NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1491298903|gb|RLI63929|]
View 

MAG: NADPH-dependent F420 reductase [Candidatus Gerdarchaeota archaeon]

Protein Classification

NADPH-dependent F420 reductase( domain architecture ID 11449986)

NADPH-dependent F420 reductase may be part of a F420-dependent NADP oxidoreductase catalyzing the reduction of NADP(+) with F420H(2) via hydride transfer, as well as the reverse reaction, the reduction of F420 with NADPH

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0052851|GO:0016491|GO:0070967|GO:0016651
SCOP:  4000104

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
6-225 5.01e-44

Predicted dinucleotide-binding enzyme [General function prediction only];


:

Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 146.47  E-value: 5.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903   6 IGLIpGTGKQSRGIALRLGAAGQQVLIGSRSEEKALRVAEELNKKIgaqmfTGYSNKEVVRKSNLLFLVVPPQYLKKTLQ 85
Cdd:COG2085     1 IGII-GTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAELGPGA-----RAGTNAEAAAAADVVVLAVPYEAVPDVLE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903  86 ELTSEFnKETILVDVTVPLIFKDKRLRwdisvlgVEEHFGSSSEFIQAHVPDGViVVGAFKTISATKL--NALKEPLNVA 163
Cdd:COG2085    75 SLGDAL-AGKIVIDATNPLPERDGFIL-------DPPGGGSAAELVAALLPGAR-VVKAFNTIGAAVLadPARPAGGRRD 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491298903 164 TFLVSDSFEAKLTVKKVLSKiLDLQILDAGPLTVANTIEHMTALVINLNKLNKIKHGsFRIV 225
Cdd:COG2085   146 VFVAGDDAEAKAVVAALIED-LGFDPVDAGPLANARRLEPLTPLLINLARTAGLELG-FRLL 205
 
Name Accession Description Interval E-value
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
6-225 5.01e-44

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 146.47  E-value: 5.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903   6 IGLIpGTGKQSRGIALRLGAAGQQVLIGSRSEEKALRVAEELNKKIgaqmfTGYSNKEVVRKSNLLFLVVPPQYLKKTLQ 85
Cdd:COG2085     1 IGII-GTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAELGPGA-----RAGTNAEAAAAADVVVLAVPYEAVPDVLE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903  86 ELTSEFnKETILVDVTVPLIFKDKRLRwdisvlgVEEHFGSSSEFIQAHVPDGViVVGAFKTISATKL--NALKEPLNVA 163
Cdd:COG2085    75 SLGDAL-AGKIVIDATNPLPERDGFIL-------DPPGGGSAAELVAALLPGAR-VVKAFNTIGAAVLadPARPAGGRRD 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491298903 164 TFLVSDSFEAKLTVKKVLSKiLDLQILDAGPLTVANTIEHMTALVINLNKLNKIKHGsFRIV 225
Cdd:COG2085   146 VFVAGDDAEAKAVVAALIED-LGFDPVDAGPLANARRLEPLTPLLINLARTAGLELG-FRLL 205
npdG TIGR01915
NADPH-dependent F420 reductase; This model represents a subset of a parent family described by ...
 6-224 1.20e-42

NADPH-dependent F420 reductase; This model represents a subset of a parent family described by pfam03807. Unlike the parent family, members of this family are found only in species with evidence of coenzyme F420. All members of this family are believed to act as NADPH-dependent F420 reductase. [Energy metabolism, Electron transport]


Pssm-ID: 273873  Cd Length: 219  Bit Score: 143.40  E-value: 1.20e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903   6 IGLIPGTGKQSRGIALRLGAAGQQVLIGSRSEEKA----LRVAEELNKKIGAQMFTGYSNKEVVRKSNLLFLVVPPQYLK 81
Cdd:TIGR01915   3 IAVLGGTGDQGKGLALRLAKAGNKIIIGSRDLEKAeeaaAKALEELGHGGSDIKVTGADNAEAAKRADVVILAVPWDHVL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903  82 KTLQELTSEFnKETILVDVTVPLIFK-DKRLRWdisvLGVEEhfGSSSEFIQAHVPDGVIVVGAFKTISATKLNALKEPL 160
Cdd:TIGR01915  83 KTLESLRDEL-SGKLVISPVVPLASDgGKGARY----LPPEE--GSAAEQAAALLPETSRVVAAFHNLSAVLLQDVDDEV 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491298903 161 NVATFLVSDSFEAKLTVKKVLSKILDLQILDAGPLTVANTIEHMTALVINLNKLNKIKHGSFRI 224
Cdd:TIGR01915 156 DCDVLVCGDDEEAKEVVAELAGRIDGLRALDAGPLENAAIVESLTPLLINLNRRNKLRDAGIRF 219
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
11-103 1.65e-14

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 66.49  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903  11 GTGKQSRGIALRLGAAGQQ--VLIGSRSEEKALRVAEELNKKIgaqmfTGYSNKEVVRKSNLLFLVVPPQYLKKTLQELT 88
Cdd:pfam03807   4 GAGNMGEALARGLVAAGPHevVVANSRNPEKAEELAEEYGVGA-----TAVDNEEAAEEADVVFLAVKPEDAPDVLSELS 78

                          90
                  ....*....|....*
gi 1491298903  89 SEFnKETILVDVTVP 103
Cdd:pfam03807  79 DLL-KGKIVISIAAG 92
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 5-100 1.85e-07

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 50.34  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903   5 TIGLIpGTGKQSRGIALRLGAAGQQV---LIGSRSEEKALRVAEElnkKIGAQmfTGYSNKEVVRKSNLLFLVVPPQYLK 81
Cdd:PLN02688    2 RVGFI-GAGKMAEAIARGLVASGVVPpsrISTADDSNPARRDVFQ---SLGVK--TAASNTEVVKSSDVIILAVKPQVVK 75

                          90
                  ....*....|....*....
gi 1491298903  82 KTLQELTSEFNKETILVDV 100
Cdd:PLN02688   76 DVLTELRPLLSKDKLLVSV 94
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 11-55 6.26e-03

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. 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 DH, 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: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 36.60  E-value: 6.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1491298903  11 GTGKQSRGIALRLGAAGQQVLIGSRSEEKALRVAEELNKKIGAQM 55
Cdd:cd01078    36 GTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLRARFGEGV 80
 
Name Accession Description Interval E-value
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
6-225 5.01e-44

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 146.47  E-value: 5.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903   6 IGLIpGTGKQSRGIALRLGAAGQQVLIGSRSEEKALRVAEELNKKIgaqmfTGYSNKEVVRKSNLLFLVVPPQYLKKTLQ 85
Cdd:COG2085     1 IGII-GTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAELGPGA-----RAGTNAEAAAAADVVVLAVPYEAVPDVLE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903  86 ELTSEFnKETILVDVTVPLIFKDKRLRwdisvlgVEEHFGSSSEFIQAHVPDGViVVGAFKTISATKL--NALKEPLNVA 163
Cdd:COG2085    75 SLGDAL-AGKIVIDATNPLPERDGFIL-------DPPGGGSAAELVAALLPGAR-VVKAFNTIGAAVLadPARPAGGRRD 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491298903 164 TFLVSDSFEAKLTVKKVLSKiLDLQILDAGPLTVANTIEHMTALVINLNKLNKIKHGsFRIV 225
Cdd:COG2085   146 VFVAGDDAEAKAVVAALIED-LGFDPVDAGPLANARRLEPLTPLLINLARTAGLELG-FRLL 205
npdG TIGR01915
NADPH-dependent F420 reductase; This model represents a subset of a parent family described by ...
 6-224 1.20e-42

NADPH-dependent F420 reductase; This model represents a subset of a parent family described by pfam03807. Unlike the parent family, members of this family are found only in species with evidence of coenzyme F420. All members of this family are believed to act as NADPH-dependent F420 reductase. [Energy metabolism, Electron transport]


Pssm-ID: 273873  Cd Length: 219  Bit Score: 143.40  E-value: 1.20e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903   6 IGLIPGTGKQSRGIALRLGAAGQQVLIGSRSEEKA----LRVAEELNKKIGAQMFTGYSNKEVVRKSNLLFLVVPPQYLK 81
Cdd:TIGR01915   3 IAVLGGTGDQGKGLALRLAKAGNKIIIGSRDLEKAeeaaAKALEELGHGGSDIKVTGADNAEAAKRADVVILAVPWDHVL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903  82 KTLQELTSEFnKETILVDVTVPLIFK-DKRLRWdisvLGVEEhfGSSSEFIQAHVPDGVIVVGAFKTISATKLNALKEPL 160
Cdd:TIGR01915  83 KTLESLRDEL-SGKLVISPVVPLASDgGKGARY----LPPEE--GSAAEQAAALLPETSRVVAAFHNLSAVLLQDVDDEV 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491298903 161 NVATFLVSDSFEAKLTVKKVLSKILDLQILDAGPLTVANTIEHMTALVINLNKLNKIKHGSFRI 224
Cdd:TIGR01915 156 DCDVLVCGDDEEAKEVVAELAGRIDGLRALDAGPLENAAIVESLTPLLINLNRRNKLRDAGIRF 219
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
11-103 1.65e-14

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 66.49  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903  11 GTGKQSRGIALRLGAAGQQ--VLIGSRSEEKALRVAEELNKKIgaqmfTGYSNKEVVRKSNLLFLVVPPQYLKKTLQELT 88
Cdd:pfam03807   4 GAGNMGEALARGLVAAGPHevVVANSRNPEKAEELAEEYGVGA-----TAVDNEEAAEEADVVFLAVKPEDAPDVLSELS 78

                          90
                  ....*....|....*
gi 1491298903  89 SEFnKETILVDVTVP 103
Cdd:pfam03807  79 DLL-KGKIVISIAAG 92
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 5-100 1.85e-07

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 50.34  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903   5 TIGLIpGTGKQSRGIALRLGAAGQQV---LIGSRSEEKALRVAEElnkKIGAQmfTGYSNKEVVRKSNLLFLVVPPQYLK 81
Cdd:PLN02688    2 RVGFI-GAGKMAEAIARGLVASGVVPpsrISTADDSNPARRDVFQ---SLGVK--TAASNTEVVKSSDVIILAVKPQVVK 75

                          90
                  ....*....|....*....
gi 1491298903  82 KTLQELTSEFNKETILVDV 100
Cdd:PLN02688   76 DVLTELRPLLSKDKLLVSV 94
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-134 7.01e-06

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: 45.89  E-value: 7.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903   1 MEKITI---GLIpGTgkqSrgIALRLGAAGQQV-LIGSRSEEKALRVAEELNkkIGAQMFTgySNKEVVRKSNLLFLVVP 76
Cdd:COG0287     1 FMRIAIiglGLI-GG---S--LALALKRAGLAHeVVGVDRSPETLERALELG--VIDRAAT--DLEEAVADADLVVLAVP 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491298903  77 PQYLKKTLQELTSEFNKETILVDVTvplifkdkrlrwdiSVLG-----VEEHFGSSSEFIQAH 134
Cdd:COG0287    71 VGATIEVLAELAPHLKPGAIVTDVG--------------SVKGavveaAEALLPDGVRFVGGH 119
PRK07680 PRK07680
late competence protein ComER; Validated
 29-103 9.57e-05

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 42.27  E-value: 9.57e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491298903  29 QVLIGSRSEEKALRVAEELNKKIGAQmftgySNKEVVRKSNLLFLVVPPQYLKKTLQELTSEFNKETILVDVTVP 103
Cdd:PRK07680   29 QLTITNRTPAKAYHIKERYPGIHVAK-----TIEEVISQSDLIFICVKPLDIYPLLQKLAPHLTDEHCLVSITSP 98
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 4-101 2.19e-04

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 41.51  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903   4 ITIGLIPGTGKQSRGIALRLGAAGQQVLIGSRSEEKALRVAEELnkkiGAQMFTgySNKEVVRKSNLLFLVVPPQYLKKT 83
Cdd:PRK08655    1 MKISIIGGTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKEL----GVEYAN--DNIDAAKDADIVIISVPINVTEDV 74

                          90
                  ....*....|....*...
gi 1491298903  84 LQELTSEFNKETILVDVT 101
Cdd:PRK08655   75 IKEVAPHVKEGSLLMDVT 92
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 6-100 3.91e-04

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 40.39  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491298903   6 IGLIpGTGKQS----RGIaLRLGAAGQQVLIGSRSEEKALRVAEELNKKIGAQmftgySNKEVVRKSNLLFLVVPPQYLK 81
Cdd:PRK06476    3 IGFI-GTGAITeamvTGL-LTSPADVSEIIVSPRNAQIAARLAERFPKVRIAK-----DNQAVVDRSDVVFLAVRPQIAE 75

                          90
                  ....*....|....*....
gi 1491298903  82 KTLQELTseFNKETILVDV 100
Cdd:PRK06476   76 EVLRALR--FRPGQTVISV 92
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 17-49 1.53e-03

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 38.61  E-value: 1.53e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1491298903  17 RGIALRLGAAGQQVLIGSRSEEKALRVAEELNK 49
Cdd:COG1028    20 RAIARALAAEGARVVITDRDAEALEAAAAELRA 52
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 5-76 1.89e-03

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 38.56  E-value: 1.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491298903   5 TIGLIpGTGKQSRGIALRLGAAGQQVLIGSRSEEKALRVAEElnkkiGAQMFTgySNKEVVRKSNLLFLVVP 76
Cdd:COG2084     3 KVGFI-GLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAA-----GARVAA--SPAEAAAAADVVITMLP 66
FabG-like PRK07231
SDR family oxidoreductase;
17-47 4.11e-03

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 37.50  E-value: 4.11e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1491298903  17 RGIALRLGAAGQQVLIGSRSEEKALRVAEEL 47
Cdd:PRK07231   19 EGIARRFAAEGARVVVTDRNEEAAERVAAEI 49
NAD_bind_H4MPT_DH cd01078
NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene ...
 11-55 6.26e-03

NADP binding domain of methylene tetrahydromethanopterin dehydrogenase; Methylene Tetrahydromethanopterin Dehydrogenase (H4MPT DH) NADP binding domain. NADP-dependent H4MPT DH catalyzes the dehydrogenation of methylene- H4MPT and methylene-tetrahydrofolate (H4F) with NADP+ as cofactor. H4F and H4MPT are both cofactors that carry the one-carbon units between the formyl and methyl oxidation level. H4F and H4MPT are structurally analogous to each other with respect to the pterin moiety, but each has distinct side chain. H4MPT is present only in anaerobic methanogenic archaea and aerobic methylotrophic proteobacteria. H4MPT seems to have evolved independently from H4F and functions as a distinct carrier in C1 metabolism. 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 DH, 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: 133446 [Multi-domain]  Cd Length: 194  Bit Score: 36.60  E-value: 6.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1491298903  11 GTGKQSRGIALRLGAAGQQVLIGSRSEEKALRVAEELNKKIGAQM 55
Cdd:cd01078    36 GTGPVGQRAAVLLAREGARVVLVGRDLERAQKAADSLRARFGEGV 80
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH