEALAIL----- 209
|
250 260 270
....*....|....*....|....*....|....*....
gi 1002286311 302 rikeigGSYEKTPTQVVLNWLICQGNV-VPIPGAKNAEQ 339
Cdd:cd19096 210 ------CGAPLSPAEWALRFLLSHPEVtTVLSGMSTPEQ 242
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
100-367 |
1.60e-17 |
|
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: 82.15 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 100 GITFFDTAEVYGagisgainSESLLGRFIKERQQKEQV---EVAIATKFaalpWRLGRGSVISALKDSLSRLGVSSVELY 176
Cdd:cd19112 37 GYRHFDCAADYK--------NEKEVGEALAEAFKTGLVkreDLFITTKL----WNSDHGHVIEACKDSLKKLQLDYLDLY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 177 QLHWPGIW------------GNEGYLD------------GLGDAYEQGLVKAVGVSNYSEKRLRD--AYERLKKrgvplA 230
Cdd:cd19112 105 LVHFPVATkhtgvgttgsalGEDGVLDidvtislettwhAMEKLVSAGLVRSIGISNYDIFLTRDclAYSKIKP-----A 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 231 SNQVNYSLIYRnpEENGVKaACDELGITLIAYSPIAQGVLT----GKYTPNNPPTgprgriytpefltklqplinrIKEI 306
Cdd:cd19112 180 VNQIETHPYFQ--RDSLVK-FCQKHGISVTAHTPLGGAAANaewfGSVSPLDDPV---------------------LKDL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002286311 307 GGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSMAREIK 367
Cdd:cd19112 236 AKKYGKSAAQIVLRWGI-QRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
92-362 |
2.21e-17 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), 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). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 81.11 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 92 AFDASVDCGITFFDTAEVYG--AGISGAINSESLlgrfikERQqkeqvEVAIATKFaalpW--RLGRGSVISALKDSLSR 167
Cdd:cd19130 28 AVATALEVGYRHIDTAAIYGneEGVGAAIAASGI------PRD-----ELFVTTKL----WndRHDGDEPAAAFAESLAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 168 LGVSSVELYQLHWPG--------IWgnegylDGLGDAYEQGLVKAVGVSNYSEKRLrdayERL-KKRGVPLASNQVNYSL 238
Cdd:cd19130 93 LGLDQVDLYLVHWPTpaagnyvhTW------EAMIELRAAGRTRSIGVSNFLPPHL----ERIvAATGVVPAVNQIELHP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 239 IYRNPEengVKAACDELGITLIAYSPIAQGVLTGkytpnnpptgprgriytpefltklQPLINRIKEIGGsyeKTPTQVV 318
Cdd:cd19130 163 AYQQRT---IRDWAQAHDVKIEAWSPLGQGKLLG------------------------DPPVGAIAAAHG---KTPAQIV 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1002286311 319 LNWLICQGNVVpIPGAKNAEQAREFAGALGWSLTDQEVEELRSM 362
Cdd:cd19130 213 LRWHLQKGHVV-FPKSVRRERMEDNLDVFDFDLTDTEIAAIDAL 255
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
53-368 |
1.20e-16 |
|
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: 80.09 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 53 LGGSDVAVTKLGIGAWswgdTTYWNEFQwDDrklkAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQ 132
Cdd:cd19159 6 LGKSGLRVSCLGLGTW----VTFGGQIS-DE----VAERLMTIAYESGVNLFDTAEVYAAG-----KAEVILGSIIKKKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 133 QKEQvEVAIATKF-----AALPWRLGRGSVISALKDSLSRLGVSSVELYQLHWPGiwGN---EGYLDGLGDAYEQGLVKA 204
Cdd:cd19159 72 WRRS-SLVITTKLywggkAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPD--SNtpmEEIVRAMTHVINQGMAMY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 205 VGVSNYSEKRLRDAYERLKKRG-VPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGKYTpNNPPTGP 283
Cdd:cd19159 149 WGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYG-NGVPESS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 284 RGRIYTPEFLT---------KLQpliNRIKEIGGSYEK---TPTQVVLNW-LICQGNVVPIPGAKNAEQAREFAGALGW- 349
Cdd:cd19159 228 RASLKCYQWLKerivseegrKQQ---NKLKDLSPIAERlgcTLPQLAVAWcLRNEGVSSVLLGSSTPEQLIENLGAIQVl 304
|
330 340
....*....|....*....|
gi 1002286311 350 -SLTDQEVEELRSMAREiKP 368
Cdd:cd19159 305 pKMTSHVVNEIDNILRN-KP 323
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
81-367 |
2.72e-16 |
|
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: 78.31 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 81 WDDRKLKAAKgAFDASVDCGITFFDTAEVYGagisgainSESLLGRFIKERQQKEQvEVAIATKFaalpWRLGRGSVISA 160
Cdd:cd19117 22 WQSKPNEVAK-AVEAALKAGYRHIDTAAIYG--------NEEEVGQGIKDSGVPRE-EIFITTKL----WCTWHRRVEEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 161 LKDSLSRLGVSSVELYQLHWP------GIWGNEGYLDGLGDAYEQ----------------GLVKAVGVSNYSEKRLRDA 218
Cdd:cd19117 88 LDQSLKKLGLDYVDLYLMHWPvpldpdGNDFLFKKDDGTKDHEPDwdfiktwelmqklpatGKVKAIGVSNFSIKNLEKL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 219 YERLKKRGVPlASNQVNyslIYRNPEENGVKAACDELGITLIAYSPIAqgvltgkyTPNNPptgprgriytpefLTKLQP 298
Cdd:cd19117 168 LASPSAKIVP-AVNQIE---LHPLLPQPKLVDFCKSKGIHATAYSPLG--------STNAP-------------LLKEPV 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286311 299 LInrikEIGGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEqaREFAGALGWSLTDQEVEELRSMAREIK 367
Cdd:cd19117 223 II----KIAKKHGKTPAQVIISWGL-QRGYSVLPKSVTPS--RIESNFKLFTLSDEEFKEIDELHKEYG 284
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
157-364 |
7.21e-16 |
|
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: 77.07 E-value: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 157 VISALKDSLSRLGVSSVELYQLHWP-----GIWGNEGYLDGLGD--------------AYEQGLVKAVGVSNYSEKRLRD 217
Cdd:cd19123 88 VLPALEKTLADLQLDYLDLYLMHWPvalkkGVGFPESGEDLLSLspipledtwrameeLVDKGLCRHIGVSNFSVKKLED 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 218 AYErlKKRGVPlASNQVNYSLIYRNPEengVKAACDELGITLIAYSPIAQGVltgkytpnnPPTGPRGRiYTPEFLTklQ 297
Cdd:cd19123 168 LLA--TARIKP-AVNQVELHPYLQQPE---LLAFCRDNGIHLTAYSPLGSGD---------RPAAMKAE-GEPVLLE--D 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002286311 298 PLINRIKEIGGSyekTPTQVVLNWLICQGNVVpIPGAKNAEQAREFAGALGWSLTDQEVEELRSMAR 364
Cdd:cd19123 230 PVINKIAEKHGA---SPAQVLIAWAIQRGTVV-IPKSVNPERIQQNLEAAEVELDASDMATIAALDR 292
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
53-359 |
1.11e-15 |
|
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: 76.95 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 53 LGGSDVAVTKLGIGAW-SWGDttywnefQWDDrklKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKER 131
Cdd:cd19160 8 LGKSGLRVSCLGLGTWvTFGS-------QISD---ETAEDLLTVAYEHGVNLFDTAEVYAAG-----KAERTLGNILKSK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 132 QQKEQVEVaIATKF-----AALPWRLGRGSVISALKDSLSRLGVSSVELyqlhwpgIWGN--------EGYLDGLGDAYE 198
Cdd:cd19160 73 GWRRSSYV-VTTKIywggqAETERGLSRKHIIEGLRGSLDRLQLEYVDI-------VFANrsdpnspmEEIVRAMTYVIN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 199 QGLVKAVGVSNYSEKRLRDAYERLKKRG-VPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGKYT-- 275
Cdd:cd19160 145 QGMAMYWGTSRWSAMEIMEAYSVARQFNlIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDgr 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 276 -PNNPPTGPRGRIYTPEFL-----TKLQPLINRIKEIGGSYEKTPTQVVLNW-LICQGNVVPIPGAKNAEQAREFAGALG 348
Cdd:cd19160 225 vPDTCRAAVKGYQWLKEKVqseegKKQQAKVKELHPIADRLGCTVAQLAIAWcLRSEGVSSVLLGVSSAEQLIENLGSIQ 304
|
330
....*....|...
gi 1002286311 349 --WSLTDQEVEEL 359
Cdd:cd19160 305 vlSQLTPQTVMEI 317
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
89-364 |
1.21e-15 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 76.69 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 89 AKGAFDASVDCGITFFDTAEVYgagisgaiNSESLLGRFIKERQQKEQV---EVAIATKFaaLPWRLGRGSVISALKDSL 165
Cdd:cd19107 19 VTEAVKVAIDAGYRHIDCAYVY--------QNENEVGEAIQEKIKEQVVkreDLFIVSKL--WCTFHEKGLVKGACQKTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 166 SRLGVSSVELYQLHWPG-----------------IWGNEGYLD---GLGDAYEQGLVKAVGVSNYSekrlRDAYER-LKK 224
Cdd:cd19107 89 SDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvIPSDTTFLDtweAMEELVDEGLVKAIGVSNFN----HLQIERiLNK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 225 RGVPL--ASNQVNySLIYRNPEEngVKAACDELGITLIAYSPIAqgvltgkyTPNNPPTGPRgriyTPEFLTklqplINR 302
Cdd:cd19107 165 PGLKYkpAVNQIE-CHPYLTQEK--LIQYCQSKGIVVTAYSPLG--------SPDRPWAKPE----DPSLLE-----DPK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002286311 303 IKEIGGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSMAR 364
Cdd:cd19107 225 IKEIAAKHNKTTAQVLIRFPI-QRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNR 285
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
53-347 |
2.13e-15 |
|
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: 75.95 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 53 LGGSDVAVTKLGIGAWswgdTTYWNefQWDDrklKAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQ 132
Cdd:cd19141 5 LGKSGLRVSCLGLGTW----VTFGS--QISD---EVAEELVTLAYENGINLFDTAEVYAAG-----KAEIVLGKILKKKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 133 QKEQVEVaIATKF-----AALPWRLGRGSVISALKDSLSRLGVSSVELyqlhwpgIWGN--------EGYLDGLGDAYEQ 199
Cdd:cd19141 71 WRRSSYV-ITTKIfwggkAETERGLSRKHIIEGLKASLERLQLEYVDI-------VFANrpdpntpmEEIVRAFTHVINQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 200 GLVKAVGVSNYSEKRLRDAYERLKKRG-VPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGKYTPNN 278
Cdd:cd19141 143 GMAMYWGTSRWSAMEIMEAYSVARQFNlIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286311 279 PPTGP---------RGRIyTPEFLTKLQPLINRIKEIGGSYEKTPTQVVLNW-LICQGNVVPIPGAKNAEQAREFAGAL 347
Cdd:cd19141 223 PEYSRaslkgyqwlKEKI-LSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWcLKNEGVSSVLLGASSTEQLYENLQAI 300
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
61-357 |
2.50e-15 |
|
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: 75.25 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 61 TKLGIGAWSWGDttywnefqwddrklKAAKGAFDASVDCGITFFDTAEVYGagisgainSESLLGRFIKERQQKEQV--- 137
Cdd:cd19128 2 PRLGFGTYKITE--------------SESKEAVKNAIKAGYRHIDCAYYYG--------NEAFIGIAFSEIFKDGGVkre 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 138 EVAIATKFaaLPWRLGRGSVISALKDSLSRLGVSSVELYQLHWPGIW----------GNEGYLDG---LGDAY------- 197
Cdd:cd19128 60 DLFITSKL--WPTMHQPENVKEQLLITLQDLQLEYLDLFLIHWPLAFdmdtdgdprdDNQIQSLSkkpLEDTWrameqcv 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 198 EQGLVKAVGVSNYSEKRLRD--AYERLKkrgvPLaSNQVNYSLIYrnPEENGVKaACDELGITLIAYSPIAQGVLTGKYT 275
Cdd:cd19128 138 DEKLTKNIGVSNYSTKLLTDllNYCKIK----PF-MNQIECHPYF--QNDKLIK-FCIENNIHVTAYRPLGGSYGDGNLT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 276 PNNPPTgprgriytpefltklqplinrIKEIGGSYEKTPTQVVLNWLICQ--GNVVPIPGAKNAEQAREFAGALGWSLTD 353
Cdd:cd19128 210 FLNDSE---------------------LKALATKYNTTPPQVIIAWHLQKwpKNYSVIPKSANKSRCQQNFDINDLALTK 268
|
....
gi 1002286311 354 QEVE 357
Cdd:cd19128 269 EDMD 272
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
92-342 |
3.45e-15 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 75.14 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 92 AFDASVDCGITFFDTAEVY------GAGISGAINSESLLGR---FI-----KERQQKEQVEvaiatkfaalpwrlgrgsv 157
Cdd:cd19118 25 AVKIALKAGYRHLDLAKVYqnqhevGQALKELLKEEPGVKRedlFItsklwNNSHRPEYVE------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 158 iSALKDSLSRLGVSSVELYQLHWP-------------GIWGNEG--YLD---GLGDAYE-------QGLVKAVGVSNYSE 212
Cdd:cd19118 86 -PALDDTLKELGLDYLDLYLIHWPvafkptgdlnpltAVPTNGGevDLDlsvSLVDTWKamvelkkTGKVKSIGVSNFSI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 213 KRLRDAYErlkKRGVPLASNQVNYSLIYRNPEengVKAACDELGITLIAYSPIAqgvltgkytpNNPPTGPRgRIYTPEf 292
Cdd:cd19118 165 DHLQAIIE---ETGVVPAVNQIEAHPLLLQDE---LVDYCKSKNIHITAYSPLG----------NNLAGLPL-LVQHPE- 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1002286311 293 ltklqplinrIKEIGGSYEKTPTQVVLNWLICQGNVVpIPGAKNAEQARE 342
Cdd:cd19118 227 ----------VKAIAAKLGKTPAQVLIAWGIQRGHSV-IPKSVTPSRIRS 265
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
52-284 |
3.52e-15 |
|
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: 75.28 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 52 RLGGSDVAVTKLGIGAWSWGdttywNEFqwDDRKLKAAKGAFDASVDCGITFFDTAEVYGAGIsgainSESLLGRFIKE- 130
Cdd:cd19163 5 KLGKTGLKVSKLGFGASPLG-----GVF--GPVDEEEAIRTVHEALDSGINYIDTAPWYGQGR-----SETVLGKALKGi 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 131 -RQQkeqveVAIATKFAalpwRLGRG----------SVISALKDSLSRLGVSSVELYQLHWP------GIWGNEGyLDGL 193
Cdd:cd19163 73 pRDS-----YYLATKVG----RYGLDpdkmfdfsaeRITKSVEESLKRLGLDYIDIIQVHDIefapslDQILNET-LPAL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 194 GDAYEQGLVKAVGVSNYSEKRLRDAYERlkkrgvplASNQVNYSLIY-----RNPEENGVKAACDELGITLIAYSPIAQG 268
Cdd:cd19163 143 QKLKEEGKVRFIGITGYPLDVLKEVLER--------SPVKIDTVLSYchytlNDTSLLELLPFFKEKGVGVINASPLSMG 214
|
250
....*....|....*.
gi 1002286311 269 VLTGKYTPNNPPTGPR 284
Cdd:cd19163 215 LLTERGPPDWHPASPE 230
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
58-286 |
4.74e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 75.05 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 58 VAVTKLGIGawswgdtTYWNEFqwDDRKLKAAKGAFDASVDCGITFFDTAEVYGAGISgainsESLLGRFIKERQQKEQV 137
Cdd:cd19099 1 LTLSSLGLG-------TYRGDS--DDETDEEYREALKAALDSGINVIDTAINYRGGRS-----ERLIGKALRELIEKGGI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 138 ---EVAIATK-----------FAALPWRL--------------GRGSVIS------ALKDSLSRLGVSSVELYQLHWPGI 183
Cdd:cd19099 67 krdEVVIVTKagyipgdgdepLRPLKYLEeklgrglidvadsaGLRHCISpayledQIERSLKRLGLDTIDLYLLHNPEE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 184 W----GNEGYLDGLGDAYE-------QGLVKAVGVSNYSEKRLRDAYE-----RLKKRGVPLASN--------QVNYSLI 239
Cdd:cd19099 147 QllelGEEEFYDRLEEAFEaleeavaEGKIRYYGISTWDGFRAPPALPghlslEKLVAAAEEVGGdnhhfkviQLPLNLL 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002286311 240 YRNP--EENGVK-------AACDELGITLIAYSPIAQGVLTGKYTPNNPPTGPRGR 286
Cdd:cd19099 227 EPEAltEKNTVKgealsllEAAKELGLGVIASRPLNQGQLLGELRLADLLALPGGA 282
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
53-347 |
7.65e-15 |
|
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: 74.74 E-value: 7.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 53 LGGSDVAVTKLGIGAWSWGDTTYWNEFqwddrklkaAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQ 132
Cdd:cd19158 6 LGKSGLRVSCLGLGTWVTFGGQITDEM---------AEHLMTLAYDNGINLFDTAEVYAAG-----KAEVVLGNIIKKKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 133 QKEQvEVAIATKF-----AALPWRLGRGSVISALKDSLSRLGVSSVELYQLHWPGI-WGNEGYLDGLGDAYEQGLVKAVG 206
Cdd:cd19158 72 WRRS-SLVITTKIfwggkAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPnTPMEETVRAMTHVINQGMAMYWG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 207 VSNYSEKRLRDAYERLKKRG-VPLASNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGKYTPNNPPTGpRG 285
Cdd:cd19158 151 TSRWSSMEIMEAYSVARQFNlIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYS-RA 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002286311 286 RIYTPEFLT---------KLQPLINRIKEIGGSYEKTPTQVVLNW-LICQGNVVPIPGAKNAEQAREFAGAL 347
Cdd:cd19158 230 SLKGYQWLKdkilseegrRQQAKLKELQAIAERLGCTLPQLAIAWcLRNEGVSSVLLGASNAEQLMENIGAI 301
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
90-370 |
8.00e-15 |
|
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: 74.34 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 90 KGAFDASVDCGITFFDTAEVYGagisgainSESLLGRFIKERQQKEQV----EVAIATKFaalpWRLGR--GSVISALKD 163
Cdd:cd19106 23 KAAVKYALDAGYRHIDCAAVYG--------NEQEVGEALKEKVGPGKAvpreDLFVTSKL----WNTKHhpEDVEPALRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 164 SLSRLGVSSVELYQLHWPGIWGNEG-----------------YLD---GLGDAYEQGLVKAVGVSNYSEKRLRDAyerLK 223
Cdd:cd19106 91 TLKDLQLDYLDLYLIHWPYAFERGDnpfpknpdgtirydsthYKEtwkAMEKLVDKGLVKAIGLSNFNSRQIDDI---LS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 224 KRGVPLASNQVNySLIYRNPEEngVKAACDELGITLIAYSPIAqgvltgkyTPNNPPTGPRgriyTPEFLTklQPlinRI 303
Cdd:cd19106 168 VARIKPAVLQVE-CHPYLAQNE--LIAHCKARGLVVTAYSPLG--------SPDRPWAKPD----EPVLLE--EP---KV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 304 KEIGGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSM---AREIKPVI 370
Cdd:cd19106 228 KALAKKYNKSPAQILLRWQV-QRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALnrnWRYIVPMI 296
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
61-270 |
1.32e-14 |
|
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: 73.55 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 61 TKLGIGAWSWGDTTYWNEfqwddrklKAAKGAFDASVDCGITFFDTAEVYGAGIsgainSESLLGRFIkerQQKEQVEVA 140
Cdd:cd19162 1 PRLGLGAASLGNLARAGE--------DEAAATLDAAWDAGIRYFDTAPLYGLGL-----SERRLGAAL---ARHPRAEYV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 141 IATKFAALP--------------WRLGRGSVISALKDSLSRLGVSSVELYQLHWPGiwgnEGYLDGLGDAYE-------Q 199
Cdd:cd19162 65 VSTKVGRLLepgaagrpagadrrFDFSADGIRRSIEASLERLGLDRLDLVFLHDPD----RHLLQALTDAFPaleelraE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002286311 200 GLVKAVGVSNYSEKRLRDAYERLKKRGVPLASnqvNYSLIyRNPEENGVKAACDELGITLIAYSPIAQGVL 270
Cdd:cd19162 141 GVVGAIGVGVTDWAALLRAARRADVDVVMVAG---RYTLL-DRRAATELLPLCAAKGVAVVAAGVFNSGIL 207
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
62-364 |
1.26e-13 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 70.49 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 62 KLGIGAWSWGDTTywnefqwddrklkaAKGAFDASVDCGITFFDTAEVYgagisgaiNSESLLGRFIKERQQKEQvEVAI 141
Cdd:PRK11565 17 QLGLGVWQASNEE--------------VITAIHKALEVGYRSIDTAAIY--------KNEEGVGKALKEASVARE-ELFI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 142 ATKFaalpWRLGRGSVISALKDSLSRLGVSSVELYQLHWPgIWGNEGYLD---GLGDAYEQGLVKAVGVSNYSEKRLrda 218
Cdd:PRK11565 74 TTKL----WNDDHKRPREALEESLKKLQLDYVDLYLMHWP-VPAIDHYVEawkGMIELQKEGLIKSIGVCNFQIHHL--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 219 yERLK-KRGVPLASNQVNYSLIYRNPEENGVKAAcdeLGITLIAYSPIAQGvltGKYTPNNPPtgprgriytpefltklq 297
Cdd:PRK11565 146 -QRLIdETGVTPVINQIELHPLMQQRQLHAWNAT---HKIQTESWSPLAQG---GKGVFDQKV----------------- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002286311 298 plinrIKEIGGSYEKTPTQVVLNWLICQGNVVpIPGAKNAEQAREFAGALGWSLtdqEVEELRSMAR 364
Cdd:PRK11565 202 -----IRDLADKYGKTPAQIVIRWHLDSGLVV-IPKSVTPSRIAENFDVFDFRL---DKDELGEIAK 259
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
63-376 |
2.39e-13 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 69.99 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 63 LGIGAW--SWGDTTywnefqwddrklKAAKGAFDAS---VDCGITFFDTAEVyGAGIS-----GAINSESLLgrfikerq 132
Cdd:cd19110 7 VGLGTWkaSPGEVT------------EAVKVAIDAGyrhFDCAYLYHNESEV-GAGIRekikeGVVRREDLF-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 133 qkeqvevaIATKFAALPWRlgRGSVISALKDSLSRLGVSSVELYQLHWPG-----------------IWGNEGYLD---G 192
Cdd:cd19110 66 --------IVSKLWCTCHK--KSLVKTACTRSLKALKLNYLDLYLIHWPMgfkpgepdlpldrsgmvIPSDTDFLDtweA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 193 LGDAYEQGLVKAVGVSNYSEKRLRDAYERLKKRGVPLaSNQVNYsliyrNPEENGVK--AACDELGITLIAYSPIAqGVL 270
Cdd:cd19110 136 MEDLVIEGLVKNIGVSNFNHEQLERLLNKPGLRVKPV-TNQIEC-----HPYLTQKKliSFCQSRNVSVTAYRPLG-GSC 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 271 TGKYTPNNPPtgprgriytpefltklqplinrIKEIGGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEQAREFAGALGWS 350
Cdd:cd19110 209 EGVDLIDDPV----------------------IQRIAKKHGKSPAQILIRFQI-QRNVIVIPKSVTPSRIKENIQVFDFE 265
|
330 340
....*....|....*....|....*.
gi 1002286311 351 LTDQEVEELRSMAREIKpVIGFPVEK 376
Cdd:cd19110 266 LTEHDMDNLLSLDRNLR-LATFPITE 290
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
63-365 |
1.28e-12 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 67.52 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 63 LGIGAWSwgdttywnefqwDDRKLKAAKGAFDASVDCGITFFDTAEVYGagisgainSESLLGRFIKERQQKEQV---EV 139
Cdd:cd19119 15 LGLGTAS------------PHEDRAEVKEAVEAAIKEGYRHIDTAYAYE--------TEDFVGEAIKRAIDDGSIkreEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 140 AIATKFaalpWRLGRGSVISALKDSLSRLGVSSVELYQLHWP------------GIW-----GNEGYLDG---------L 193
Cdd:cd19119 75 FITTKV----WPTFYDEVERSLDESLKALGLDYVDLLLVHWPvcfekdsddsgkPFTpvnddGKTRYAASgdhittykqL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 194 GDAYEQGLVKAVGVSNYSEKRLrdayERLKK--RGVPlASNQVnySLIYRNPEENGVKaACDELGITLIAYSPIAQGvlt 271
Cdd:cd19119 151 EKIYLDGRAKAIGVSNYSIVYL----ERLIKecKVVP-AVNQV--ELHPHLPQMDLRD-FCFKHGILVTAYSPLGSH--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 272 gkytpnnppTGPRGRIytpefltklqPLinrIKEIGGSYEKTPTQVVLNWLICQGNVVpIPgaKNAEQAREFAGALGWSL 351
Cdd:cd19119 220 ---------GAPNLKN----------PL---VKKIAEKYNVSTGDILISYHVRQGVIV-LP--KSLKPVRIVSNGKIVSL 274
|
330
....*....|....
gi 1002286311 352 TDQEVEELRSMARE 365
Cdd:cd19119 275 TKEDLQKLDDIGEK 288
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
97-365 |
1.69e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 64.22 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 97 VDCGITFFDTAEVYGAGISGAInsesllgrfIKERQQKEQVEVAIATKFAA--------LPWRlGRGSVISALKDSLSRL 168
Cdd:PRK10376 50 VALGVNHIDTSDFYGPHVTNQL---------IREALHPYPDDLTIVTKVGArrgedgswLPAF-SPAELRRAVHDNLRNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 169 GVSSVELYQLHwpgIWGN---------EGYLDGLGDAYEQGLVKAVGVSNYSEKRLRDAyerlkKRGVPLASNQVNYSLI 239
Cdd:PRK10376 120 GLDVLDVVNLR---LMGDghgpaegsiEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEA-----RKIAEIVCVQNHYNLA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 240 YRNPEengvkAACDELGitliayspiAQGVltgKYTPNNPPTGprgriYTPefltkLQPliNRIKEIGGSYEKTPTQVVL 319
Cdd:PRK10376 192 HRADD-----ALIDALA---------RDGI---AYVPFFPLGG-----FTP-----LQS--STLSDVAASLGATPMQVAL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1002286311 320 NWLICQG-NVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSMARE 365
Cdd:PRK10376 243 AWLLQRSpNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDGIARE 289
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
58-373 |
1.94e-10 |
|
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: 61.29 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 58 VAVTKLGIGAWSWGDTtyWNEFQWDDRKLKAAKgAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQKEQV 137
Cdd:cd19146 9 VRVSPLCLGAMSFGEA--WKSMMGECDKETAFK-LLDAFYEQGGNFIDTANNYQGE-----ESERWVGEWMASRGNRDEM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 138 evAIATKFAALPWRLG------------RGSVISALKDSLSRLGVSSVELYQLHWpgiW----GNEGYLDGLGDAYEQGL 201
Cdd:cd19146 81 --VLATKYTTGYRRGGpikiksnyqgnhAKSLRLSVEASLKKLQTSYIDILYVHW---WdyttSIPELMQSLNHLVAAGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 202 VKAVGVSNYSEKRLRDAYERLKKRGV-PLASNQVNYSLIYRNPEENgVKAACDELGITLIAYSPIAQGVL-TGKYTPNNP 279
Cdd:cd19146 156 VLYLGVSDTPAWVVSKANAYARAHGLtQFVVYQGHWSAAFRDFERD-ILPMCEAEGMALAPWGVLGQGQFrTEEEFKRRG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 280 PTGPRGRIYTPEFLTKLQPLINRIKEIGgsyeKTPTQVVLNWLICQGN-VVPIPGAKNAEQAREFAGALGWSLTDQEVEE 358
Cdd:cd19146 235 RSGRKGGPQTEKERKVSEKLEKVAEEKG----TAITSVALAYVMHKAPyVFPIVGGRKVEHLKGNIEALGISLSDEEIQE 310
|
330
....*....|....*.
gi 1002286311 359 LRSMAreikPV-IGFP 373
Cdd:cd19146 311 IEDAY----PFdVGFP 322
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
157-369 |
2.12e-10 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 60.97 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 157 VISALKDSLSRLGVSSVELYQLHWPGIW--GNEGY---------------------LDGLGDAyeqGLVKAVGVSNYSEK 213
Cdd:cd19109 84 VRPTLERTLKVLQLDYVDLYIIEMPMAFkpGDEIYprdengkwlyhktnlcatweaLEACKDA---GLVKSIGVSNFNRR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 214 RLRDAYER--LKKRGVplaSNQVNYSLIYRNPEengVKAACDELGITLIAYSPIAqgvltgkyTPNNPPTGprgRIYTPE 291
Cdd:cd19109 161 QLELILNKpgLKHKPV---SNQVECHPYFTQPK---LLEFCQQHDIVIVAYSPLG--------TCRDPIWV---NVSSPP 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002286311 292 FLTklQPLINrikEIGGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSMAREIKPV 369
Cdd:cd19109 224 LLE--DPLLN---SIGKKYNKTAAQVVLRFNI-QRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYV 295
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
89-362 |
3.05e-10 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 60.24 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 89 AKGAFDASVDCGITFFDTAEVY------GAGISGAINSesllgrfIKERQqkeqvEVAIATKFaalpWRLGRGSVISALK 162
Cdd:cd19121 27 VKAAVAHALKIGYRHIDGALCYqnedevGEGIKEAIAG-------GVKRE-----DLFVTTKL----WSTYHRRVELCLD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 163 DSLSRLGVSSVELYQLHWPGIWGNEG-------YLDG----------------LGDAYEQGLVKAVGVSNYSEKRLRday 219
Cdd:cd19121 91 RSLKSLGLDYVDLYLVHWPVLLNPNGnhdlfptLPDGsrdldwdwnhvdtwkqMEKVLKTGKTKAIGVSNYSIPYLE--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 220 ERLKKRGVPLASNQV-NYSLIyrnPEENGVKaACDELGITLIAYSPIAQgvlTGkytpnnpptGPrgriytpefLTKLQP 298
Cdd:cd19121 168 ELLKHATVVPAVNQVeNHPYL---PQQELVD-FCKEKGILIEAYSPLGS---TG---------SP---------LISDEP 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002286311 299 LInrikEIGGSYEKTPTQVVLNWLICQGNVVpIPgaKNAEQAREFAGALGWSLTDQEVEELRSM 362
Cdd:cd19121 223 VV----EIAKKHNVGPGTVLISYQVARGAVV-LP--KSVTPDRIKSNLEIIDLDDEDMNKLNDI 279
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
61-272 |
1.04e-09 |
|
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: 59.16 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 61 TKLGIGAWSWGDTtywnefqWDDRKLKAAKGAFDASVDCGITFFDTAEVYGAGIsgainSESLLGRFIKErqqKEQVEVA 140
Cdd:cd19152 1 PKLGFGTAPLGNL-------YEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGL-----SEERLGAALRE---LGREDYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 141 IATK--------------FAALPW-RLGRGSV--ISA------LKDSLSRLGVSSVELYQLHWP-----GIWGNEGYLDG 192
Cdd:cd19152 66 ISTKvgrllvplqeveptFEPGFWnPLPFDAVfdYSYdgilrsIEDSLQRLGLSRIDLLSIHDPdedlaGAESDEHFAQA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 193 LGDAY-------EQGLVKAVGVSNYSEKRLRDAYERLKKRGVPLASnqvNYSLiYRNPEENGVKAACDELGITLIAYSPI 265
Cdd:cd19152 146 IKGAFraleelrEEGVIKAIGLGVNDWEVILRILEEADLDWVMLAG---RYTL-LDHSAARELLPECEKRGVKVVNAGPF 221
|
....*..
gi 1002286311 266 AQGVLTG 272
Cdd:cd19152 222 NSGFLAG 228
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
88-342 |
2.18e-09 |
|
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: 57.85 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 88 AAKGAFDASVDCGITFFDTAEVYgagisgaiNSESLLGRFIKERQQKEQV---EVAIATKFAALPWRLGRgsVISALKDS 164
Cdd:cd19129 20 ATRNAVKAALEAGFRHFDCAERY--------RNEAEVGEAMQEVFKAGKIrreDLFVTTKLWNTNHRPER--VKPAFEAS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 165 LSRLGVSSVELYQLHWP------------GIWGNEGYLDG---------LGDAYEQGLVKAVGVSNYSEKRLRDAYE--R 221
Cdd:cd19129 90 LKRLQLDYLDLYLIHTPfafqpgdeqdprDANGNVIYDDGvtlldtwraMERLVDEGRCKAIGLSDVSLEKLREIFEaaR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 222 LKKRGVPLASnqvnysliyrNP--EENGVKAACDELGITLIAYSPIAQGVltgkytpnnpptgprgriyTPEFLTklQPL 299
Cdd:cd19129 170 IKPAVVQVES----------HPylPEWELLDFCKNHGIVLQAFAPLGHGM-------------------EPKLLE--DPV 218
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1002286311 300 INrikEIGGSYEKTPTQVVLNWLICQGnVVPIPGAKNAEQARE 342
Cdd:cd19129 219 IT---AIARRVNKTPAQVLLAWAIQRG-TALLTTSKTPSRIRE 257
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
58-359 |
1.06e-08 |
|
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: 55.99 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 58 VAVTKLGIGAWSWGDTtyWNEFQWDDRKLKAAKgAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQQKEQV 137
Cdd:cd19147 8 IRVSPLILGAMSIGDA--WSGFMGSMDKEQAFE-LLDAFYEAGGNFIDTANNYQDE-----QSETWIGEWMKSRKNRDQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 138 evAIATKFAA--LPWRLGRG-----------SVISALKDSLSRLGVSSVELYQLHWpgiW----GNEGYLDGLGDAYEQG 200
Cdd:cd19147 80 --VIATKFTTdyKAYEVGKGkavnycgnhkrSLHVSVRDSLRKLQTDWIDILYVHW---WdyttSIEEVMDSLHILVQQG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 201 LVKAVGVSNYSEKRLRDAYERLKKRG-VPLASNQVNYSLIYRNPEENGVKAAcDELGITLIAYSPIAQGVLTGKYT---- 275
Cdd:cd19147 155 KVLYLGVSDTPAWVVSAANYYATAHGkTPFSVYQGRWNVLNRDFERDIIPMA-RHFGMALAPWDVLGGGKFQSKKAveer 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 276 -PNNPP--TGPRGRIYTPEfLTKLQPLINRIKEIGGSyeKTPTQVVLNWLICQG-NVVPIPGAKNAEQAREFAGALGWSL 351
Cdd:cd19147 234 kKNGEGlrSFVGGTEQTPE-EVKISEALEKVAEEHGT--ESVTAIALAYVRSKApNVFPLVGGRKIEHLKDNIEALSIKL 310
|
....*...
gi 1002286311 352 TDQEVEEL 359
Cdd:cd19147 311 TPEEIEYL 318
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
197-367 |
1.29e-08 |
|
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: 55.89 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 197 YEQGLVKAVGVSNYSEKRLRDA--YERLKKrgvplASNQVNYsliyrNP---EENGVKAACDElGITLIAYSPIaqgvlt 271
Cdd:cd19115 154 VDKGLARSIGVSNFSAQLLMDLlrYARIRP-----ATLQIEH-----HPyltQPRLVKYAQKE-GIAVTAYSSF------ 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 272 gkytpnnpptGPRGRIytpEF----LTKLQPLINR--IKEIGGSYEKTPTQVVLNWlICQGNVVPIPGAKNAEQAREFAG 345
Cdd:cd19115 217 ----------GPQSFL---ELdlpgAKDTPPLFEHdvIKSIAEKHGKTPAQVLLRW-ATQRGIAVIPKSNNPKRLAQNLD 282
|
170 180
....*....|....*....|..
gi 1002286311 346 ALGWSLTDQEVEELRSMAREIK 367
Cdd:cd19115 283 VTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
87-341 |
2.95e-07 |
|
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: 51.56 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 87 KAAKGAFDASVDCGITFFDTAEVYGAGIsgainSESLLGRFIKErqqKEQVEVAIATK-------------------FAA 147
Cdd:cd19161 20 ADADATLDAAWDSGIRYFDTAPMYGHGL-----AEHRLGDFLRE---KPRDEFVLSTKvgrllkparegsvpdpngfVDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 148 LPWRL----GRGSVISALKDSLSRLGVSSVELYQLH--------------WPGIWGNEGYlDGLGDAYEQGLVKAVGVSN 209
Cdd:cd19161 92 LPFEIvydySYDGIMRSFEDSLQRLGLNRIDILYVHdigvythgdrkerhHFAQLMSGGF-KALEELKKAGVIKAFGLGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 210 YSEKRLRDAYERLKKRGVPLASnqvNYSLIYRNPEEnGVKAACDELGITLIAYSPIAQGVL-TG-----KYTPNNPPtgp 283
Cdd:cd19161 171 NEVQICLEALDEADLDCFLLAG---RYSLLDQSAEE-EFLPRCEQRGTSLVIGGVFNSGILaTGtksgaKFNYGDAP--- 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002286311 284 rgriytPEFLTKlqplINRIKEIGGSYEKTPTQVVLNWLICQGNVVPI-PGAKNAEQAR 341
Cdd:cd19161 244 ------AEIISR----VMEIEKICDAYNVPLAAAALQFPLRHPAVASVlTGARNPAQLR 292
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
97-364 |
6.03e-07 |
|
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: 50.70 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 97 VDCGITFFDTAEVyGAGISGainsesllgrFIKERQQKEQVEVAIATKFaalpW-RLGR-GSVISALKDSLSRLGVSSVE 174
Cdd:cd19122 41 LDCAWFYLNEDEV-GDAVRD----------FLKENPSVKREDLFICTKV----WnHLHEpEDVKWSIDNSLKNLKLDYID 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 175 LYQLHWP-------------GIWGNEGYLDGLGD-----------AYEQGLVKAVGVSNYSEKRLRdayERLKKRGVPLA 230
Cdd:cd19122 106 LFLVHWPiaaekndqrspklGPDGKYVILKDLTEnpeptwrameeIYESGKAKAIGVSNWTIPGLK---KLLSFAKVKPH 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 231 SNQVNYSLIYRNPEengVKAACDELGITLIAYSPIAqgvltgkyTPNN-PPTGPRgriytpeflTKLQPLINRIKEIGGS 309
Cdd:cd19122 183 VNQIEIHPFLPNEE---LVDYCFSNDILPEAYSPLG--------SQNQvPSTGER---------VSENPTLNEVAEKGGY 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1002286311 310 yekTPTQVVLNWLICQGNVVpIPgaKNAEQAREFAGALGWSLTDQEVEELRSMAR 364
Cdd:cd19122 243 ---SLAQVLIAWGLRRGYVV-LP--KSSTPSRIESNFKSIELSDEDFEAINQVAK 291
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
53-273 |
6.70e-06 |
|
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: 47.46 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 53 LGGSDVAVTKLGIGAWSwgdtTYWNEFQWDdrklkAAKGAFDASVDCGITFFDTAEVYGAGisgaiNSESLLGRFIKERQ 132
Cdd:cd19142 6 LGKSGLRVSNVGLGTWS----TFSTAISEE-----QAEEIVTLAYENGINYFDTSDAFTSG-----QAETELGRILKKKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 133 QKeQVEVAIATKfaaLPWR-------LGRGSVISALKDSLSRLGVSSVELYQLH-WPGIWGNEGYLDGLGDAYEQGLVKA 204
Cdd:cd19142 72 WK-RSSYIVSTK---IYWSygseergLSRKHIIESVRASLRRLQLDYIDIVIIHkADPMCPMEEVVRAMSYLIDNGLIMY 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 205 VGVSNYSEKRLRDAYERLKKRGVPLA-SNQVNYSLIYRNPEENGVKAACDELGITLIAYSPIAQGVLTGK 273
Cdd:cd19142 148 WGTSRWSPVEIMEAFSIARQFNCPTPiCEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGI 217
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
94-363 |
6.92e-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: 47.34 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 94 DASVDCGITFFDTAEVYGAgisgainSESLLGRFIKERQQKEQvEVAIATKFA---ALPWRLgRGSV-------ISALK- 162
Cdd:cd19098 42 DAAWAAGVRYFDAARSYGR-------AEEFLGSWLRSRNIAPD-AVFVGSKWGytyTADWQV-DAAVhevkdhsLARLLk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 163 ---DSLSRLGvSSVELYQLHW----PGIWGNEGYLDGLGDAYEQGLvkAVGVSNYSEKR---LRDAYErLKKRGVPL-AS 231
Cdd:cd19098 113 qweETRSLLG-KHLDLYQIHSatleSGVLEDADVLAALAELKAEGV--KIGLSLSGPQQaetLRRALE-IEIDGARLfDS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 232 NQVNYSLIYRNPEENGVKAAcdELGITLIAYSPIAQGVLTgkytpnnpptgprGRIYTPEFLTKLQPLinriKEIGGSYE 311
Cdd:cd19098 189 VQATWNLLEQSAGEALEEAH--EAGMGVIVKEALANGRLT-------------DRNPSPELAPLMAVL----KAVADRLG 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1002286311 312 KTPTQVVLNWLICQG--NVVpIPGAKNAEQAREFAGALGWSLTDQEVEELRSMA 363
Cdd:cd19098 250 VTPDALALAAVLAQPfvDVV-LSGAATPEQLRSNLRALDVSLDLELLAALADLA 302
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
96-367 |
7.57e-06 |
|
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: 47.17 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 96 SVDCGITFFDTAEVYGagisgainSESLLGRFIKERQQKEQV---EVAIATKFaalpWRL--GRGSVISALKDSLSRLGV 170
Cdd:cd19114 26 AIKVGYRLIDGALLYG--------NEAEVGRGIRKAIQEGLVkreDLFIVTKL----WNNfhGKDHVREAFDRQLKDYGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 171 SSVELYQLHWP--------GIWGNEGYLDG------------------LGDAYEQGLVKAVGVSNYSEKRLRD--AYERL 222
Cdd:cd19114 94 DYIDLYLIHFPipaayvdpAENYPFLWKDKelkkfpleqspmqecwreMEKLVDAGLVRNIGIANFNVQLILDllTYAKI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 223 KKrgvplASNQVNYSLIYrnPEENGVKAAcDELGITLIAYSPIaqgvltgkytpnnpptGPRGRIYTPEFLTKLQPLINR 302
Cdd:cd19114 174 KP-----AVLQIEHHPYL--QQKRLIDWA-KKQGIQITAYSSF----------------GNAVYTKVTKHLKHFTNLLEH 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002286311 303 --IKEIGGSYEKTPTQVVLNWLIcQGNVVPIPGAKNAEQAREFAGALGWSLTDQEVEELRSMAREIK 367
Cdd:cd19114 230 pvVKKLADKHKRDTGQVLLRWAV-QRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
100-297 |
1.09e-04 |
|
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: 43.68 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 100 GITFFDTAEVYGAGIsgainSESLLGRFIKeRQQKEQVEVAIATK---FAALPWRLGRGSVISALKDSLSRLGVSSVELY 176
Cdd:cd19153 46 GINHFDTSPYYGAES-----SEAVLGKALA-ALQVPRSSYTVATKvgrYRDSEFDYSAERVRASVATSLERLHTTYLDVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 177 QLHwpgiwgNEGYLDGLGDAYE----------QGLVKAVGVSNYSEKRLRDAYERLKKRGVPLASNQVNYSLIYR--NPE 244
Cdd:cd19153 120 YLH------DIEFVDYDTLVDEalpalrtlkdEGVIKRIGIAGYPLDTLTRATRRCSPGSLDAVLSYCHLTLQDArlESD 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002286311 245 ENGVKAACdelGITLIAYSPIAQGVLTGKYTPNNPPTGPRGRIYTPEFLTKLQ 297
Cdd:cd19153 194 APGLVRGA---GPHVINASPLSMGLLTSQGPPPWHPASGELRHYAAAADAVCA 243
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
53-283 |
2.89e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 42.46 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 53 LGGSDVAVTKLGIGAWSWGDTtywnefqWDDRKLKAAKGAFDASVDCGITFFDTAEVYGAGIsgainSESLLGRFIKERQ 132
Cdd:PLN02587 4 LGSTGLKVSSVGFGASPLGSV-------FGPVSEEDAIASVREAFRLGINFFDTSPYYGGTL-----SEKVLGKALKALG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 133 QKEQvEVAIATKFAalpwRLGRGSVISA------LKDSLSRLGVSSVELYQLHwpGIwgNEGYLD--------GLGDAYE 198
Cdd:PLN02587 72 IPRE-KYVVSTKCG----RYGEGFDFSAervtksVDESLARLQLDYVDILHCH--DI--EFGSLDqivnetipALQKLKE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002286311 199 QGLVKAVGVSNYSEKRLRDAYERLKKRGVPLASNQVNYSLiyRNPEENGVKAACDELGITLIAYSPIAQGVLTGKYTPNN 278
Cdd:PLN02587 143 SGKVRFIGITGLPLAIFTYVLDRVPPGTVDVILSYCHYSL--NDSSLEDLLPYLKSKGVGVISASPLAMGLLTENGPPEW 220
|
....*
gi 1002286311 279 PPTGP 283
Cdd:PLN02587 221 HPAPP 225
|
|
| homeo_ZF_HD |
TIGR01565 |
homeobox domain, ZF-HD class; This model represents a class of homoebox domain that differs ... |
334-367 |
8.23e-03 |
|
homeobox domain, ZF-HD class; This model represents a class of homoebox domain that differs substantially from the typical homoebox domain described in pfam00046. It is found in both C4 and C3 plants.
Pssm-ID: 130628 Cd Length: 58 Bit Score: 34.46 E-value: 8.23e-03
10 20 30
....*....|....*....|....*....|....
gi 1002286311 334 AKNAEQAREFAGALGWSLTDQEVEELRSMAREIK 367
Cdd:TIGR01565 10 AEQKEKMRDFAEKLGWKLKDKRREEVREFCEEIG 43
|
|
| |
