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Conserved domains on  [gi|490366870|ref|WP_004246534|]
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MULTISPECIES: formate dehydrogenase accessory sulfurtransferase FdhD [Proteus]

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;
15-273 4.67e-147

formate dehydrogenase accessory sulfurtransferase FdhD;


:

Pssm-ID: 234823  Cd Length: 263  Bit Score: 412.27  E-value: 4.67e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  15 IVGIDQTTVQHKGSLNQAEQDYIALEVPVALVYNGISHVVMMASPKNLELFAVGFSLSEGIIGSSNEIRSIEIVESChGG 94
Cdd:PRK00724   4 PVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESC-NG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  95 TEVQIELSSRRFMQLKERRRSMAGRTGCGICGTEQLAEIFRPIAPLPFTQTFSLSLLDNALEQLKTVQEIGELTGCTHAA 174
Cdd:PRK00724  83 VEVQLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870 175 AWLSPEGQLQGGCEDVGRHVALDKLIG--LKTQQKWTEGAILVSSRASYEMVQKSAMCGAEILFAVSAATSLAVEVANQY 252
Cdd:PRK00724 163 ALLCPDGELLAVREDVGRHNALDKLIGaaLRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEEL 242
                        250       260
                 ....*....|....*....|.
gi 490366870 253 NLTLVGFCRRGRATVFTHPQR 273
Cdd:PRK00724 243 GLTLVGFARGGRFNIYTHPQR 263
 
Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
15-273 4.67e-147

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 412.27  E-value: 4.67e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  15 IVGIDQTTVQHKGSLNQAEQDYIALEVPVALVYNGISHVVMMASPKNLELFAVGFSLSEGIIGSSNEIRSIEIVESChGG 94
Cdd:PRK00724   4 PVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESC-NG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  95 TEVQIELSSRRFMQLKERRRSMAGRTGCGICGTEQLAEIFRPIAPLPFTQTFSLSLLDNALEQLKTVQEIGELTGCTHAA 174
Cdd:PRK00724  83 VEVQLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870 175 AWLSPEGQLQGGCEDVGRHVALDKLIG--LKTQQKWTEGAILVSSRASYEMVQKSAMCGAEILFAVSAATSLAVEVANQY 252
Cdd:PRK00724 163 ALLCPDGELLAVREDVGRHNALDKLIGaaLRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEEL 242
                        250       260
                 ....*....|....*....|.
gi 490366870 253 NLTLVGFCRRGRATVFTHPQR 273
Cdd:PRK00724 243 GLTLVGFARGGRFNIYTHPQR 263
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
21-274 3.74e-127

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 361.78  E-value: 3.74e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  21 TTVQHKGSLNQAEQDYIALEVPVALVYNGISHVVMMASPKNLELFAVGFSLSEGIIGSSNEIRSIEIVESCHGGtEVQIE 100
Cdd:COG1526    6 PVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGI-VVRVE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870 101 LSSRRFMQLKERRRSMAGRTGCGICGTEQLAEIFRPIAPLPFTQTFSLSLLDNALEQLKTVQEIGELTGCTHAAAWLSPE 180
Cdd:COG1526   85 LAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAALFDPD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870 181 GQLQGGCEDVGRHVALDKLIG--LKTQQKWTEGAILVSSRASYEMVQKSAMCGAEILFAVSAATSLAVEVANQYNLTLVG 258
Cdd:COG1526  165 GELLLVREDVGRHNALDKLIGaaLLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGLTLIG 244
                        250
                 ....*....|....*.
gi 490366870 259 FCRRGRATVFTHPQRL 274
Cdd:COG1526  245 FARGDRFNVYTHPERI 260
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
35-274 3.87e-99

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: 290.14  E-value: 3.87e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870   35 DYIALEVPVALVYNGISHVVMMASPKNLELFAVGFSLSEGIIGSSNEIRSIEIVESChgGTEVQIELSSRRFMQLKERRr 114
Cdd:TIGR00129   3 DEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNI--NIEVQIDLSSRRFMILKENR- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  115 smagrTGCGICGTEQLAEIFRPIAPLPFTQTFSLSLLDNALEQLKTVQEIGELTGCTHAAAWLSPEGQLqGGCEDVGRHV 194
Cdd:TIGR00129  80 -----TGCSGCGRERLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLGGLV-SRMEDVGRHN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  195 ALDKLIG--LKTQQKWTEGAILVSSRASYEMVQKSAMCGAEILFAVSAATSLAVEVANQYNLTLVGFCRRGRATVFTHPQ 272
Cdd:TIGR00129 154 AVDKLIGsaLLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIYTHPE 233

                  ..
gi 490366870  273 RL 274
Cdd:TIGR00129 234 RL 235
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
38-274 2.09e-91

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: 270.19  E-value: 2.09e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870   38 ALEVPVALVYNGISHVVMMASPKNLELFAVGFSLSEGIIGSSNEIRSIEIVESCHggtevQIELSSRRFMQLKERRRSM- 116
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGG-----SVEVATRRGLLKLERRFLKr 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  117 AGRTGCGIcGTE---QLAEIFRPIAPLPFTQTFSLSLLDNALEQLKTVQEIGELTGCTHAAAWLSPEGQLQGGCEDVGRH 193
Cdd:pfam02634  76 TGTSGCGL-GVEfleDALDALRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  194 VALDKLIGLKTQQKW--TEGAILVSSRASYEMVQKSAMCGAEILFAVSAATSLAVEVANQYNLTLVGFCRRGRATVFTHP 271
Cdd:pfam02634 155 NALDKLIGAALLNGIdlSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVYTHP 234

                  ...
gi 490366870  272 QRL 274
Cdd:pfam02634 235 ERI 237
 
Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
15-273 4.67e-147

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 412.27  E-value: 4.67e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  15 IVGIDQTTVQHKGSLNQAEQDYIALEVPVALVYNGISHVVMMASPKNLELFAVGFSLSEGIIGSSNEIRSIEIVESChGG 94
Cdd:PRK00724   4 PVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESC-NG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  95 TEVQIELSSRRFMQLKERRRSMAGRTGCGICGTEQLAEIFRPIAPLPFTQTFSLSLLDNALEQLKTVQEIGELTGCTHAA 174
Cdd:PRK00724  83 VEVQLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870 175 AWLSPEGQLQGGCEDVGRHVALDKLIG--LKTQQKWTEGAILVSSRASYEMVQKSAMCGAEILFAVSAATSLAVEVANQY 252
Cdd:PRK00724 163 ALLCPDGELLAVREDVGRHNALDKLIGaaLRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEEL 242
                        250       260
                 ....*....|....*....|.
gi 490366870 253 NLTLVGFCRRGRATVFTHPQR 273
Cdd:PRK00724 243 GLTLVGFARGGRFNIYTHPQR 263
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
21-274 3.74e-127

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 361.78  E-value: 3.74e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  21 TTVQHKGSLNQAEQDYIALEVPVALVYNGISHVVMMASPKNLELFAVGFSLSEGIIGSSNEIRSIEIVESCHGGtEVQIE 100
Cdd:COG1526    6 PVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGI-VVRVE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870 101 LSSRRFMQLKERRRSMAGRTGCGICGTEQLAEIFRPIAPLPFTQTFSLSLLDNALEQLKTVQEIGELTGCTHAAAWLSPE 180
Cdd:COG1526   85 LAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAALFDPD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870 181 GQLQGGCEDVGRHVALDKLIG--LKTQQKWTEGAILVSSRASYEMVQKSAMCGAEILFAVSAATSLAVEVANQYNLTLVG 258
Cdd:COG1526  165 GELLLVREDVGRHNALDKLIGaaLLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGLTLIG 244
                        250
                 ....*....|....*.
gi 490366870 259 FCRRGRATVFTHPQRL 274
Cdd:COG1526  245 FARGDRFNVYTHPERI 260
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
35-274 3.87e-99

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: 290.14  E-value: 3.87e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870   35 DYIALEVPVALVYNGISHVVMMASPKNLELFAVGFSLSEGIIGSSNEIRSIEIVESChgGTEVQIELSSRRFMQLKERRr 114
Cdd:TIGR00129   3 DEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNI--NIEVQIDLSSRRFMILKENR- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  115 smagrTGCGICGTEQLAEIFRPIAPLPFTQTFSLSLLDNALEQLKTVQEIGELTGCTHAAAWLSPEGQLqGGCEDVGRHV 194
Cdd:TIGR00129  80 -----TGCSGCGRERLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLGGLV-SRMEDVGRHN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  195 ALDKLIG--LKTQQKWTEGAILVSSRASYEMVQKSAMCGAEILFAVSAATSLAVEVANQYNLTLVGFCRRGRATVFTHPQ 272
Cdd:TIGR00129 154 AVDKLIGsaLLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIYTHPE 233

                  ..
gi 490366870  273 RL 274
Cdd:TIGR00129 234 RL 235
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
38-274 2.09e-91

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: 270.19  E-value: 2.09e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870   38 ALEVPVALVYNGISHVVMMASPKNLELFAVGFSLSEGIIGSSNEIRSIEIVESCHggtevQIELSSRRFMQLKERRRSM- 116
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGG-----SVEVATRRGLLKLERRFLKr 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  117 AGRTGCGIcGTE---QLAEIFRPIAPLPFTQTFSLSLLDNALEQLKTVQEIGELTGCTHAAAWLSPEGQLQGGCEDVGRH 193
Cdd:pfam02634  76 TGTSGCGL-GVEfleDALDALRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366870  194 VALDKLIGLKTQQKW--TEGAILVSSRASYEMVQKSAMCGAEILFAVSAATSLAVEVANQYNLTLVGFCRRGRATVFTHP 271
Cdd:pfam02634 155 NALDKLIGAALLNGIdlSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVYTHP 234

                  ...
gi 490366870  272 QRL 274
Cdd:pfam02634 235 ERI 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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