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Conserved domains on  [gi|1034586145|ref|XP_016876458|]
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NADP-dependent oxidoreductase domain-containing protein 1 isoform X3 [Homo sapiens]

Protein Classification

pyrroline-5-carboxylate reductase( domain architecture ID 11417420)

pyrroline-5-carboxylate reductase catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 78-177 8.40e-17

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: 77.03  E-value: 8.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586145  78 KVGIIGGGHLGKQLAGTLLQLGpIPAESLRISTRRPETLGEL-QKLGIKCFYHNADLVSWADVIFLCCLPSQLPNICVEI 156
Cdd:COG0345     4 KIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALaERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEEL 82

                          90       100
                  ....*....|....*....|.
gi 1034586145 157 YTSLEKASIVYSFVAAIPLPR 177
Cdd:COG0345    83 APLLDPDKLVISIAAGVTLAT 103
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 78-177 8.40e-17

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: 77.03  E-value: 8.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586145  78 KVGIIGGGHLGKQLAGTLLQLGpIPAESLRISTRRPETLGEL-QKLGIKCFYHNADLVSWADVIFLCCLPSQLPNICVEI 156
Cdd:COG0345     4 KIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALaERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEEL 82

                          90       100
                  ....*....|....*....|.
gi 1034586145 157 YTSLEKASIVYSFVAAIPLPR 177
Cdd:COG0345    83 APLLDPDKLVISIAAGVTLAT 103
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 78-175 2.97e-13

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 67.09  E-value: 2.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586145  78 KVGIIGGGHLGKQLAGTLLQLGpIPAESLRISTRRPETLGEL-QKLGIKCFYHNADLVSWADVIFLCCLPSQLPNICVEI 156
Cdd:PRK11880    4 KIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALaEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLSEL 82

                          90
                  ....*....|....*....
gi 1034586145 157 YTSLEKasIVYSFVAAIPL 175
Cdd:PRK11880   83 KGQLDK--LVVSIAAGVTL 99
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
80-171 1.20e-10

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 56.47  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586145  80 GIIGGGHLGKQLAGTLLQLGPipaESLRISTRR-PETLGEL-QKLGIKCF-YHNADLVSWADVIFLCCLPSQLPNICVEI 156
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGP---HEVVVANSRnPEKAEELaEEYGVGATaVDNEEAAEEADVVFLAVKPEDAPDVLSEL 77

                          90
                  ....*....|....*
gi 1034586145 157 YTSLeKASIVYSFVA 171
Cdd:pfam03807  78 SDLL-KGKIVISIAA 91
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 73-146 6.50e-03

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: 37.09  E-value: 6.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034586145  73 TPEEFKVGIIGGGHLGKQLAGTLLQLGpipaesLRIS--TRRPETLGelqklGIKCFYHNADL---VSWADvIFLCCLP 146
Cdd:cd12164   129 PAAERRVGVLGLGELGAAVARRLAALG------FPVSgwSRSPKDIE-----GVTCFHGEEGLdafLAQTD-ILVCLLP 195
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 78-177 8.40e-17

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: 77.03  E-value: 8.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586145  78 KVGIIGGGHLGKQLAGTLLQLGpIPAESLRISTRRPETLGEL-QKLGIKCFYHNADLVSWADVIFLCCLPSQLPNICVEI 156
Cdd:COG0345     4 KIGFIGAGNMGSAIIKGLLKSG-VPPEDIIVSDRSPERLEALaERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEEL 82

                          90       100
                  ....*....|....*....|.
gi 1034586145 157 YTSLEKASIVYSFVAAIPLPR 177
Cdd:COG0345    83 APLLDPDKLVISIAAGVTLAT 103
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 78-175 2.97e-13

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 67.09  E-value: 2.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586145  78 KVGIIGGGHLGKQLAGTLLQLGpIPAESLRISTRRPETLGEL-QKLGIKCFYHNADLVSWADVIFLCCLPSQLPNICVEI 156
Cdd:PRK11880    4 KIGFIGGGNMASAIIGGLLASG-VPAKDIIVSDPSPEKRAALaEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLSEL 82

                          90
                  ....*....|....*....
gi 1034586145 157 YTSLEKasIVYSFVAAIPL 175
Cdd:PRK11880   83 KGQLDK--LVVSIAAGVTL 99
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
80-171 1.20e-10

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 56.47  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586145  80 GIIGGGHLGKQLAGTLLQLGPipaESLRISTRR-PETLGEL-QKLGIKCF-YHNADLVSWADVIFLCCLPSQLPNICVEI 156
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGP---HEVVVANSRnPEKAEELaEEYGVGATaVDNEEAAEEADVVFLAVKPEDAPDVLSEL 77

                          90
                  ....*....|....*
gi 1034586145 157 YTSLeKASIVYSFVA 171
Cdd:pfam03807  78 SDLL-KGKIVISIAA 91
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 77-175 3.70e-10

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 58.43  E-value: 3.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586145  77 FKVGIIGGGHLGKQLAGTLLQLGPIPAESLRISTRRPETLGEL-QKLGIKCFYHNADLVSWADVIFLCCLPSQLPNICVE 155
Cdd:PLN02688    1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRDVfQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTE 80

                          90       100
                  ....*....|....*....|
gi 1034586145 156 IYTSLEKASIVYSFVAAIPL 175
Cdd:PLN02688   81 LRPLLSKDKLLVSVAAGITL 100
PRK07680 PRK07680
late competence protein ComER; Validated
 78-173 3.69e-06

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 46.50  E-value: 3.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586145  78 KVGIIGGGHLGKQLAGTLLQLGPIPAESLRISTRRPETLGELQKL--GIKCFYHNADLVSWADVIFLCCLPSQLPNICVE 155
Cdd:PRK07680    2 NIGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERypGIHVAKTIEEVISQSDLIFICVKPLDIYPLLQK 81

                          90
                  ....*....|....*...
gi 1034586145 156 IYTSLEKASIVYSFVAAI 173
Cdd:PRK07680   82 LAPHLTDEHCLVSITSPI 99
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 78-143 5.26e-04

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 40.10  E-value: 5.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034586145  78 KVGIIGGGHLGKQLAGTLLQLGpipaESLRISTRRPETLGELQKLGIKCFYHNADLVSWADVIFLC 143
Cdd:COG2084     3 KVGFIGLGAMGAPMARNLLKAG----HEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITM 64
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 78-143 7.39e-04

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: 38.99  E-value: 7.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034586145  78 KVGIIGGGHLGKQLAGTLLQLGpipaESLRISTRRPETLGELQKLGIKCFYHNADLVSWADVIFLC 143
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAG----YTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITM 62
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 78-166 1.95e-03

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 38.57  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586145  78 KVGIIGGGHLGKQLAGTLLQLGPipAESLRISTRRPETLGELQKLGI--KCFYHNADLVSWADVIFLCCLPSQLPNICVE 155
Cdd:COG0287     3 RIAIIGLGLIGGSLALALKRAGL--AHEVVGVDRSPETLERALELGVidRAATDLEEAVADADLVVLAVPVGATIEVLAE 80

                          90
                  ....*....|.
gi 1034586145 156 IYTSLEKASIV 166
Cdd:COG0287    81 LAPHLKPGAIV 91
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 78-177 4.75e-03

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 37.44  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034586145  78 KVGIIGGGHLGKQLAGTLLQLGPIPAESLRISTRRP-ETLGELQKL--GIKCFYHNADLVSWADVIFLCCLPSQLPNICV 154
Cdd:PRK06928    3 KIGFIGYGSMADMIATKLLETEVATPEEIILYSSSKnEHFNQLYDKypTVELADNEAEIFTKCDHSFICVPPLAVLPLLK 82

                          90       100
                  ....*....|....*....|...
gi 1034586145 155 EIYTSLEKASIVYSFVAAIPLPR 177
Cdd:PRK06928   83 DCAPVLTPDRHVVSIAAGVSLDD 105
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 73-146 6.50e-03

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: 37.09  E-value: 6.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034586145  73 TPEEFKVGIIGGGHLGKQLAGTLLQLGpipaesLRIS--TRRPETLGelqklGIKCFYHNADL---VSWADvIFLCCLP 146
Cdd:cd12164   129 PAAERRVGVLGLGELGAAVARRLAALG------FPVSgwSRSPKDIE-----GVTCFHGEEGLdafLAQTD-ILVCLLP 195
 
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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