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Conserved domains on  [gi|1966635263|ref|WP_202385913|]
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formate dehydrogenase accessory sulfurtransferase FdhD [Alteraurantiacibacter aestuarii]

Protein Classification

formate dehydrogenase accessory sulfurtransferase FdhD( domain architecture ID 10003943)

formate dehydrogenase accessory sulfurtransferase FdhD is involved in the production or activity of formate dehydrogenase-H

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
9-253 2.79e-90

Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and conversion];


:

Pssm-ID: 441135  Cd Length: 260  Bit Score: 267.79  E-value: 2.79e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263   9 PVEYTRDGHCHPVARSFVPEVPVALEYNGLSYAVMMASPSDLADFALGFALTEGLAQSAADVTDLDVVEVDAGWICRAQL 88
Cdd:COG1526     6 PVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGIVVRVEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263  89 SGLGIEKLTERVRTRVAESSCGLCGIENLEAVGRPLPQVPAHKALDPQAIFAALSKLRDHQPLTKATGAAHAAAFCTPDG 168
Cdd:COG1526    86 APGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAALFDPDG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263 169 TILTAREDVGRHNAMDKLIGALATAGQSAADGFILSSARCSYEIVEKAVRAGAHTLVTISLPTSMAAERAKAAGLSLWCL 248
Cdd:COG1526   166 ELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGLTLIGF 245

                  ....*
gi 1966635263 249 ARDDS 253
Cdd:COG1526   246 ARGDR 250
 
Name Accession Description Interval E-value
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
9-253 2.79e-90

Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and conversion];


Pssm-ID: 441135  Cd Length: 260  Bit Score: 267.79  E-value: 2.79e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263   9 PVEYTRDGHCHPVARSFVPEVPVALEYNGLSYAVMMASPSDLADFALGFALTEGLAQSAADVTDLDVVEVDAGWICRAQL 88
Cdd:COG1526     6 PVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGIVVRVEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263  89 SGLGIEKLTERVRTRVAESSCGLCGIENLEAVGRPLPQVPAHKALDPQAIFAALSKLRDHQPLTKATGAAHAAAFCTPDG 168
Cdd:COG1526    86 APGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAALFDPDG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263 169 TILTAREDVGRHNAMDKLIGALATAGQSAADGFILSSARCSYEIVEKAVRAGAHTLVTISLPTSMAAERAKAAGLSLWCL 248
Cdd:COG1526   166 ELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGLTLIGF 245

                  ....*
gi 1966635263 249 ARDDS 253
Cdd:COG1526   246 ARGDR 250
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
1-253 2.09e-73

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 224.67  E-value: 2.09e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263   1 MAIPTPAEPVEYTRDGHCHPVARSFVPEVPVALEYNGLSYAVMMASPSDLADFALGFALTEGLAQSAADVTDLDVVEVDA 80
Cdd:PRK00724    2 MGPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263  81 GWICRAQLSGLGIEKLTERVRTRVAESSCGLCGIENLEAVGRPLPQVPAHKALDPQAIFAALSKLRDHQPLTKATGAAHA 160
Cdd:PRK00724   82 GVEVQLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263 161 AAFCTPDGTILTAREDVGRHNAMDKLIGALATAGQSAADGFILSSARCSYEIVEKAVRAGAHTLVTISLPTSMAAERAKA 240
Cdd:PRK00724  162 AALLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEE 241
                         250
                  ....*....|...
gi 1966635263 241 AGLSLWCLARDDS 253
Cdd:PRK00724  242 LGLTLVGFARGGR 254
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
28-253 6.40e-68

FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and FdhD are required for formate dehydrogenase activity. Structurally, they possess a deaminase fold with a characteriztic binding pocket, suggesting that they might bind a nucleotide or related molecule allosterically to regulate the formate dehydrogenase catalytic subunit.


Pssm-ID: 460633  Cd Length: 238  Bit Score: 210.10  E-value: 6.40e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263  28 EVPVALEYNGLSYAVMMASPSDLADFALGFALTEGLAQSAADVTDLDVVEVDAGWICRaqlSGLGIEKLTERVRTRVAES 107
Cdd:pfam02634   3 EVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGGSVEVA---TRRGLLKLERRFLKRTGTS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263 108 SCGLcGIENLEAVG---RPLPQVPAHKALDPQAIFAALSKLRDHQPLTKATGAAHAAAFCTPDGTILTAREDVGRHNAMD 184
Cdd:pfam02634  80 GCGL-GVEFLEDALdalRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRHNALD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1966635263 185 KLIGALATAGQSAADGFILSSARCSYEIVEKAVRAGAHTLVTISLPTSMAAERAKAAGLSLWCLARDDS 253
Cdd:pfam02634 159 KLIGAALLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGR 227
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
26-250 1.32e-47

formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis are required for the activity of formate dehydrogenase. The gene name in B. subtilis reflects the requirement of the neighboring gene narA for nitrate assimilation, for which NarQ is not required. In some species, the gene is associated not with a known formate dehydrogenase but with a related putative molybdopterin-binding oxidoreductase. A reasonable hypothesis is that this protein helps prepare a required cofactor for assembly into the holoenzyme. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]


Pssm-ID: 272923  Cd Length: 237  Bit Score: 158.02  E-value: 1.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263  26 VPEVPVALEYNGLSYAVMMASPSDLADFALGFALTEGLAQSAADVTDLDVVEVDAGWIcRAQLSGLGIEKLTERvrtrva 105
Cdd:TIGR00129   6 AVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNINIEV-QIDLSSRRFMILKEN------ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263 106 ESSCGLCGIENLEAVGRPLPQVPAHKALDPQAIFAALSKLRDHQPLTKATGAAHAAAFCTPDGTILtAREDVGRHNAMDK 185
Cdd:TIGR00129  79 RTGCSGCGRERLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLGGLVS-RMEDVGRHNAVDK 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1966635263 186 LIGALATAGQSAADGFILSSARCSYEIVEKAVRAGAHTLVTISLPTSMAAERAKAAGLSLWCLAR 250
Cdd:TIGR00129 158 LIGSALLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFAR 222
 
Name Accession Description Interval E-value
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
9-253 2.79e-90

Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and conversion];


Pssm-ID: 441135  Cd Length: 260  Bit Score: 267.79  E-value: 2.79e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263   9 PVEYTRDGHCHPVARSFVPEVPVALEYNGLSYAVMMASPSDLADFALGFALTEGLAQSAADVTDLDVVEVDAGWICRAQL 88
Cdd:COG1526     6 PVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGIVVRVEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263  89 SGLGIEKLTERVRTRVAESSCGLCGIENLEAVGRPLPQVPAHKALDPQAIFAALSKLRDHQPLTKATGAAHAAAFCTPDG 168
Cdd:COG1526    86 APGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAALFDPDG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263 169 TILTAREDVGRHNAMDKLIGALATAGQSAADGFILSSARCSYEIVEKAVRAGAHTLVTISLPTSMAAERAKAAGLSLWCL 248
Cdd:COG1526   166 ELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGLTLIGF 245

                  ....*
gi 1966635263 249 ARDDS 253
Cdd:COG1526   246 ARGDR 250
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
1-253 2.09e-73

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 224.67  E-value: 2.09e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263   1 MAIPTPAEPVEYTRDGHCHPVARSFVPEVPVALEYNGLSYAVMMASPSDLADFALGFALTEGLAQSAADVTDLDVVEVDA 80
Cdd:PRK00724    2 MGPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263  81 GWICRAQLSGLGIEKLTERVRTRVAESSCGLCGIENLEAVGRPLPQVPAHKALDPQAIFAALSKLRDHQPLTKATGAAHA 160
Cdd:PRK00724   82 GVEVQLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263 161 AAFCTPDGTILTAREDVGRHNAMDKLIGALATAGQSAADGFILSSARCSYEIVEKAVRAGAHTLVTISLPTSMAAERAKA 240
Cdd:PRK00724  162 AALLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEE 241
                         250
                  ....*....|...
gi 1966635263 241 AGLSLWCLARDDS 253
Cdd:PRK00724  242 LGLTLVGFARGGR 254
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
28-253 6.40e-68

FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and FdhD are required for formate dehydrogenase activity. Structurally, they possess a deaminase fold with a characteriztic binding pocket, suggesting that they might bind a nucleotide or related molecule allosterically to regulate the formate dehydrogenase catalytic subunit.


Pssm-ID: 460633  Cd Length: 238  Bit Score: 210.10  E-value: 6.40e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263  28 EVPVALEYNGLSYAVMMASPSDLADFALGFALTEGLAQSAADVTDLDVVEVDAGWICRaqlSGLGIEKLTERVRTRVAES 107
Cdd:pfam02634   3 EVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGGSVEVA---TRRGLLKLERRFLKRTGTS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263 108 SCGLcGIENLEAVG---RPLPQVPAHKALDPQAIFAALSKLRDHQPLTKATGAAHAAAFCTPDGTILTAREDVGRHNAMD 184
Cdd:pfam02634  80 GCGL-GVEFLEDALdalRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRHNALD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1966635263 185 KLIGALATAGQSAADGFILSSARCSYEIVEKAVRAGAHTLVTISLPTSMAAERAKAAGLSLWCLARDDS 253
Cdd:pfam02634 159 KLIGAALLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGR 227
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
26-250 1.32e-47

formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis are required for the activity of formate dehydrogenase. The gene name in B. subtilis reflects the requirement of the neighboring gene narA for nitrate assimilation, for which NarQ is not required. In some species, the gene is associated not with a known formate dehydrogenase but with a related putative molybdopterin-binding oxidoreductase. A reasonable hypothesis is that this protein helps prepare a required cofactor for assembly into the holoenzyme. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]


Pssm-ID: 272923  Cd Length: 237  Bit Score: 158.02  E-value: 1.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263  26 VPEVPVALEYNGLSYAVMMASPSDLADFALGFALTEGLAQSAADVTDLDVVEVDAGWIcRAQLSGLGIEKLTERvrtrva 105
Cdd:TIGR00129   6 AVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNINIEV-QIDLSSRRFMILKEN------ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1966635263 106 ESSCGLCGIENLEAVGRPLPQVPAHKALDPQAIFAALSKLRDHQPLTKATGAAHAAAFCTPDGTILtAREDVGRHNAMDK 185
Cdd:TIGR00129  79 RTGCSGCGRERLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLGGLVS-RMEDVGRHNAVDK 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1966635263 186 LIGALATAGQSAADGFILSSARCSYEIVEKAVRAGAHTLVTISLPTSMAAERAKAAGLSLWCLAR 250
Cdd:TIGR00129 158 LIGSALLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFAR 222
 
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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