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Conserved domains on  [gi|976214092|gb|KVB23011|]
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formate dehydrogenase accessory protein FdhD [Burkholderia cepacia]

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 ...
15-275 2.63e-109

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


:

Pssm-ID: 441135  Cd Length: 260  Bit Score: 316.71  E-value: 2.63e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092  15 GAIELSVRRTRGGAVETAHDYVGQEWPVALVFNGISHAVMMCTPCDLEAFAVGFAISEGIVARGSDIKDIEVILHADApl 94
Cdd:COG1526    1 ATKRVPVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGG-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092  95 phAEVHLEVVQQAFAALKDRRRALAGRTGCGVCGIESIDLLDLAPERVPDTgflARLAPDALTRAAQALPAHQALTRLTG 174
Cdd:COG1526   79 --IVVRVELAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSD---LRLSAEALLALLDALREAQPLFRRTG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092 175 GLHAAAWCDATGAIRMAFEDVGRHNALDKLIGSLVLSRADPTDGFVFLSSRASYELVRKAARVGIPMVATISAPSSLAIE 254
Cdd:COG1526  154 GVHAAALFDPDGELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVE 233
                        250       260
                 ....*....|....*....|.
gi 976214092 255 IAKAAGLRLVSFCRETGHVDY 275
Cdd:COG1526  234 LAEEAGLTLIGFARGDRFNVY 254
 
Name Accession Description Interval E-value
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
15-275 2.63e-109

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 316.71  E-value: 2.63e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092  15 GAIELSVRRTRGGAVETAHDYVGQEWPVALVFNGISHAVMMCTPCDLEAFAVGFAISEGIVARGSDIKDIEVILHADApl 94
Cdd:COG1526    1 ATKRVPVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGG-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092  95 phAEVHLEVVQQAFAALKDRRRALAGRTGCGVCGIESIDLLDLAPERVPDTgflARLAPDALTRAAQALPAHQALTRLTG 174
Cdd:COG1526   79 --IVVRVELAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSD---LRLSAEALLALLDALREAQPLFRRTG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092 175 GLHAAAWCDATGAIRMAFEDVGRHNALDKLIGSLVLSRADPTDGFVFLSSRASYELVRKAARVGIPMVATISAPSSLAIE 254
Cdd:COG1526  154 GVHAAALFDPDGELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVE 233
                        250       260
                 ....*....|....*....|.
gi 976214092 255 IAKAAGLRLVSFCRETGHVDY 275
Cdd:COG1526  234 LAEEAGLTLIGFARGDRFNVY 254
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
21-269 5.52e-99

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 290.54  E-value: 5.52e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092  21 VRRTRGGAVETAHDYVGQEWPVALVFNGISHAVMMCTPCDLEAFAVGFAISEGIVARGSDIKDIEVILHADaplpHAEVH 100
Cdd:PRK00724  11 IVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCN----GVEVQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092 101 LEVVQQAFAALKDRRRALAGRTGCGVCGIESIDLLDLAPERVPDTgflARLAPDALTRAAQALPAHQALTRLTGGLHAAA 180
Cdd:PRK00724  87 LELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFT---QTFTAEDLDRAMAQLQDAQPLFQLTGGVHAAA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092 181 WCDATGAIRMAFEDVGRHNALDKLIGSLVLSRADPTDGFVFLSSRASYELVRKAARVGIPMVATISAPSSLAIEIAKAAG 260
Cdd:PRK00724 164 LLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEELG 243

                 ....*....
gi 976214092 261 LRLVSFCRE 269
Cdd:PRK00724 244 LTLVGFARG 252
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
39-275 2.38e-80

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: 242.45  E-value: 2.38e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092   39 EWPVALVFNGISHAVMMCTPCDLEAFAVGFAISEGIVARGSDIKDIEVilhaDAPLPHAEVHLEVVQqafAALKDRRRAL 118
Cdd:pfam02634   3 EVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEV----DEDGGSVEVATRRGL---LKLERRFLKR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092  119 AGRTGCGVcGIESIDLLDLAPERVPDTGFLARLAPDALTRAAQALPAHQALTRLTGGLHAAAWCDATGAIRMAFEDVGRH 198
Cdd:pfam02634  76 TGTSGCGL-GVEFLEDALDALRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRH 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976214092  199 NALDKLIGSLVLSRADPTDGFVFLSSRASYELVRKAARVGIPMVATISAPSSLAIEIAKAAGLRLVSFCRETGHVDY 275
Cdd:pfam02634 155 NALDKLIGAALLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVY 231
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
34-269 1.07e-63

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: 200.00  E-value: 1.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092   34 DYVGQEWPVALVFNGISHAVMMCTPCDLEAFAVGFAISEGIVARGSDIKDIEVIlhadaPLPHAEVHLEVVQQAFAALKD 113
Cdd:TIGR00129   3 DEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEID-----DNINIEVQIDLSSRRFMILKE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092  114 RRralagrTGCGVCGIESidlLDLAPERVPDTGFLARLAPDALTRAAQALPAHQALTRLTGGLHAAAWCDATGAIRMaFE 193
Cdd:TIGR00129  78 NR------TGCSGCGRER---LNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLGGLVSR-ME 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 976214092  194 DVGRHNALDKLIGSLVLSRADPTDGFVFLSSRASYELVRKAARVGIPMVATISAPSSLAIEIAKAAGLRLVSFCRE 269
Cdd:TIGR00129 148 DVGRHNAVDKLIGSALLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARN 223
 
Name Accession Description Interval E-value
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
15-275 2.63e-109

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 316.71  E-value: 2.63e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092  15 GAIELSVRRTRGGAVETAHDYVGQEWPVALVFNGISHAVMMCTPCDLEAFAVGFAISEGIVARGSDIKDIEVILHADApl 94
Cdd:COG1526    1 ATKRVPVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGG-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092  95 phAEVHLEVVQQAFAALKDRRRALAGRTGCGVCGIESIDLLDLAPERVPDTgflARLAPDALTRAAQALPAHQALTRLTG 174
Cdd:COG1526   79 --IVVRVELAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSD---LRLSAEALLALLDALREAQPLFRRTG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092 175 GLHAAAWCDATGAIRMAFEDVGRHNALDKLIGSLVLSRADPTDGFVFLSSRASYELVRKAARVGIPMVATISAPSSLAIE 254
Cdd:COG1526  154 GVHAAALFDPDGELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVE 233
                        250       260
                 ....*....|....*....|.
gi 976214092 255 IAKAAGLRLVSFCRETGHVDY 275
Cdd:COG1526  234 LAEEAGLTLIGFARGDRFNVY 254
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
21-269 5.52e-99

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 290.54  E-value: 5.52e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092  21 VRRTRGGAVETAHDYVGQEWPVALVFNGISHAVMMCTPCDLEAFAVGFAISEGIVARGSDIKDIEVILHADaplpHAEVH 100
Cdd:PRK00724  11 IVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCN----GVEVQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092 101 LEVVQQAFAALKDRRRALAGRTGCGVCGIESIDLLDLAPERVPDTgflARLAPDALTRAAQALPAHQALTRLTGGLHAAA 180
Cdd:PRK00724  87 LELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFT---QTFTAEDLDRAMAQLQDAQPLFQLTGGVHAAA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092 181 WCDATGAIRMAFEDVGRHNALDKLIGSLVLSRADPTDGFVFLSSRASYELVRKAARVGIPMVATISAPSSLAIEIAKAAG 260
Cdd:PRK00724 164 LLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEELG 243

                 ....*....
gi 976214092 261 LRLVSFCRE 269
Cdd:PRK00724 244 LTLVGFARG 252
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
39-275 2.38e-80

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: 242.45  E-value: 2.38e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092   39 EWPVALVFNGISHAVMMCTPCDLEAFAVGFAISEGIVARGSDIKDIEVilhaDAPLPHAEVHLEVVQqafAALKDRRRAL 118
Cdd:pfam02634   3 EVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEV----DEDGGSVEVATRRGL---LKLERRFLKR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092  119 AGRTGCGVcGIESIDLLDLAPERVPDTGFLARLAPDALTRAAQALPAHQALTRLTGGLHAAAWCDATGAIRMAFEDVGRH 198
Cdd:pfam02634  76 TGTSGCGL-GVEFLEDALDALRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRH 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 976214092  199 NALDKLIGSLVLSRADPTDGFVFLSSRASYELVRKAARVGIPMVATISAPSSLAIEIAKAAGLRLVSFCRETGHVDY 275
Cdd:pfam02634 155 NALDKLIGAALLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVY 231
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
34-269 1.07e-63

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: 200.00  E-value: 1.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092   34 DYVGQEWPVALVFNGISHAVMMCTPCDLEAFAVGFAISEGIVARGSDIKDIEVIlhadaPLPHAEVHLEVVQQAFAALKD 113
Cdd:TIGR00129   3 DEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEID-----DNINIEVQIDLSSRRFMILKE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 976214092  114 RRralagrTGCGVCGIESidlLDLAPERVPDTGFLARLAPDALTRAAQALPAHQALTRLTGGLHAAAWCDATGAIRMaFE 193
Cdd:TIGR00129  78 NR------TGCSGCGRER---LNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLGGLVSR-ME 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 976214092  194 DVGRHNALDKLIGSLVLSRADPTDGFVFLSSRASYELVRKAARVGIPMVATISAPSSLAIEIAKAAGLRLVSFCRE 269
Cdd:TIGR00129 148 DVGRHNAVDKLIGSALLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARN 223
 
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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