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Conserved domains on  [gi|446451375|ref|WP_000529230|]
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MULTISPECIES: formate dehydrogenase accessory sulfurtransferase FdhD [Bacillus]

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;
1-260 1.55e-134

formate dehydrogenase accessory sulfurtransferase FdhD;


:

Pssm-ID: 234823  Cd Length: 263  Bit Score: 380.29  E-value: 1.55e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375   1 MGPTQETYTIVRYQSGTFSKQLDEIVTESPITIKLNGEEYVTVVCTPNYIEDMVIGFLISEGIISSYKDVEELWVQKDNG 80
Cdd:PRK00724   2 MGPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375  81 IVHVKSSKVNPLYQTL-YNKRYITSCCGKGRQGFIFVNDAAKAKDLHDIHVKITPEECFHLMNTLQQSSTTFRQTGGVHN 159
Cdd:PRK00724  82 GVEVQLELSSRRFAGLkARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375 160 TA-LCDRNNILLSRMDIGRHNALDKIYGHCLRNDISIKGKIIAFSGRISSEILLKVSKIGCEIVLSKSAPTKLALQLAHD 238
Cdd:PRK00724 162 AAlLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEE 241
                        250       260
                 ....*....|....*....|..
gi 446451375 239 LGITVVGFIRNESCNIYTHPKR 260
Cdd:PRK00724 242 LGLTLVGFARGGRFNIYTHPQR 263
 
Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
1-260 1.55e-134

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 380.29  E-value: 1.55e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375   1 MGPTQETYTIVRYQSGTFSKQLDEIVTESPITIKLNGEEYVTVVCTPNYIEDMVIGFLISEGIISSYKDVEELWVQKDNG 80
Cdd:PRK00724   2 MGPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375  81 IVHVKSSKVNPLYQTL-YNKRYITSCCGKGRQGFIFVNDAAKAKDLHDIHVKITPEECFHLMNTLQQSSTTFRQTGGVHN 159
Cdd:PRK00724  82 GVEVQLELSSRRFAGLkARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375 160 TA-LCDRNNILLSRMDIGRHNALDKIYGHCLRNDISIKGKIIAFSGRISSEILLKVSKIGCEIVLSKSAPTKLALQLAHD 238
Cdd:PRK00724 162 AAlLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEE 241
                        250       260
                 ....*....|....*....|..
gi 446451375 239 LGITVVGFIRNESCNIYTHPKR 260
Cdd:PRK00724 242 LGLTLVGFARGGRFNIYTHPQR 263
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
26-262 3.24e-114

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: 327.97  E-value: 3.24e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375   26 VTESPITIKLNGEEYVTVVCTPNYIEDMVIGFLISEGIISSYKDVEELWVQKDNGIVHVKSSKVNPLYQTLYNKRYITSC 105
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGGSVEVATRRGLLKLERRFLKRTGTSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375  106 CGKGRQGFIFVNDAAKAKDLHDIHVKITPEECFHLMNTLQQSSTTFRQTGGVHNTALCD-RNNILLSRMDIGRHNALDKI 184
Cdd:pfam02634  81 CGLGVEFLEDALDALRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDaEGGLLLFREDIGRHNALDKL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446451375  185 YGHCLRNDISIKGKIIAFSGRISSEILLKVSKIGCEIVLSKSAPTKLALQLAHDLGITVVGFIRNESCNIYTHPKRID 262
Cdd:pfam02634 161 IGAALLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVYTHPERII 238
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
6-261 1.02e-103

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 302.07  E-value: 1.02e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375   6 ETYTIVRYQSGTFSKQLDEIVTESPITIKLNGEEYVTVVCTPNYIEDMVIGFLISEGIISSYKDVEELWV--QKDNGIVH 83
Cdd:COG1526    3 KRVPVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVdeDEGGIVVR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375  84 VK-SSKVNPLYQTLYNKRYITSCCGK-GRQgfifVNDAA--KAKDLHDiHVKITPEECFHLMNTLQQSSTTFRQTGGVHN 159
Cdd:COG1526   83 VElAPGAFADLKERRRRLTGTSGCGLcGTE----SLDALlrPLPPLPS-DLRLSAEALLALLDALREAQPLFRRTGGVHA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375 160 TALCDRN-NILLSRMDIGRHNALDKIYGHCLRNDISIKGKIIAFSGRISSEILLKVSKIGCEIVLSKSAPTKLALQLAHD 238
Cdd:COG1526  158 AALFDPDgELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEE 237
                        250       260
                 ....*....|....*....|...
gi 446451375 239 LGITVVGFIRNESCNIYTHPKRI 261
Cdd:COG1526  238 AGLTLIGFARGDRFNVYTHPERI 260
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
22-261 7.29e-74

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: 225.43  E-value: 7.29e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375   22 LDEIVTESPITIKLNGEEYVTVVCTPNYIEDMVIGFLISEGIISSYKDVEELWVQKDNGIvHVKSSKVNPLYQTLYNKRY 101
Cdd:TIGR00129   2 EDEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNINI-EVQIDLSSRRFMILKENRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375  102 ITSCCGKGRQgFIFVNDAAKAKDLHDIhVKITPEECFHLMNTLQqssTTFRQTGGVHNTALCDRNNILLSRMDIGRHNAL 181
Cdd:TIGR00129  81 GCSGCGRERL-NRIPKMVGPVKATERF-DLEEIDEALNYMEKEQ---VVWRKTGGTHAAALVDLGGLVSRMEDVGRHNAV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375  182 DKIYGHCLRNDISIKGKIIAFSGRISSEILLKVSKIGCEIVLSKSAPTKLALQLAHDLGITVVGFIRNESCNIYTHPKRI 261
Cdd:TIGR00129 156 DKLIGSALLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIYTHPERL 235
 
Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
1-260 1.55e-134

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 380.29  E-value: 1.55e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375   1 MGPTQETYTIVRYQSGTFSKQLDEIVTESPITIKLNGEEYVTVVCTPNYIEDMVIGFLISEGIISSYKDVEELWVQKDNG 80
Cdd:PRK00724   2 MGPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375  81 IVHVKSSKVNPLYQTL-YNKRYITSCCGKGRQGFIFVNDAAKAKDLHDIHVKITPEECFHLMNTLQQSSTTFRQTGGVHN 159
Cdd:PRK00724  82 GVEVQLELSSRRFAGLkARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375 160 TA-LCDRNNILLSRMDIGRHNALDKIYGHCLRNDISIKGKIIAFSGRISSEILLKVSKIGCEIVLSKSAPTKLALQLAHD 238
Cdd:PRK00724 162 AAlLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEE 241
                        250       260
                 ....*....|....*....|..
gi 446451375 239 LGITVVGFIRNESCNIYTHPKR 260
Cdd:PRK00724 242 LGLTLVGFARGGRFNIYTHPQR 263
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
26-262 3.24e-114

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: 327.97  E-value: 3.24e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375   26 VTESPITIKLNGEEYVTVVCTPNYIEDMVIGFLISEGIISSYKDVEELWVQKDNGIVHVKSSKVNPLYQTLYNKRYITSC 105
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGGSVEVATRRGLLKLERRFLKRTGTSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375  106 CGKGRQGFIFVNDAAKAKDLHDIHVKITPEECFHLMNTLQQSSTTFRQTGGVHNTALCD-RNNILLSRMDIGRHNALDKI 184
Cdd:pfam02634  81 CGLGVEFLEDALDALRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDaEGGLLLFREDIGRHNALDKL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446451375  185 YGHCLRNDISIKGKIIAFSGRISSEILLKVSKIGCEIVLSKSAPTKLALQLAHDLGITVVGFIRNESCNIYTHPKRID 262
Cdd:pfam02634 161 IGAALLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVYTHPERII 238
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
6-261 1.02e-103

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 302.07  E-value: 1.02e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375   6 ETYTIVRYQSGTFSKQLDEIVTESPITIKLNGEEYVTVVCTPNYIEDMVIGFLISEGIISSYKDVEELWV--QKDNGIVH 83
Cdd:COG1526    3 KRVPVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVdeDEGGIVVR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375  84 VK-SSKVNPLYQTLYNKRYITSCCGK-GRQgfifVNDAA--KAKDLHDiHVKITPEECFHLMNTLQQSSTTFRQTGGVHN 159
Cdd:COG1526   83 VElAPGAFADLKERRRRLTGTSGCGLcGTE----SLDALlrPLPPLPS-DLRLSAEALLALLDALREAQPLFRRTGGVHA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375 160 TALCDRN-NILLSRMDIGRHNALDKIYGHCLRNDISIKGKIIAFSGRISSEILLKVSKIGCEIVLSKSAPTKLALQLAHD 238
Cdd:COG1526  158 AALFDPDgELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEE 237
                        250       260
                 ....*....|....*....|...
gi 446451375 239 LGITVVGFIRNESCNIYTHPKRI 261
Cdd:COG1526  238 AGLTLIGFARGDRFNVYTHPERI 260
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
22-261 7.29e-74

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: 225.43  E-value: 7.29e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375   22 LDEIVTESPITIKLNGEEYVTVVCTPNYIEDMVIGFLISEGIISSYKDVEELWVQKDNGIvHVKSSKVNPLYQTLYNKRY 101
Cdd:TIGR00129   2 EDEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNINI-EVQIDLSSRRFMILKENRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375  102 ITSCCGKGRQgFIFVNDAAKAKDLHDIhVKITPEECFHLMNTLQqssTTFRQTGGVHNTALCDRNNILLSRMDIGRHNAL 181
Cdd:TIGR00129  81 GCSGCGRERL-NRIPKMVGPVKATERF-DLEEIDEALNYMEKEQ---VVWRKTGGTHAAALVDLGGLVSRMEDVGRHNAV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446451375  182 DKIYGHCLRNDISIKGKIIAFSGRISSEILLKVSKIGCEIVLSKSAPTKLALQLAHDLGITVVGFIRNESCNIYTHPKRI 261
Cdd:TIGR00129 156 DKLIGSALLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIYTHPERL 235
 
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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