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Conserved domains on  [gi|1609639925|gb|TGF18965|]
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sulfurtransferase FdhD [Escherichia coli]

Protein Classification

formate dehydrogenase accessory sulfurtransferase FdhD( domain architecture ID 10011499)

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
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
12-274 1.91e-164

formate dehydrogenase accessory sulfurtransferase FdhD;


:

Pssm-ID: 234823  Cd Length: 263  Bit Score: 456.18  E-value: 1.91e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  12 VTNITGVRQIELWRRDDLQHPRLDEVAEEVPVALVYNGISHVVMMASPKDLEYFALGFSLSEGIIESPRDIFGMDVVPSC 91
Cdd:PRK00724    1 MMGPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  92 NGLEVQIELSSRRFMGLKERRRALAGRTGCGVCGVEQLNDIGKPVQPLPFTQTFDLNKLDDALRHLNDFQPVGQLTGCTH 171
Cdd:PRK00724   81 NGVEVQLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 172 AAAWMLPSGELVGGHEDVGRHVALDKLLGRRSQEGESWQQGAVLVSSRASYEMVQKSAMCGVEILFAVSAATTLAVEVAE 251
Cdd:PRK00724  161 AAALLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAE 240
                         250       260
                  ....*....|....*....|...
gi 1609639925 252 RCNLTLVGFCKPGRATVYTHPQR 274
Cdd:PRK00724  241 ELGLTLVGFARGGRFNIYTHPQR 263
 
Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
12-274 1.91e-164

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 456.18  E-value: 1.91e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  12 VTNITGVRQIELWRRDDLQHPRLDEVAEEVPVALVYNGISHVVMMASPKDLEYFALGFSLSEGIIESPRDIFGMDVVPSC 91
Cdd:PRK00724    1 MMGPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  92 NGLEVQIELSSRRFMGLKERRRALAGRTGCGVCGVEQLNDIGKPVQPLPFTQTFDLNKLDDALRHLNDFQPVGQLTGCTH 171
Cdd:PRK00724   81 NGVEVQLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 172 AAAWMLPSGELVGGHEDVGRHVALDKLLGRRSQEGESWQQGAVLVSSRASYEMVQKSAMCGVEILFAVSAATTLAVEVAE 251
Cdd:PRK00724  161 AAALLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAE 240
                         250       260
                  ....*....|....*....|...
gi 1609639925 252 RCNLTLVGFCKPGRATVYTHPQR 274
Cdd:PRK00724  241 ELGLTLVGFARGGRFNIYTHPQR 263
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
17-275 1.69e-136

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 385.28  E-value: 1.69e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  17 GVRQIELWR-RDDLQHPRLDEVAEEVPVALVYNGISHVVMMASPKDLEYFALGFSLSEGIIESPRDIFGMDVVPSCNGLE 95
Cdd:COG1526     1 ATKRVPVLRiRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  96 VQIELSSRRFMGLKERRRALAGRTGCGVCGVEQLNDIGKPVQPLPFTQTFDLNKLDDALRHLNDFQPVGQLTGCTHAAAW 175
Cdd:COG1526    81 VRVELAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 176 MLPSGELVGGHEDVGRHVALDKLLGRRSQEGESWQQGAVLVSSRASYEMVQKSAMCGVEILFAVSAATTLAVEVAERCNL 255
Cdd:COG1526   161 FDPDGELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGL 240
                         250       260
                  ....*....|....*....|
gi 1609639925 256 TLVGFCKPGRATVYTHPQRL 275
Cdd:COG1526   241 TLIGFARGDRFNVYTHPERI 260
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
33-277 1.06e-130

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: 369.88  E-value: 1.06e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  33 RLDEVAEEVPVALVYNGISHVVMMASPKDLEYFALGFSLSEGIIESPRDIFGMDVVPSCNgLEVQIELSSRRFMGLKERR 112
Cdd:TIGR00129   1 VEDEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNIN-IEVQIDLSSRRFMILKENR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 113 ralagrTGCGVCGVEQLNDIGKPVQPLPFTQTFDLNKLDDALRHLNDFQPVGQLTGCTHAAAWMLPsGELVGGHEDVGRH 192
Cdd:TIGR00129  80 ------TGCSGCGRERLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDL-GGLVSRMEDVGRH 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 193 VALDKLLGRRSQEGESWQQGAVLVSSRASYEMVQKSAMCGVEILFAVSAATTLAVEVAERCNLTLVGFCKPGRATVYTHP 272
Cdd:TIGR00129 153 NAVDKLIGSALLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIYTHP 232

                  ....*
gi 1609639925 273 QRLSN 277
Cdd:TIGR00129 233 ERLLE 237
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
38-275 2.86e-96

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: 282.52  E-value: 2.86e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  38 AEEVPVALVYNGISHVVMMASPKDLEYFALGFSLSEGIIESPRDIFGMDVVPSCNGLEVqielSSRRFMGLKERRRA-LA 116
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGGSVEV----ATRRGLLKLERRFLkRT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 117 GRTGCGVcGVEQLNDIGKPVQPLPF---TQTFDLNKLDDALRHLNDFQPVGQLTGCTHAAAWMLPSGELVGGHEDVGRHV 193
Cdd:pfam02634  77 GTSGCGL-GVEFLEDALDALRALPLpssDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRHN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 194 ALDKLLGRRSQEGESWQQGAVLVSSRASYEMVQKSAMCGVEILFAVSAATTLAVEVAERCNLTLVGFCKPGRATVYTHPQ 273
Cdd:pfam02634 156 ALDKLIGAALLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVYTHPE 235

                  ..
gi 1609639925 274 RL 275
Cdd:pfam02634 236 RI 237
 
Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
12-274 1.91e-164

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 456.18  E-value: 1.91e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  12 VTNITGVRQIELWRRDDLQHPRLDEVAEEVPVALVYNGISHVVMMASPKDLEYFALGFSLSEGIIESPRDIFGMDVVPSC 91
Cdd:PRK00724    1 MMGPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  92 NGLEVQIELSSRRFMGLKERRRALAGRTGCGVCGVEQLNDIGKPVQPLPFTQTFDLNKLDDALRHLNDFQPVGQLTGCTH 171
Cdd:PRK00724   81 NGVEVQLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 172 AAAWMLPSGELVGGHEDVGRHVALDKLLGRRSQEGESWQQGAVLVSSRASYEMVQKSAMCGVEILFAVSAATTLAVEVAE 251
Cdd:PRK00724  161 AAALLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAE 240
                         250       260
                  ....*....|....*....|...
gi 1609639925 252 RCNLTLVGFCKPGRATVYTHPQR 274
Cdd:PRK00724  241 ELGLTLVGFARGGRFNIYTHPQR 263
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
17-275 1.69e-136

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 385.28  E-value: 1.69e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  17 GVRQIELWR-RDDLQHPRLDEVAEEVPVALVYNGISHVVMMASPKDLEYFALGFSLSEGIIESPRDIFGMDVVPSCNGLE 95
Cdd:COG1526     1 ATKRVPVLRiRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  96 VQIELSSRRFMGLKERRRALAGRTGCGVCGVEQLNDIGKPVQPLPFTQTFDLNKLDDALRHLNDFQPVGQLTGCTHAAAW 175
Cdd:COG1526    81 VRVELAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAAL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 176 MLPSGELVGGHEDVGRHVALDKLLGRRSQEGESWQQGAVLVSSRASYEMVQKSAMCGVEILFAVSAATTLAVEVAERCNL 255
Cdd:COG1526   161 FDPDGELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGL 240
                         250       260
                  ....*....|....*....|
gi 1609639925 256 TLVGFCKPGRATVYTHPQRL 275
Cdd:COG1526   241 TLIGFARGDRFNVYTHPERI 260
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
33-277 1.06e-130

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: 369.88  E-value: 1.06e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  33 RLDEVAEEVPVALVYNGISHVVMMASPKDLEYFALGFSLSEGIIESPRDIFGMDVVPSCNgLEVQIELSSRRFMGLKERR 112
Cdd:TIGR00129   1 VEDEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNIN-IEVQIDLSSRRFMILKENR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 113 ralagrTGCGVCGVEQLNDIGKPVQPLPFTQTFDLNKLDDALRHLNDFQPVGQLTGCTHAAAWMLPsGELVGGHEDVGRH 192
Cdd:TIGR00129  80 ------TGCSGCGRERLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDL-GGLVSRMEDVGRH 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 193 VALDKLLGRRSQEGESWQQGAVLVSSRASYEMVQKSAMCGVEILFAVSAATTLAVEVAERCNLTLVGFCKPGRATVYTHP 272
Cdd:TIGR00129 153 NAVDKLIGSALLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIYTHP 232

                  ....*
gi 1609639925 273 QRLSN 277
Cdd:TIGR00129 233 ERLLE 237
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
38-275 2.86e-96

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: 282.52  E-value: 2.86e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925  38 AEEVPVALVYNGISHVVMMASPKDLEYFALGFSLSEGIIESPRDIFGMDVVPSCNGLEVqielSSRRFMGLKERRRA-LA 116
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGGSVEV----ATRRGLLKLERRFLkRT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 117 GRTGCGVcGVEQLNDIGKPVQPLPF---TQTFDLNKLDDALRHLNDFQPVGQLTGCTHAAAWMLPSGELVGGHEDVGRHV 193
Cdd:pfam02634  77 GTSGCGL-GVEFLEDALDALRALPLpssDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRHN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609639925 194 ALDKLLGRRSQEGESWQQGAVLVSSRASYEMVQKSAMCGVEILFAVSAATTLAVEVAERCNLTLVGFCKPGRATVYTHPQ 273
Cdd:pfam02634 156 ALDKLIGAALLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVYTHPE 235

                  ..
gi 1609639925 274 RL 275
Cdd:pfam02634 236 RI 237
 
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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