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Conserved domains on  [gi|494882164|ref|WP_007608214|]
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NADPH-dependent F420 reductase [Rhizobium sp. PDO1-076]

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

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List of domain hits

 Name Accession Description Interval E-value
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
3-206 2.99e-58

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


:

Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 183.45  E-value: 2.99e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   3 IGILGTGNMGRVLTRKLAAAGHDVKVAnSRGPQTIEAEVLETG--AQAVTTEDAVKDVEVVIMTMPhpaFERIRQLIAAL 80
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAAGHEVVIG-SRDPEKAAALAAELGpgARAGTNAEAAAAADVVVLAVP---YEAVPDVLESL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164  81 PEE---TVVIDISNYFPGRDPVNPELDSDIAESEWVRDYF-GRPIAKAWNSIGMVSFETKGMPkgQPGRVALPVSADRGH 156
Cdd:COG2085   77 GDAlagKIVIDATNPLPERDGFILDPPGGGSAAELVAALLpGARVVKAFNTIGAAVLADPARP--AGGRRDVFVAGDDAE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 494882164 157 DRDIAMALVDDTGFDGFDAGSLADSWRQQPGSPVYITDLTYDEMGPALAL 206
Cdd:COG2085  155 AKAVVAALIEDLGFDPVDAGPLANARRLEPLTPLLINLARTAGLELGFRL 204
 
Name Accession Description Interval E-value
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
3-206 2.99e-58

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 183.45  E-value: 2.99e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   3 IGILGTGNMGRVLTRKLAAAGHDVKVAnSRGPQTIEAEVLETG--AQAVTTEDAVKDVEVVIMTMPhpaFERIRQLIAAL 80
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAAGHEVVIG-SRDPEKAAALAAELGpgARAGTNAEAAAAADVVVLAVP---YEAVPDVLESL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164  81 PEE---TVVIDISNYFPGRDPVNPELDSDIAESEWVRDYF-GRPIAKAWNSIGMVSFETKGMPkgQPGRVALPVSADRGH 156
Cdd:COG2085   77 GDAlagKIVIDATNPLPERDGFILDPPGGGSAAELVAALLpGARVVKAFNTIGAAVLADPARP--AGGRRDVFVAGDDAE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 494882164 157 DRDIAMALVDDTGFDGFDAGSLADSWRQQPGSPVYITDLTYDEMGPALAL 206
Cdd:COG2085  155 AKAVVAALIEDLGFDPVDAGPLANARRLEPLTPLLINLARTAGLELGFRL 204
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
4-92 3.72e-19

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 79.20  E-value: 3.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164    4 GILGTGNMGRVLTRKLAAAG-HDVKVANSRGPQTIE--AEVLETGAQAVTTEDAVKDVEVVIMTMPHPAFERIRQLIAAL 80
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGpHEVVVANSRNPEKAEelAEEYGVGATAVDNEEAAEEADVVFLAVKPEDAPDVLSELSDL 80

                          90
                  ....*....|..
gi 494882164   81 PEETVVIDISNY 92
Cdd:pfam03807  81 LKGKIVISIAAG 92
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 1-89 8.84e-09

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 54.99  E-value: 8.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILG-TGNMGRVLTRKLAAAGHDVKVAnSRGPQTIEAEVLETGAQAVTT-EDAVKDVEVVIMTMPHPAFER-IRQLI 77
Cdd:PRK08655   1 MKISIIGgTGGLGKWFARFLKEKGFEVIVT-GRDPKKGKEVAKELGVEYANDnIDAAKDADIVIISVPINVTEDvIKEVA 79

                         90
                 ....*....|..
gi 494882164  78 AALPEETVVIDI 89
Cdd:PRK08655  80 PHVKEGSLLMDV 91
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 1-105 4.31e-04

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 41.06  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164    1 MKIGILGTGNMGRVLTRKLAAAGHDV--------KVANSR---------GPQTIEAEVLETGAQAVTTE--DAVKDVEVV 61
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVtgvdidqeKVDKLNkgkspiyepGLDELLAKALKAGRLRATTDyeEAIRDADVI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 494882164   62 IMTMPHPAFER-----------IRQLIAALPEETVVIDISNYFPG--RDPVNPELDS 105
Cdd:TIGR03026  81 IICVPTPLKEDgspdlsyvesaAETIAKHLRKGATVVLESTVPPGttEEVVKPILER 137
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
 1-64 1.13e-03

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 39.62  E-value: 1.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVKVANSRGPQTIEAEVLETGA----QAVTTEDAVKDVEVVIMT 64
Cdd:cd05229    1 TAHVLGASGPIGREVARELRRRGWDVRLVSRSGSKLAWLPGVEIVAadamDASSVIAAARGADVIYHC 68
 
Name Accession Description Interval E-value
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
3-206 2.99e-58

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


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 183.45  E-value: 2.99e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   3 IGILGTGNMGRVLTRKLAAAGHDVKVAnSRGPQTIEAEVLETG--AQAVTTEDAVKDVEVVIMTMPhpaFERIRQLIAAL 80
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAAGHEVVIG-SRDPEKAAALAAELGpgARAGTNAEAAAAADVVVLAVP---YEAVPDVLESL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164  81 PEE---TVVIDISNYFPGRDPVNPELDSDIAESEWVRDYF-GRPIAKAWNSIGMVSFETKGMPkgQPGRVALPVSADRGH 156
Cdd:COG2085   77 GDAlagKIVIDATNPLPERDGFILDPPGGGSAAELVAALLpGARVVKAFNTIGAAVLADPARP--AGGRRDVFVAGDDAE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 494882164 157 DRDIAMALVDDTGFDGFDAGSLADSWRQQPGSPVYITDLTYDEMGPALAL 206
Cdd:COG2085  155 AKAVVAALIEDLGFDPVDAGPLANARRLEPLTPLLINLARTAGLELGFRL 204
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
4-92 3.72e-19

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 79.20  E-value: 3.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164    4 GILGTGNMGRVLTRKLAAAG-HDVKVANSRGPQTIE--AEVLETGAQAVTTEDAVKDVEVVIMTMPHPAFERIRQLIAAL 80
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGpHEVVVANSRNPEKAEelAEEYGVGATAVDNEEAAEEADVVFLAVKPEDAPDVLSELSDL 80

                          90
                  ....*....|..
gi 494882164   81 PEETVVIDISNY 92
Cdd:pfam03807  81 LKGKIVISIAAG 92
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-90 4.96e-14

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 69.76  E-value: 4.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVKVANsRGPQTIEAeVLETGAQAVTT-EDAVKDVEVVIMTMPHPA-----FERIR 74
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWN-RTPAKAEA-LVAAGARVAASpAEAAAAADVVITMLPDDAaveevLLGED 79

                         90
                 ....*....|....*.
gi 494882164  75 QLIAALPEETVVIDIS 90
Cdd:COG2084   80 GLLAALRPGAVVVDMS 95
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-94 1.25e-11

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: 60.95  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164    2 KIGILGTGNMGRVLTRKLAAAGHDVKVANsRGPQTIEaEVLETGAQAVTT-EDAVKDVEVVIMTMPHPA------FEriR 74
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYN-RTPEKVE-ELVAAGAIAAASpAEFVAGLDVVITMVPAGAavdaviFG--E 76

                          90       100
                  ....*....|....*....|
gi 494882164   75 QLIAALPEETVVIDISNYFP 94
Cdd:pfam03446  77 GLLPGLKPGDIIIDGSTSSP 96
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 1-89 8.84e-09

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 54.99  E-value: 8.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILG-TGNMGRVLTRKLAAAGHDVKVAnSRGPQTIEAEVLETGAQAVTT-EDAVKDVEVVIMTMPHPAFER-IRQLI 77
Cdd:PRK08655   1 MKISIIGgTGGLGKWFARFLKEKGFEVIVT-GRDPKKGKEVAKELGVEYANDnIDAAKDADIVIISVPINVTEDvIKEVA 79

                         90
                 ....*....|..
gi 494882164  78 AALPEETVVIDI 89
Cdd:PRK08655  80 PHVKEGSLLMDV 91
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-87 1.05e-08

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 54.43  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVKVANSRGPQTIEAEVLETGAQAVTT-EDAVKDVEVVIMTMPHPAFERIRQLIAA 79
Cdd:COG5495    4 MKIGIIGAGRVGTALAAALRAAGHEVVGVYSRSPASAERAAALLGAVPALDlEELAAEADLVLLAVPDDAIAEVAAGLAA 83

                         90
                 ....*....|.
gi 494882164  80 ---LPEETVVI 87
Cdd:COG5495   84 agaLRPGQLVV 94
PRK08306 PRK08306
dipicolinate synthase subunit DpsA;
5-90 3.60e-08

dipicolinate synthase subunit DpsA;


Pssm-ID: 181371 [Multi-domain]  Cd Length: 296  Bit Score: 52.92  E-value: 3.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   5 ILGTGNMGRVLTRKLAAAGHDVKVAnSRGPQTIeAEVLETGAQAVTT---EDAVKDVEVVIMTMPHPAFEriRQLIAALP 81
Cdd:PRK08306 157 VLGFGRTGMTLARTLKALGANVTVG-ARKSAHL-ARITEMGLSPFHLselAEEVGKIDIIFNTIPALVLT--KEVLSKMP 232


                 ....*....
gi 494882164  82 EETVVIDIS 90
Cdd:PRK08306 233 PEALIIDLA 241
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-87 1.62e-07

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 51.01  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVK-VANSRGPQTIEAEVLE-TGA---------QAVTTEDAVKDVEVVIMTMPHPA 69
Cdd:COG1893    1 MKIAILGAGAIGGLLGARLARAGHDVTlVARGAHAEALRENGLRlESPdgdrttvpvPAVTDPEELGPADLVLVAVKAYD 80

                         90
                 ....*....|....*....
gi 494882164  70 FER-IRQLIAALPEETVVI 87
Cdd:COG1893   81 LEAaAEALAPLLGPDTVVL 99
PRK07417 PRK07417
prephenate/arogenate dehydrogenase;
1-89 1.87e-07

prephenate/arogenate dehydrogenase;


Pssm-ID: 180970 [Multi-domain]  Cd Length: 279  Bit Score: 50.66  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVkVANSRGPQTIEAEVLETGAQAVTTEDAV-KDVEVVIMTMP-----HPAferiR 74
Cdd:PRK07417   1 MKIGIVGLGLIGGSLGLDLRSLGHTV-YGVSRRESTCERAIERGLVDEASTDLSLlKDCDLVILALPiglllPPS----E 75

                         90
                 ....*....|....*
gi 494882164  75 QLIAALPEETVVIDI 89
Cdd:PRK07417  76 QLIPALPPEAIVTDV 90
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-99 3.62e-07

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: 49.68  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAG---HDVKVANsRGPQTIEAEVLETGAQAVTT-EDAVKDVEVVIMTM-PHPAFERIRQ 75
Cdd:COG0345    3 MKIGFIGAGNMGSAIIKGLLKSGvppEDIIVSD-RSPERLEALAERYGVRVTTDnAEAAAQADVVVLAVkPQDLAEVLEE 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 494882164  76 LIAALPEETVVI---------DISNYFPGRDPV 99
Cdd:COG0345   82 LAPLLDPDKLVIsiaagvtlaTLEEALGGGAPV 114
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-94 1.66e-06

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 48.12  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVKVANsRGPQTIeAEVLETGAQAVTTEDAVKDVEVVIMTMpHPAFERIRQ----- 75
Cdd:PRK11559   3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYD-RNPEAV-AEVIAAGAETASTAKAVAEQCDVIITM-LPNSPHVKEvalge 79

                         90       100
                 ....*....|....*....|.
gi 494882164  76 --LIAALPEETVVIDISNYFP 94
Cdd:PRK11559  80 ngIIEGAKPGTVVIDMSSIAP 100
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
1-88 4.12e-06

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 46.67  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVkVANSRGPQTIEAEVlETGAQAVTT-EDAVKDVE---VVIMTMPH--PAFERIR 74
Cdd:PRK09599   1 MQLGMIGLGRMGGNMARRLLRGGHEV-VGYDRNPEAVEALA-EEGATGADSlEELVAKLPaprVVWLMVPAgeITDATID 78

                         90
                 ....*....|....
gi 494882164  75 QLIAALPEETVVID 88
Cdd:PRK09599  79 ELAPLLSPGDIVID 92
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-90 4.92e-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: 46.66  E-value: 4.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVKV-ANSRGPQTIEaEVLETGA--QAVTT-EDAVKDVEVVIMTMPHPAFERI-RQ 75
Cdd:COG0287    2 MRIAIIGLGLIGGSLALALKRAGLAHEVvGVDRSPETLE-RALELGVidRAATDlEEAVADADLVVLAVPVGATIEVlAE 80

                         90
                 ....*....|....*
gi 494882164  76 LIAALPEETVVIDIS 90
Cdd:COG0287   81 LAPHLKPGAIVTDVG 95
PLN02968 PLN02968
Probable N-acetyl-gamma-glutamyl-phosphate reductase
 2-102 3.49e-05

Probable N-acetyl-gamma-glutamyl-phosphate reductase


Pssm-ID: 215522 [Multi-domain]  Cd Length: 381  Bit Score: 44.43  E-value: 3.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   2 KIGILG-TGNMGRVLTRKLAAAGH-DVKV--ANSRGPQTIEAEVLETGAQAVTTEDAVKD-----VEVVIMTMPHPAFER 72
Cdd:PLN02968  40 RIFVLGaSGYTGAEVRRLLANHPDfEITVmtADRKAGQSFGSVFPHLITQDLPNLVAVKDadfsdVDAVFCCLPHGTTQE 119

                         90       100       110
                 ....*....|....*....|....*....|
gi 494882164  73 IrqlIAALPEETVVIDISNYFPGRDPVNPE 102
Cdd:PLN02968 120 I---IKALPKDLKIVDLSADFRLRDIAEYE 146
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 2-80 4.03e-05

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 43.30  E-value: 4.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   2 KIGILG-TGNMGRVLTRKLAAAGHDVKVAnSRGPQTiEAEVLETGAQAV--------TTEDAVKDVEVVIMTMP---HPA 69
Cdd:COG0702    1 KILVTGaTGFIGRRVVRALLARGHPVRAL-VRDPEK-AAALAAAGVEVVqgdlddpeSLAAALAGVDAVFLLVPsgpGGD 78

                         90
                 ....*....|.
gi 494882164  70 FERIRQLIAAL 80
Cdd:COG0702   79 FAVDVEGARNL 89
NAD_Gly3P_dh_N pfam01210
NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent ...
 2-111 7.86e-05

NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus; NAD-dependent glycerol-3-phosphate dehydrogenase (GPDH) catalyzes the interconversion of dihydroxyacetone phosphate and L-glycerol-3-phosphate. This family represents the N-terminal NAD-binding domain.


Pssm-ID: 395967 [Multi-domain]  Cd Length: 158  Bit Score: 41.79  E-value: 7.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164    2 KIGILGTGNMGRVLTRKLAAAGHDVKVAnSRGPQTIEA-------------EVLETGAQAVTT-EDAVKDVEVVIMTMPH 67
Cdd:pfam01210   1 KIAVLGAGSWGTALAKVLADNGHEVRLW-GRDEELIEEintthenvrylpgIKLPENLKATTDlAEALKGADIIVIVVPS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 494882164   68 PAFERI-RQLIAALPEETVVIDISNyfpGRDPVNPELDSDIAESE 111
Cdd:pfam01210  80 QALREVlKQLKGLLKPDAILVSLSK---GIEPGTLKLLSEVIEEE 121
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 1-90 7.99e-05

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 42.10  E-value: 7.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164    1 MKIGILGTGNMGRVLTRKLAAAGHDVKVANSRGPQTIEAEVLetGAQAVTTEDAVKDVEVVIMTMP-HPAFERI--RQLI 77
Cdd:pfam02826  37 KTVGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEEL--GARYVSLDELLAESDVVSLHLPlTPETRHLinAERL 114

                          90
                  ....*....|...
gi 494882164   78 AALPEETVVIDIS 90
Cdd:pfam02826 115 ALMKPGAILINTA 127
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-87 9.96e-05

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 42.53  E-value: 9.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVKVANSRGPQ---------TIEAEVLETGAQAVTTEDAVKDVEVVIMT-----MP 66
Cdd:PRK06522   1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHldalnenglRLEDGEITVPVLAADDPAELGPQDLVILAvkayqLP 80

                         90       100
                 ....*....|....*....|.
gi 494882164  67 HpAFERIRQLIaalPEETVVI 87
Cdd:PRK06522  81 A-ALPSLAPLL---GPDTPVL 97
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-91 2.24e-04

Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 426831 [Multi-domain]  Cd Length: 147  Bit Score: 40.29  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164    3 IGILGTGNMGRVLTRKLAAAGHDVK-VANSRGPQTIEAE----VLETGAQ------AVTTEDAVKDVEVVIMTMP-HPAF 70
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTlILRGAELAAIKKNglrlTSPGGERivpppaVTSASESLGPIDLVIVTVKaYQTE 80

                          90       100
                  ....*....|....*....|.
gi 494882164   71 ERIRQLIAALPEETVVIDISN 91
Cdd:pfam02558  81 EALEDIAPLLGPNTVVLLLQN 101
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 1-105 4.31e-04

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 41.06  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164    1 MKIGILGTGNMGRVLTRKLAAAGHDV--------KVANSR---------GPQTIEAEVLETGAQAVTTE--DAVKDVEVV 61
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVtgvdidqeKVDKLNkgkspiyepGLDELLAKALKAGRLRATTDyeEAIRDADVI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 494882164   62 IMTMPHPAFER-----------IRQLIAALPEETVVIDISNYFPG--RDPVNPELDS 105
Cdd:TIGR03026  81 IICVPTPLKEDgspdlsyvesaAETIAKHLRKGATVVLESTVPPGttEEVVKPILER 137
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 6-90 4.55e-04

3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that catalyzes the NAD+-dependent oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde of the valine catabolism pathway. In Pseudomonas aeruginosa, 3-hydroxyisobutyrate dehydrogenase (mmsB) is co-induced with methylmalonate-semialdehyde dehydrogenase (mmsA) when grown on medium containing valine as the sole carbon source. The positive transcriptional regulator of this operon (mmsR) is located upstream of these genes and has been identified as a member of the XylS/AraC family of transcriptional regulators. 3-hydroxyisobutyrate dehydrogenase shares high sequence homology to the characterized 3-hydroxyisobutyrate dehydrogenase from rat liver with conservation of proposed NAD+ binding residues at the N-terminus (G-8,10,13,24 and D-31). This enzyme belongs to the 3-hydroxyacid dehydrogenase family, sharing a common evolutionary origin and enzymatic mechanism with 6-phosphogluconate. HIBADH exhibits sequence similarity to the NAD binding domain of 6-phosphogluconate dehydrogenase above trusted (pfam03446). [Energy metabolism, Amino acids and amines]


Pssm-ID: 130753 [Multi-domain]  Cd Length: 288  Bit Score: 40.55  E-value: 4.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164    6 LGTGNMGRVLTRKLAAAGHDVKVANSRgPQTIEaEVLETGAQAVTT-EDAVKDVEVVIMTMP-----HPAFERIRQLIAA 79
Cdd:TIGR01692   2 IGLGNMGGPMAANLLKAGHPVRVFDLF-PDAVE-EAVAAGAQAAASpAEAAEGADRVITMLPagqhvISVYSGDEGILPK 79

                          90
                  ....*....|.
gi 494882164   80 LPEETVVIDIS 90
Cdd:TIGR01692  80 VAKGSLLIDCS 90
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
1-65 7.25e-04

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 40.00  E-value: 7.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVKVaNSRGPqtIEAEVLETGAQAVTTEDAVKDVEVVIMTM 65
Cdd:PRK15059   1 MKLGFIGLGIMGTPMAINLARAGHQLHV-TTIGP--VADELLSLGAVSVETARQVTEASDIIFIM 62
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
2-85 7.48e-04

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 39.45  E-value: 7.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   2 KIGILG-TGNMGRVLTRKLAAAGHDVkVANSRGPQTIEAEvlETGAQAVT--------TEDAVKDVEVVIMTMPHPAFER 72
Cdd:COG2910    1 KIAVIGaTGRVGSLIVREALARGHEV-TALVRNPEKLPDE--HPGLTVVVgdvldpaaVAEALAGADAVVSALGAGGGNP 77

                         90       100
                 ....*....|....*....|
gi 494882164  73 -------IRQLIAALPEETV 85
Cdd:COG2910   78 ttvlsdgARALIDAMKAAGV 97
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-79 9.94e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 39.52  E-value: 9.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAA-AGHDVKVANSRGPQTIEAEVLETGAQAVTTEDAV---KDVEVVIMTMPHPA-FERIRQ 75
Cdd:COG0673    4 LRVGIIGAGGIGRAHAPALAAlPGVELVAVADRDPERAEAFAEEYGVRVYTDYEELladPDIDAVVIATPNHLhAELAIA 83


                 ....
gi 494882164  76 LIAA 79
Cdd:COG0673   84 ALEA 87
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-62 1.05e-03

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 39.36  E-value: 1.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVK--VANSRGPQTIEAEVLETGAQAVTT-EDAVKDVEVVI 62
Cdd:PRK11880   3 KKIGFIGGGNMASAIIGGLLASGVPAKdiIVSDPSPEKRAALAEEYGVRAATDnQEAAQEADVVV 67
SDR_a3 cd05229
atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a ...
 1-64 1.13e-03

atypical (a) SDRs, subgroup 3; These atypical SDR family members of unknown function have a glycine-rich NAD(P)-binding motif consensus that is very similar to the extended SDRs, GXXGXXG. Generally, this group has poor conservation of the active site tetrad, However, individual sequences do contain matches to the YXXXK active site motif, and generally Tyr or Asn in place of the upstream Ser found in most SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187540 [Multi-domain]  Cd Length: 302  Bit Score: 39.62  E-value: 1.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVKVANSRGPQTIEAEVLETGA----QAVTTEDAVKDVEVVIMT 64
Cdd:cd05229    1 TAHVLGASGPIGREVARELRRRGWDVRLVSRSGSKLAWLPGVEIVAadamDASSVIAAARGADVIYHC 68
GDH_like_2 cd12164
Putative glycerate dehydrogenase and related proteins of the D-specific 2-hydroxy ...
 1-87 1.23e-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: 39.40  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVKvANSRGPQTIEAEVLETGAQAVttEDAVKDVEVVIMTMP-HPAFERI--RQLI 77
Cdd:cd12164  133 RRVGVLGLGELGAAVARRLAALGFPVS-GWSRSPKDIEGVTCFHGEEGL--DAFLAQTDILVCLLPlTPETRGIlnAELL 209

                         90
                 ....*....|
gi 494882164  78 AALPEETVVI 87
Cdd:cd12164  210 ARLPRGAALI 219
PLN02256 PLN02256
arogenate dehydrogenase
 1-36 2.18e-03

arogenate dehydrogenase


Pssm-ID: 215144 [Multi-domain]  Cd Length: 304  Bit Score: 38.49  E-value: 2.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVkVANSRGPQT 36
Cdd:PLN02256  37 LKIGIVGFGNFGQFLAKTFVKQGHTV-LATSRSDYS 71
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
2-94 2.58e-03

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 38.30  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   2 KIGILGTGNMGRVLTRKLAAAGHDVKVANSrGPQTIEAEVLETGAQAVTTEDAVKDVEVVIMTMPHPafERIRQLI---- 77
Cdd:PRK15461   3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDV-NPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNG--DLVRSVLfgen 79

                         90       100
                 ....*....|....*....|
gi 494882164  78 ---AALPEETVVIDISNYFP 94
Cdd:PRK15461  80 gvcEGLSRDALVIDMSTIHP 99
PRK12557 PRK12557
H(2)-dependent methylenetetrahydromethanopterin dehydrogenase-related protein; Provisional
 1-86 2.77e-03

H(2)-dependent methylenetetrahydromethanopterin dehydrogenase-related protein; Provisional


Pssm-ID: 237136  Cd Length: 342  Bit Score: 38.53  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNM--------------------GRVLTRKLAAAGHDVKVAN-SRGPQTIEA-EVLETGAQAVTTED--AVK 56
Cdd:PRK12557   1 MKVSVYGAGNQklyleqlnlpekfggeppygGSRMAIEFAEAGHDVVLAEpNRSILSEELwKKVEDAGVKVVSDDaeAAK 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 494882164  57 DVEVVIMTMP--HPAFERIRQLIAALPEETVV 86
Cdd:PRK12557  81 HGEIHILFTPfgKKTVEIAKNILPHLPENAVI 112
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
 1-33 2.98e-03

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 38.04  E-value: 2.98e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 494882164   1 MKIGILG-TGNMGRVLTRKLAAAGHDVKVANsRG 33
Cdd:cd05265    1 MKILIIGgTRFIGKALVEELLAAGHDVTVFN-RG 33
YfcH COG1090
NAD dependent epimerase/dehydratase family enzyme [General function prediction only];
7-62 7.90e-03

NAD dependent epimerase/dehydratase family enzyme [General function prediction only];


Pssm-ID: 440707 [Multi-domain]  Cd Length: 298  Bit Score: 36.97  E-value: 7.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 494882164   7 GTGNMGRVLTRKLAAAGHDVKVAnSRGPQTIEAEVLE---TGAQAVTTEDAVKDVEVVI 62
Cdd:COG1090    7 GTGFIGSALVAALLARGHEVVVL-TRRPPKAPDEVTYvawDPETGGIDAAALEGADAVI 64
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
1-87 8.06e-03

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 36.97  E-value: 8.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVkVANSRGPQTIEA-------------EVLETGAQAVTT-EDAVKDVEVVIMTMP 66
Cdd:PRK00094   2 MKIAVLGAGSWGTALAIVLARNGHDV-TLWARDPEQAAEinadrenprylpgIKLPDNLRATTDlAEALADADLILVAVP 80

                         90       100
                 ....*....|....*....|..
gi 494882164  67 HPAF-ERIRQLIAALPEETVVI 87
Cdd:PRK00094  81 SQALrEVLKQLKPLLPPDAPIV 102
SDR_a4 cd05266
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ...
 3-82 8.38e-03

atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187576 [Multi-domain]  Cd Length: 251  Bit Score: 36.53  E-value: 8.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   3 IGILGTGNMGRVLTRKLAAAGHDVkVANSRGPQTIEAEVLEtGAQAVTTE----DAVKDVEVVIMTMPHPAF-------E 71
Cdd:cd05266    1 VLILGCGYLGQRLARQLLAQGWQV-TGTTRSPEKLAADRPA-GVTPLAADltqpGLLADVDHLVISLPPPAGsyrggydP 78

                         90
                 ....*....|.
gi 494882164  72 RIRQLIAALPE 82
Cdd:cd05266   79 GLRALLDALAQ 89
PRK14619 PRK14619
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
 1-87 8.70e-03

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237771 [Multi-domain]  Cd Length: 308  Bit Score: 36.89  E-value: 8.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494882164   1 MKIGILGTGNMGRVLTRKLAAAGHDVKVANSRGPQTIEAevletgaqavttedAVKDVEVVIMTMPHPAFERIRQLIAAL 80
Cdd:PRK14619   5 KTIAILGAGAWGSTLAGLASANGHRVRVWSRRSGLSLAA--------------VLADADVIVSAVSMKGVRPVAEQVQAL 70


                 ....*....
gi 494882164  81 --PEETVVI 87
Cdd:PRK14619  71 nlPPETIIV 79
 
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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