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Conserved domains on  [gi|1218758985|gb|OXI14747|]
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sulfurtransferase FdhD [Burkholderia sp. AU16482]

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 ...
12-268 1.63e-104

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


:

Pssm-ID: 441135  Cd Length: 260  Bit Score: 304.77  E-value: 1.63e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  12 GSTACRVTRHRAGDARDTVDRVVDETPVALVFNGISHTVMMATPIDLDAFGLGFALSEGIVERASDVFDIESECRPGGAE 91
Cdd:COG1526     1 ATKRVPVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  92 VRLTVSQQAFMALKAHRRALAGRTGCGVCGIESIAQLDLQPPRIAAAGAAAGIGADAIARAARALparQTLMRETGGIHA 171
Cdd:COG1526    81 VRVELAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREA---QPLFRRTGGVHA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985 172 AAWCDRDGAVLDVFEDVGRHNALDKLIGQLARRRADWSAGFVFLSSRASYELVRKAARVGIPMVATISAPTSLAIDVARE 251
Cdd:COG1526   158 AALFDPDGELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEE 237
                         250
                  ....*....|....*..
gi 1218758985 252 AGVRLLGFCRNDGFVEY 268
Cdd:COG1526   238 AGLTLIGFARGDRFNVY 254
 
Name Accession Description Interval E-value
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
12-268 1.63e-104

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 304.77  E-value: 1.63e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  12 GSTACRVTRHRAGDARDTVDRVVDETPVALVFNGISHTVMMATPIDLDAFGLGFALSEGIVERASDVFDIESECRPGGAE 91
Cdd:COG1526     1 ATKRVPVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  92 VRLTVSQQAFMALKAHRRALAGRTGCGVCGIESIAQLDLQPPRIAAAGAAAGIGADAIARAARALparQTLMRETGGIHA 171
Cdd:COG1526    81 VRVELAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREA---QPLFRRTGGVHA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985 172 AAWCDRDGAVLDVFEDVGRHNALDKLIGQLARRRADWSAGFVFLSSRASYELVRKAARVGIPMVATISAPTSLAIDVARE 251
Cdd:COG1526   158 AALFDPDGELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEE 237
                         250
                  ....*....|....*..
gi 1218758985 252 AGVRLLGFCRNDGFVEY 268
Cdd:COG1526   238 AGLTLIGFARGDRFNVY 254
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
17-268 1.20e-96

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 285.15  E-value: 1.20e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  17 RVTRHRAGDARDTVDRVVDETPVALVFNGISHTVMMATPIDLDAFGLGFALSEGIVERASDVFDIESECRPGGAEVRLTV 96
Cdd:PRK00724   10 TIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCNGVEVQLEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  97 SQQAFMALKAHRRALAGRTGCGVCGIESIAQLDLQPPRIAAAGAAAGIGADAIARAARALparQTLMRETGGIHAAAWCD 176
Cdd:PRK00724   90 SSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDA---QPLFQLTGGVHAAALLC 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985 177 RDGAVLDVFEDVGRHNALDKLIGQLARRRADWSAGFVFLSSRASYELVRKAARVGIPMVATISAPTSLAIDVAREAGVRL 256
Cdd:PRK00724  167 PDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEELGLTL 246
                         250
                  ....*....|..
gi 1218758985 257 LGFCRNDGFVEY 268
Cdd:PRK00724  247 VGFARGGRFNIY 258
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
34-268 2.17e-74

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: 227.43  E-value: 2.17e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  34 VDETPVALVFNGISHTVMMATPIDLDAFGLGFALSEGIVERASDVFDIESECRPGGAEVRLTVSqqafmALKAHRRAL-- 111
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGGSVEVATRRG-----LLKLERRFLkr 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985 112 AGRTGCGVcGIESIAQLDLQPPRIAAAGAAAGIGADAIARAARALPARQTLMRETGGIHAAAWCDRDGAVLDVFEDVGRH 191
Cdd:pfam02634  76 TGTSGCGL-GVEFLEDALDALRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRH 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1218758985 192 NALDKLIGQLARRRADWSAGFVFLSSRASYELVRKAARVGIPMVATISAPTSLAIDVAREAGVRLLGFCRNDGFVEY 268
Cdd:pfam02634 155 NALDKLIGAALLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVY 231
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
31-271 1.54e-64

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: 202.31  E-value: 1.54e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  31 DRVVDETPVALVFNGISHTVMMATPIDLDAFGLGFALSEGIVERASDV--FDIESECrpgGAEVRLTVSQQAFMALKAHR 108
Cdd:TIGR00129   3 DEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIegIEIDDNI---NIEVQIDLSSRRFMILKENR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985 109 ralagrTGCGVCGIEsiaQLDLQPPRIAAAGAAAGIGADAIARAARALPARQTLMRETGGIHAAAWCDRDGAVLdVFEDV 188
Cdd:TIGR00129  80 ------TGCSGCGRE---RLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLGGLVS-RMEDV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985 189 GRHNALDKLIGQLARRRADWSAGFVFLSSRASYELVRKAARVGIPMVATISAPTSLAIDVAREAGVRLLGFCRNDGFVEY 268
Cdd:TIGR00129 150 GRHNAVDKLIGSALLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIY 229

                  ...
gi 1218758985 269 VSP 271
Cdd:TIGR00129 230 THP 232
 
Name Accession Description Interval E-value
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
12-268 1.63e-104

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 304.77  E-value: 1.63e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  12 GSTACRVTRHRAGDARDTVDRVVDETPVALVFNGISHTVMMATPIDLDAFGLGFALSEGIVERASDVFDIESECRPGGAE 91
Cdd:COG1526     1 ATKRVPVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  92 VRLTVSQQAFMALKAHRRALAGRTGCGVCGIESIAQLDLQPPRIAAAGAAAGIGADAIARAARALparQTLMRETGGIHA 171
Cdd:COG1526    81 VRVELAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREA---QPLFRRTGGVHA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985 172 AAWCDRDGAVLDVFEDVGRHNALDKLIGQLARRRADWSAGFVFLSSRASYELVRKAARVGIPMVATISAPTSLAIDVARE 251
Cdd:COG1526   158 AALFDPDGELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEE 237
                         250
                  ....*....|....*..
gi 1218758985 252 AGVRLLGFCRNDGFVEY 268
Cdd:COG1526   238 AGLTLIGFARGDRFNVY 254
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
17-268 1.20e-96

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 285.15  E-value: 1.20e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  17 RVTRHRAGDARDTVDRVVDETPVALVFNGISHTVMMATPIDLDAFGLGFALSEGIVERASDVFDIESECRPGGAEVRLTV 96
Cdd:PRK00724   10 TIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCNGVEVQLEL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  97 SQQAFMALKAHRRALAGRTGCGVCGIESIAQLDLQPPRIAAAGAAAGIGADAIARAARALparQTLMRETGGIHAAAWCD 176
Cdd:PRK00724   90 SSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDA---QPLFQLTGGVHAAALLC 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985 177 RDGAVLDVFEDVGRHNALDKLIGQLARRRADWSAGFVFLSSRASYELVRKAARVGIPMVATISAPTSLAIDVAREAGVRL 256
Cdd:PRK00724  167 PDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEELGLTL 246
                         250
                  ....*....|..
gi 1218758985 257 LGFCRNDGFVEY 268
Cdd:PRK00724  247 VGFARGGRFNIY 258
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
34-268 2.17e-74

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: 227.43  E-value: 2.17e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  34 VDETPVALVFNGISHTVMMATPIDLDAFGLGFALSEGIVERASDVFDIESECRPGGAEVRLTVSqqafmALKAHRRAL-- 111
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGGSVEVATRRG-----LLKLERRFLkr 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985 112 AGRTGCGVcGIESIAQLDLQPPRIAAAGAAAGIGADAIARAARALPARQTLMRETGGIHAAAWCDRDGAVLDVFEDVGRH 191
Cdd:pfam02634  76 TGTSGCGL-GVEFLEDALDALRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRH 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1218758985 192 NALDKLIGQLARRRADWSAGFVFLSSRASYELVRKAARVGIPMVATISAPTSLAIDVAREAGVRLLGFCRNDGFVEY 268
Cdd:pfam02634 155 NALDKLIGAALLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVY 231
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
31-271 1.54e-64

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: 202.31  E-value: 1.54e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985  31 DRVVDETPVALVFNGISHTVMMATPIDLDAFGLGFALSEGIVERASDV--FDIESECrpgGAEVRLTVSQQAFMALKAHR 108
Cdd:TIGR00129   3 DEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIegIEIDDNI---NIEVQIDLSSRRFMILKENR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985 109 ralagrTGCGVCGIEsiaQLDLQPPRIAAAGAAAGIGADAIARAARALPARQTLMRETGGIHAAAWCDRDGAVLdVFEDV 188
Cdd:TIGR00129  80 ------TGCSGCGRE---RLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLGGLVS-RMEDV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1218758985 189 GRHNALDKLIGQLARRRADWSAGFVFLSSRASYELVRKAARVGIPMVATISAPTSLAIDVAREAGVRLLGFCRNDGFVEY 268
Cdd:TIGR00129 150 GRHNAVDKLIGSALLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIY 229

                  ...
gi 1218758985 269 VSP 271
Cdd:TIGR00129 230 THP 232
 
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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