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Conserved domains on  [gi|1261293051|ref|WP_097820505.1|]
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NAD(P)-dependent oxidoreductase

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 ...
 21-303 6.28e-60

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 193.02  E-value: 6.28e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  21 RKSVTVIGLGPMGQAMADVFLEYGYSLTVWNRTSSKADQLVAKGAIRVSTVNEALAANELVILSLTDYNVMYSIL---EP 97
Cdd:COG2084     1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLlgeDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  98 VSENLF-GKVLVNLSSDTPEKARKAAKWLEDRGAWHITGGVQVPPSGIGKSESYTYYSGDRVVFEAHRETLKVLTSTDYR 176
Cdd:COG2084    81 LLAALRpGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051 177 GEDPGLAMLYYQIQMDIFWTAMLSYLHALAIANANGITAEQFLPY--ASAMMSslpKFVEFYTPRLDEGEH-PGdvDRLA 253
Cdd:COG2084   161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVlsGGAAGS---WVLENRGPRMLAGDFdPG--FALD 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1261293051 254 MGLASVEHVVHTTQEAGIDIALPATVLEVFRRGMKTGHASDSFTSLIETF 303
Cdd:COG2084   236 LMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 21-303 6.28e-60

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 193.02  E-value: 6.28e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  21 RKSVTVIGLGPMGQAMADVFLEYGYSLTVWNRTSSKADQLVAKGAIRVSTVNEALAANELVILSLTDYNVMYSIL---EP 97
Cdd:COG2084     1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLlgeDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  98 VSENLF-GKVLVNLSSDTPEKARKAAKWLEDRGAWHITGGVQVPPSGIGKSESYTYYSGDRVVFEAHRETLKVLTSTDYR 176
Cdd:COG2084    81 LLAALRpGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051 177 GEDPGLAMLYYQIQMDIFWTAMLSYLHALAIANANGITAEQFLPY--ASAMMSslpKFVEFYTPRLDEGEH-PGdvDRLA 253
Cdd:COG2084   161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVlsGGAAGS---WVLENRGPRMLAGDFdPG--FALD 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1261293051 254 MGLASVEHVVHTTQEAGIDIALPATVLEVFRRGMKTGHASDSFTSLIETF 303
Cdd:COG2084   236 LMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 23-137 3.50e-18

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: 79.82  E-value: 3.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  23 SVTVIGLGPMGQAMADVFLEYGYSLTVWNRTSSKADQLVAKGAIRVSTVNEALAANELVILSLTDYNVMYSIL--EPVSE 100
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIfgEGLLP 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1261293051 101 NLF-GKVLVNLSSDTPEKARKAAKWLEDRGAWHITGGV 137
Cdd:pfam03446  81 GLKpGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPV 118
garR PRK11559
tartronate semialdehyde reductase; Provisional
 27-303 8.73e-11

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 61.61  E-value: 8.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  27 IGLGPMGQAMADVFLEYGYSLTVWNRTSSKADQLVAKGAIRVSTVNEALAANELVILSLTDYNV-------MYSILEPVS 99
Cdd:PRK11559    8 IGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHvkevalgENGIIEGAK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051 100 EnlfGKVLVNLSSDTPEKARKAAKWLEDRGAWHI----TGGvqvPPSGIGKSESYTyYSGDRVVFEAHRETLKVLTSTDY 175
Cdd:PRK11559   88 P---GTVVIDMSSIAPLASREIAAALKAKGIEMLdapvSGG---EPKAIDGTLSVM-VGGDKAIFDKYYDLMKAMAGSVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051 176 RGEDPG---LAMLYYQIQMDIFWTAMlsyLHALAIANANGITAEqfLPY--------ASAMMSSLPKFVefytprLDEGE 244
Cdd:PRK11559  161 HTGDIGagnVTKLANQVIVALNIAAM---SEALVLATKAGVNPD--LVYqairgglaGSTVLDAKAPMV------MDRNF 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293051 245 HPGdvDRLAMGLASVEHVVHTTQEAGIDIALPATVLEVFRRGMKTGHASDSFTSLIETF 303
Cdd:PRK11559  230 KPG--FRIDLHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYY 286
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 22-82 5.66e-03

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 36.87  E-value: 5.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261293051  22 KSVTVIGLGPMGQAMADVFLEYGYS-LTVWNRTSSKADQLVAKGAIRVSTVN-----EALAANELVI 82
Cdd:cd01065    20 KKVLILGAGGAARAVAYALAELGAAkIVIVNRTLEKAKALAERFGELGIAIAyldleELLAEADLII 86
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 21-303 6.28e-60

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 193.02  E-value: 6.28e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  21 RKSVTVIGLGPMGQAMADVFLEYGYSLTVWNRTSSKADQLVAKGAIRVSTVNEALAANELVILSLTDYNVMYSIL---EP 97
Cdd:COG2084     1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLlgeDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  98 VSENLF-GKVLVNLSSDTPEKARKAAKWLEDRGAWHITGGVQVPPSGIGKSESYTYYSGDRVVFEAHRETLKVLTSTDYR 176
Cdd:COG2084    81 LLAALRpGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051 177 GEDPGLAMLYYQIQMDIFWTAMLSYLHALAIANANGITAEQFLPY--ASAMMSslpKFVEFYTPRLDEGEH-PGdvDRLA 253
Cdd:COG2084   161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVlsGGAAGS---WVLENRGPRMLAGDFdPG--FALD 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1261293051 254 MGLASVEHVVHTTQEAGIDIALPATVLEVFRRGMKTGHASDSFTSLIETF 303
Cdd:COG2084   236 LMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 23-137 3.50e-18

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: 79.82  E-value: 3.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  23 SVTVIGLGPMGQAMADVFLEYGYSLTVWNRTSSKADQLVAKGAIRVSTVNEALAANELVILSLTDYNVMYSIL--EPVSE 100
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIfgEGLLP 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1261293051 101 NLF-GKVLVNLSSDTPEKARKAAKWLEDRGAWHITGGV 137
Cdd:pfam03446  81 GLKpGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPV 118
garR PRK11559
tartronate semialdehyde reductase; Provisional
 27-303 8.73e-11

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 61.61  E-value: 8.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  27 IGLGPMGQAMADVFLEYGYSLTVWNRTSSKADQLVAKGAIRVSTVNEALAANELVILSLTDYNV-------MYSILEPVS 99
Cdd:PRK11559    8 IGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHvkevalgENGIIEGAK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051 100 EnlfGKVLVNLSSDTPEKARKAAKWLEDRGAWHI----TGGvqvPPSGIGKSESYTyYSGDRVVFEAHRETLKVLTSTDY 175
Cdd:PRK11559   88 P---GTVVIDMSSIAPLASREIAAALKAKGIEMLdapvSGG---EPKAIDGTLSVM-VGGDKAIFDKYYDLMKAMAGSVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051 176 RGEDPG---LAMLYYQIQMDIFWTAMlsyLHALAIANANGITAEqfLPY--------ASAMMSSLPKFVefytprLDEGE 244
Cdd:PRK11559  161 HTGDIGagnVTKLANQVIVALNIAAM---SEALVLATKAGVNPD--LVYqairgglaGSTVLDAKAPMV------MDRNF 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1261293051 245 HPGdvDRLAMGLASVEHVVHTTQEAGIDIALPATVLEVFRRGMKTGHASDSFTSLIETF 303
Cdd:PRK11559  230 KPG--FRIDLHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYY 286
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
27-129 2.46e-08

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 54.09  E-value: 2.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  27 IGLGPMGQAMADVFLEYGYSLTVWNRTSSKADQLVAKGAIRVSTVNEALAANELVILSLTDYNVMYSILE---PVSENLF 103
Cdd:PRK15461    7 IGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFgenGVCEGLS 86

                          90       100
                  ....*....|....*....|....*..
gi 1261293051 104 GKVLV-NLSSDTPEKARKAAKWLEDRG 129
Cdd:PRK15461   87 RDALViDMSTIHPLQTDKLIADMQAKG 113
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 22-108 9.80e-08

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: 51.99  E-value: 9.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  22 KSVTVIGLGPMGQAMADVFLEYGYS---LTVWNRTSSKADQLVAKGAIRVSTVNEALAAN-ELVILSLTDYnVMYSILEP 97
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAERYGVRVTTDNAEAAAQaDVVVLAVKPQ-DLAEVLEE 81

                          90
                  ....*....|.
gi 1261293051  98 VSENLFGKVLV 108
Cdd:COG0345    82 LAPLLDPDKLV 92
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
27-170 3.81e-06

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 47.71  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  27 IGLGPMGQAMADVFLEYGYSLTVwNRTSSKADQLVAKGAIRVSTVNEALAANELVILSLTDY----NVMYSILEPVSENL 102
Cdd:PRK15059    6 IGLGIMGTPMAINLARAGHQLHV-TTIGPVADELLSLGAVSVETARQVTEASDIIFIMVPDTpqveEVLFGENGCTKASL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1261293051 103 FGKVLVNLSSDTPEKARKAAKWLEDRGAWHItggvQVPPSG--IGKSESY--TYYSGDRVVFEAHRETLKVL 170
Cdd:PRK15059   85 KGKTIVDMSSISPIETKRFARQVNELGGDYL----DAPVSGgeIGAREGTlsIMVGGDEAVFERVKPLFELL 152
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 26-65 2.58e-05

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: 45.45  E-value: 2.58e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1261293051  26 VIGLGPMGQAMADVFLEYGYSLTVWNRTSSKADQLVAKGA 65
Cdd:COG0362     7 VIGLAVMGRNLALNIADHGFSVAVYNRTAEKTDAFLAEHG 46
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
26-77 4.24e-05

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 44.35  E-value: 4.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1261293051  26 VIGLGPMGQAMADVFLEYGYSLTVWNRTSSKADQLVAKGAIRVSTVNEALAA 77
Cdd:PRK09599    5 MIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAK 56
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
26-108 4.49e-05

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 41.45  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  26 VIGLGPMGQAMADVFLEYGYS--LTVWNRTSSKADQLVAKGAIRVSTVN--EALAANELVILSLTdYNVMYSILEPVSEN 101
Cdd:pfam03807   2 FIGAGNMGEALARGLVAAGPHevVVANSRNPEKAEELAEEYGVGATAVDneEAAEEADVVFLAVK-PEDAPDVLSELSDL 80


                  ....*..
gi 1261293051 102 LFGKVLV 108
Cdd:pfam03807  81 LKGKIVI 87
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 22-84 3.61e-04

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 39.86  E-value: 3.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1261293051  22 KSVTVIGLGPMGQAMADVFLEYGY-SLTVWNRTSSKADQLVAK----GAIRVSTVNEALAANELVILS 84
Cdd:pfam01488  13 KKVLLIGAGEMGELVAKHLLAKGAkEVTIANRTIERAQELAEKfggvEALPLDDLKEYLAEADIVISA 80
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 20-82 3.89e-04

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 41.71  E-value: 3.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261293051  20 NRKSVTVIGLGPMGQAMADVFLEYGYS-LTVWNRTSSKADQLVAK---GAIRVSTVNEALAANELVI 82
Cdd:PRK00045  181 SGKKVLVIGAGEMGELVAKHLAEKGVRkITVANRTLERAEELAEEfggEAIPLDELPEALAEADIVI 247
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 26-63 4.20e-03

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 38.62  E-value: 4.20e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1261293051  26 VIGLGPMGQAMADVFLEYGYSLTVWNRTSSKADQLVAK 63
Cdd:PTZ00142    6 LIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVKK 43
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 22-82 5.12e-03

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 38.17  E-value: 5.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1261293051  22 KSVTVIGLGPMGQAMADVFLEYGYS-LTVWNRTSSKADQLVAK---GAIRVSTVNEALAANELVI 82
Cdd:COG0373   183 KTVLVIGAGEMGELAARHLAAKGVKrITVANRTLERAEELAEEfggEAVPLEELPEALAEADIVI 247
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 23-102 5.43e-03

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 37.13  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1261293051  23 SVTVIGLGPMGQAMADVFLEYGYSLTV-----------WNRTSSKADQLVAKGAIRVSTVNEALAAnelvILSLTDYNVM 91
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLvdiseealekaLERIESSLERLVEKGRITEEEVDAALAR----ISFTTDLAAA 76

                          90
                  ....*....|....
gi 1261293051  92 YS---ILEPVSENL 102
Cdd:pfam02737  77 VDadlVIEAVPENL 90
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 22-82 5.66e-03

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 36.87  E-value: 5.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1261293051  22 KSVTVIGLGPMGQAMADVFLEYGYS-LTVWNRTSSKADQLVAKGAIRVSTVN-----EALAANELVI 82
Cdd:cd01065    20 KKVLILGAGGAARAVAYALAELGAAkIVIVNRTLEKAKALAERFGELGIAIAyldleELLAEADLII 86
 
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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