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Conserved domains on  [gi|1002237949|ref|XP_015623177|]
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glyoxylate/succinic semialdehyde reductase 1 [Oryza sativa Japonica Group]

Protein Classification

NAD(P)-dependent oxidoreductase( domain architecture ID 11449905)

NAD(P)-dependent oxidoreductase similar to 3-hydroxyisobutyrate dehydrogenase, L-threonate dehydrogenase, 2-(hydroxymethyl)glutarate dehydrogenase, and glyoxylate/succinic semialdehyde reductase

CATH:  3.40.50.720
EC:  1.1.-.-
Gene Ontology:  GO:0050661|GO:0051287|GO:0016491
PubMed:  8749365
SCOP:  4000072

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-284 2.96e-108

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 315.52  E-value: 2.96e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   1 MEVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDKDGV 80
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  81 LEQIGEGKGYVDMSTVDAATSCKISEAIKQKGGAFVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKSFFL 160
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949 161 GEIGNGAKMKLVVNMIMGSMMNALSEGLSLADNSGLSPQTLLDVLDLGAIANPMFKLKGPSMLQGSYNPAFPLKHQQKDM 240
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1002237949 241 RLALALGDENAVSMPVAAASNEAFKKARSLGLGDLDFSAVYEVL 284
Cdd:COG2084   242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-284 2.96e-108

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 315.52  E-value: 2.96e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   1 MEVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDKDGV 80
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  81 LEQIGEGKGYVDMSTVDAATSCKISEAIKQKGGAFVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKSFFL 160
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949 161 GEIGNGAKMKLVVNMIMGSMMNALSEGLSLADNSGLSPQTLLDVLDLGAIANPMFKLKGPSMLQGSYNPAFPLKHQQKDM 240
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1002237949 241 RLALALGDENAVSMPVAAASNEAFKKARSLGLGDLDFSAVYEVL 284
Cdd:COG2084   242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-286 6.25e-55

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 179.86  E-value: 6.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   1 MEVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDKDGV 80
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  81 LEQIGEGKGYVDMSTVDAATSCKISEAIKQKGGAFVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKSFFL 160
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949 161 GEIGNGAKMKLVVNMIMGSMMNALSEGLSLADNSGLSPQTLLDVLDLGAIANPMFKLKGPSMLQGSYNPAFPLKHQQKDM 240
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1002237949 241 RLALALGDENAVSMPVAAASNEAFKKARSLGLGDLDFSAV---YEVLKG 286
Cdd:PRK11559  243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALacyYEKLAK 291
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 2-285 7.15e-54

2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism.


Pssm-ID: 130569 [Multi-domain]  Cd Length: 291  Bit Score: 177.00  E-value: 7.15e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   2 EVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDKDGVL 81
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  82 EQIGEGKGYVDMSTVDAATSCKISEAIKQKGGAFVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKSFFLG 161
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949 162 EIGNGAKMKLVVNMIMGSMMNALSEGLSLADNSGLSPQTLLDVLDLGAIANPMFKLKGPSMLQGSYNPAFPLKHQQKDMR 241
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1002237949 242 LALALGDENAVSMPVAAASNEAFKKARSLGLGDLDFSAVYEVLK 285
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALE 284
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-161 3.47e-49

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 160.33  E-value: 3.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   2 EVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDkDGVL 81
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFG-EGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  82 EQIGEGKGYVDMSTVDAATSCKISEAIKQKGGAFVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKSFFLG 161
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 1-32 1.04e-05

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240641 [Multi-domain]  Cd Length: 306  Bit Score: 45.95  E-value: 1.04e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1002237949   1 MEVGFLGLGIMGKAMAANLLRHGFRVTVWNRT 32
Cdd:cd12164   133 RRVGVLGLGELGAAVARRLAALGFPVSGWSRS 164
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-284 2.96e-108

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 315.52  E-value: 2.96e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   1 MEVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDKDGV 80
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  81 LEQIGEGKGYVDMSTVDAATSCKISEAIKQKGGAFVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKSFFL 160
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949 161 GEIGNGAKMKLVVNMIMGSMMNALSEGLSLADNSGLSPQTLLDVLDLGAIANPMFKLKGPSMLQGSYNPAFPLKHQQKDM 240
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1002237949 241 RLALALGDENAVSMPVAAASNEAFKKARSLGLGDLDFSAVYEVL 284
Cdd:COG2084   242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-286 6.25e-55

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 179.86  E-value: 6.25e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   1 MEVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDKDGV 80
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  81 LEQIGEGKGYVDMSTVDAATSCKISEAIKQKGGAFVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKSFFL 160
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949 161 GEIGNGAKMKLVVNMIMGSMMNALSEGLSLADNSGLSPQTLLDVLDLGAIANPMFKLKGPSMLQGSYNPAFPLKHQQKDM 240
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1002237949 241 RLALALGDENAVSMPVAAASNEAFKKARSLGLGDLDFSAV---YEVLKG 286
Cdd:PRK11559  243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALacyYEKLAK 291
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 2-285 7.15e-54

2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism.


Pssm-ID: 130569 [Multi-domain]  Cd Length: 291  Bit Score: 177.00  E-value: 7.15e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   2 EVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDKDGVL 81
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  82 EQIGEGKGYVDMSTVDAATSCKISEAIKQKGGAFVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKSFFLG 161
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949 162 EIGNGAKMKLVVNMIMGSMMNALSEGLSLADNSGLSPQTLLDVLDLGAIANPMFKLKGPSMLQGSYNPAFPLKHQQKDMR 241
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1002237949 242 LALALGDENAVSMPVAAASNEAFKKARSLGLGDLDFSAVYEVLK 285
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALE 284
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-161 3.47e-49

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 160.33  E-value: 3.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   2 EVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDkDGVL 81
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFG-EGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  82 EQIGEGKGYVDMSTVDAATSCKISEAIKQKGGAFVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKSFFLG 161
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
3-289 3.71e-42

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 146.92  E-value: 3.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   3 VGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDKDGVLE 82
Cdd:PRK15461    4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVCE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  83 QIGEGKGYVDMSTVDAATSCKISEAIKQKGGAFVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKSFFLGE 162
Cdd:PRK15461   84 GLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAGG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949 163 IGNGAKMKLvVNMIMGSMMNALS-EGLSLADNSGLSPQTLLDVLDLGAIANPMFKLKGPS-MLQGSYNPAFPLKHQQKDM 240
Cdd:PRK15461  164 PGMGIRVKL-INNYMSIALNALSaEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWPNkVLKGDLSPAFMIDLAHKDL 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1002237949 241 RLALALGDENAVSMPVAAASNEAFKKARSLGLGDLDFSAVYEVLKGAGG 289
Cdd:PRK15461  243 GIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAG 291
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
1-285 8.34e-41

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 143.24  E-value: 8.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   1 MEVGFLGLGIMGKAMAANLLRHGFRVTVwNRTLSKCQELVALGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDKDGV 80
Cdd:PRK15059    1 MKLGFIGLGIMGTPMAINLARAGHQLHV-TTIGPVADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  81 LEQIGEGKGYVDMSTVDAATSCKISEAIKQKGGAFVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKSFFL 160
Cdd:PRK15059   80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949 161 GEIGNGAKMKLVVNMIMGSMMNALSEGLSLADNSGLSPQTLLDVLDLGAIANPMFKLKGPSMLQGSYNPAFPLKHQQKDM 240
Cdd:PRK15059  160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1002237949 241 RLALALGDENAVSMPVAAASNEAFKKARSLGLGDLDFSAVYEVLK 285
Cdd:PRK15059  240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALE 284
PLN02858 PLN02858
fructose-bisphosphate aldolase
 3-293 3.64e-30

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 119.96  E-value: 3.64e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949    3 VGFLGLGIMGKAMAANLLRHGFRVT---VWNRTLSKCQELvalGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDKDG 79
Cdd:PLN02858   327 IGFIGLGAMGFGMASHLLKSNFSVCgydVYKPTLVRFENA---GGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLG 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   80 VLEQIGEGKGYVDMSTVDAATSCKISEAIK--QKGGAFVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKS 157
Cdd:PLN02858   404 AVSALPAGASIVLSSTVSPGFVIQLERRLEneGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKL 483

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  158 FFL-GEIGNGAKMKLVVNMIMGSMMNALSEGLSLADNSGLSPQTLLDVLDLGAIANPMFKLKGPSMLQGSYNPAFPLKHQ 236
Cdd:PLN02858   484 YVIkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIF 563

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  237 QKDMRLALALGDENAVSMPVAAASNEAFKKARSLGLGDLDFSA---VYEVLKGAGGSGKA 293
Cdd:PLN02858   564 VKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAvvkVYETLTGVKVEGRL 623
PLN02858 PLN02858
fructose-bisphosphate aldolase
 3-283 1.98e-28

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 114.95  E-value: 1.98e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949    3 VGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETPAAVVAKCRYTIAMLSDPSAALSVVFDKDGVLE 82
Cdd:PLN02858     7 VGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDEGAAK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   83 QIGEGKGYVDMSTVDAATSCKISEAIKQKGGA--FVEAPVSGSKKPAEDGQLVILAAGDKVLYDDMVPAFDVLGKKSFFL 160
Cdd:PLN02858    87 GLQKGAVILIRSTILPLQLQKLEKKLTERKEQifLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLYTF 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  161 -GEIGNGAKMKLVVNMIMGSMMNALSEGLSLADNSGLSPQTLLDVLDLGAIANPMFKLKGPSMLQGSYNPAFPLKHQQKD 239
Cdd:PLN02858   167 eGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLNVLVQN 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1002237949  240 MRLALALGDENAVSMPVAAASNEAFKKARSLGLGDLDFSAVYEV 283
Cdd:PLN02858   247 LGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKV 290
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 164-284 6.70e-27

NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidized to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure.


Pssm-ID: 434252 [Multi-domain]  Cd Length: 122  Bit Score: 101.45  E-value: 6.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949 164 GNGAKMKLVVNMIMGSMMNALSEGLSLADNSGLSPQTLLDVLDLGAIANPMFKLKGP-SMLQGSYNPAFPLKHQQKDMRL 242
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPqRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1002237949 243 ALALGDENAVSMPVAAASNEAFKKARSLGLGDLDFSAVYEVL 284
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
1-211 2.31e-12

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 65.93  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   1 MEVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETPAAVVAKcrytiamLSDPSA------ALSVV 74
Cdd:PRK09599    1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAK-------LPAPRVvwlmvpAGEIT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  75 fdkDGVLEQIGE--GKGyvDMsTVDAATS-----CKISEAIKQKGGAFVEAPVSGSKKPAEDGQ-LVIlaAGDKVLYDDM 146
Cdd:PRK09599   74 ---DATIDELAPllSPG--DI-VIDGGNSyykddIRRAELLAEKGIHFVDVGTSGGVWGLERGYcLMI--GGDKEAVERL 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002237949 147 VPAFDVL---GKKSF-FLGEIGNG--AKMklVVNMIMGSMMNALSEGLSLADNSGLspqtlldVLDLGAIA 211
Cdd:PRK09599  146 EPIFKALaprAEDGYlHAGPVGAGhfVKM--VHNGIEYGMMQAYAEGFELLEASRF-------DLDLAAVA 207
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 1-41 5.59e-09

6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate dehydrogenase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 440131 [Multi-domain]  Cd Length: 467  Bit Score: 56.62  E-value: 5.59e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1002237949   1 MEVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVA 41
Cdd:COG0362     3 ADIGVIGLAVMGRNLALNIADHGFSVAVYNRTAEKTDAFLA 43
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 2-186 3.29e-08

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 54.41  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   2 EVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVAlGAAVGETPAAVVAKCRYTIAMLSDPSAALSVV-----FD 76
Cdd:PTZ00142    3 DIGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVK-KAKEGNTRVKGYHTLEELVNSLKKPRKVILLIkageaVD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949  77 K--DGVLEQIGEGKGYVDMSTVDAATSCKISEAIKQKGGAFVEAPVSGSKKPAEDGQlVILAAGDKVLYDDMVPAFDVLG 154
Cdd:PTZ00142   82 EtiDNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDILEKCS 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1002237949 155 KKS------FFLGEIGNGAKMKLVVNMIMGSMMNALSE 186
Cdd:PTZ00142  161 AKVgdspcvTYVGPGSSGHYVKMVHNGIEYGDMQLISE 198
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-61 1.00e-05

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 45.82  E-value: 1.00e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002237949   1 MEVGFLGLGIMGKAMAANLLRHGF---RVTVWNRTLSKCQELVA-LGAAVGETPAAVVAKCRYTI 61
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGVppeDIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVV 67
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 1-32 1.04e-05

Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy dehydrogenase family; This group contains a variety of proteins variously identified as glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase) and other enzymes of the 2-hydroxyacid dehydrogenase family. GDH catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 2-hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240641 [Multi-domain]  Cd Length: 306  Bit Score: 45.95  E-value: 1.04e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1002237949   1 MEVGFLGLGIMGKAMAANLLRHGFRVTVWNRT 32
Cdd:cd12164   133 RRVGVLGLGELGAAVARRLAALGFPVSGWSRS 164
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 2-50 4.76e-05

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 44.71  E-value: 4.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002237949   2 EVGFLGLGIMGKAMAANLLRHGFRVTVWNRTLSKCQELVALGAAVGETP 50
Cdd:PLN02350    8 RIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETVERAKKEGNLP 56
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
11-41 8.03e-05

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 43.57  E-value: 8.03e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1002237949  11 MGKAMAANLLRHGFRVTVWNRTLSKCQELVA 41
Cdd:PRK09287    1 MGKNLALNIASHGYTVAVYNRTPEKTDEFLA 31
Sacchrp_dh_NADP pfam03435
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ...
 3-55 2.11e-03

Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.


Pssm-ID: 397480 [Multi-domain]  Cd Length: 120  Bit Score: 37.18  E-value: 2.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002237949   3 VGFLGLGIMGKAMAANLLRHG--FRVTVWNRTLSKCQELVALGAAVGETPAAVVA 55
Cdd:pfam03435   1 VLIIGAGSVGQGVAPLLARHFdvDRITVADRTLEKAQALAAKLGGVRFIAVAVDA 55
PRK06130 PRK06130
3-hydroxybutyryl-CoA dehydrogenase; Validated
 6-86 3.24e-03

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 235707 [Multi-domain]  Cd Length: 311  Bit Score: 38.60  E-value: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002237949   6 LGLGIMGKAMAANLLRHGFRVTVWN---RTLSKCQELVALGAAVGEtPAAVVAKCRYTIAMLSDPSAAlsvVFDKDGVLE 82
Cdd:PRK06130   10 IGAGTMGSGIAALFARKGLQVVLIDvmeGALERARGVIERALGVYA-PLGIASAGMGRIRMEAGLAAA---VSGADLVIE 85


                  ....
gi 1002237949  83 QIGE 86
Cdd:PRK06130   86 AVPE 89
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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