NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|238691427|sp|B2K7H2|]
View 

RecName: Full=Sulfur carrier protein FdhD

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
17-272 1.02e-156

formate dehydrogenase accessory sulfurtransferase FdhD;


:

Pssm-ID: 234823  Cd Length: 263  Bit Score: 436.53  E-value: 1.02e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  17 GARQLDVLQRHKLAEPQQDWLAEEVPVALVYNGISHVVMMATPKDLAAFALGFSLSEGIISSPQDIYAIEMTPGCNGIEV 96
Cdd:PRK00724   6 TVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCNGVEV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  97 NIELSSRRFAGLKERRRAMAGRTGCGVCGIEQLDDIFRPITPLPFTQAFNLEHLDTALAQLKQVQPVGQLTGCTHAAAWI 176
Cdd:PRK00724  86 QLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHAAALL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427 177 NPEGELLGGCEDVGRHVALDKLLG--IRAKQPWQQGAVLVSSRASYEMVQKTAMCGAEILFAVSAATTLAVEVAERCNLT 254
Cdd:PRK00724 166 CPDGELLAVREDVGRHNALDKLIGaaLRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEELGLT 245
                        250
                 ....*....|....*...
gi 238691427 255 LVGFSKPGRATVYTHPQR 272
Cdd:PRK00724 246 LVGFARGGRFNIYTHPQR 263
 
Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
17-272 1.02e-156

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 436.53  E-value: 1.02e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  17 GARQLDVLQRHKLAEPQQDWLAEEVPVALVYNGISHVVMMATPKDLAAFALGFSLSEGIISSPQDIYAIEMTPGCNGIEV 96
Cdd:PRK00724   6 TVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCNGVEV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  97 NIELSSRRFAGLKERRRAMAGRTGCGVCGIEQLDDIFRPITPLPFTQAFNLEHLDTALAQLKQVQPVGQLTGCTHAAAWI 176
Cdd:PRK00724  86 QLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHAAALL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427 177 NPEGELLGGCEDVGRHVALDKLLG--IRAKQPWQQGAVLVSSRASYEMVQKTAMCGAEILFAVSAATTLAVEVAERCNLT 254
Cdd:PRK00724 166 CPDGELLAVREDVGRHNALDKLIGaaLRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEELGLT 245
                        250
                 ....*....|....*...
gi 238691427 255 LVGFSKPGRATVYTHPQR 272
Cdd:PRK00724 246 LVGFARGGRFNIYTHPQR 263
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
26-273 3.66e-134

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 379.50  E-value: 3.66e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  26 RHKLAEPQQDWLAEEVPVALVYNGISHVVMMATPKDLAAFALGFSLSEGIISSPQDIYAIEMTPGCNGIEVNIELSSRRF 105
Cdd:COG1526   11 RDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGIVVRVELAPGAF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427 106 AGLKERRRAMAGRTGCGVCGIEQLDDIFRPITPLPFTQAFNLEHLDTALAQLKQVQPVGQLTGCTHAAAWINPEGELLGG 185
Cdd:COG1526   91 ADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAALFDPDGELLLV 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427 186 CEDVGRHVALDKLLG--IRAKQPWQQGAVLVSSRASYEMVQKTAMCGAEILFAVSAATTLAVEVAERCNLTLVGFSKPGR 263
Cdd:COG1526  171 REDVGRHNALDKLIGaaLLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGLTLIGFARGDR 250
                        250
                 ....*....|
gi 238691427 264 ATVYTHPQRI 273
Cdd:COG1526  251 FNVYTHPERI 260
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
35-273 2.35e-105

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: 305.55  E-value: 2.35e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427   35 DWLAEEVPVALVYNGISHVVMMATPKDLAAFALGFSLSEGIISSPQDIYAIEMTPGCNgIEVNIELSSRRFAGLKERRra 114
Cdd:TIGR00129   3 DEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNIN-IEVQIDLSSRRFMILKENR-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  115 magrTGCGVCGIEQLDDIFRPITPLPFTQAFNLEHLDTALAQLKQVQPVGQLTGCTHAAAWINPeGELLGGCEDVGRHVA 194
Cdd:TIGR00129  80 ----TGCSGCGRERLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDL-GGLVSRMEDVGRHNA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  195 LDKLLGIRAKQ--PWQQGAVLVSSRASYEMVQKTAMCGAEILFAVSAATTLAVEVAERCNLTLVGFSKPGRATVYTHPQR 272
Cdd:TIGR00129 155 VDKLIGSALLNgaNLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIYTHPER 234

                  .
gi 238691427  273 I 273
Cdd:TIGR00129 235 L 235
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
38-273 3.23e-95

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: 279.82  E-value: 3.23e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427   38 AEEVPVALVYNGISHVVMMATPKDLAAFALGFSLSEGIISSPQDIYAIEMTPGCNGIEVnielSSRRFAGLKERRRAM-A 116
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGGSVEV----ATRRGLLKLERRFLKrT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  117 GRTGC--GVCGIEQLDDIFRPITPLPFTQAFNLEHLDTALAQLKQVQPVGQLTGCTHAAAWINPEGELLGGCEDVGRHVA 194
Cdd:pfam02634  77 GTSGCglGVEFLEDALDALRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRHNA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  195 LDKLLG--IRAKQPWQQGAVLVSSRASYEMVQKTAMCGAEILFAVSAATTLAVEVAERCNLTLVGFSKPGRATVYTHPQR 272
Cdd:pfam02634 157 LDKLIGaaLLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVYTHPER 236

                  .
gi 238691427  273 I 273
Cdd:pfam02634 237 I 237
 
Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
17-272 1.02e-156

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 436.53  E-value: 1.02e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  17 GARQLDVLQRHKLAEPQQDWLAEEVPVALVYNGISHVVMMATPKDLAAFALGFSLSEGIISSPQDIYAIEMTPGCNGIEV 96
Cdd:PRK00724   6 TVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCNGVEV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  97 NIELSSRRFAGLKERRRAMAGRTGCGVCGIEQLDDIFRPITPLPFTQAFNLEHLDTALAQLKQVQPVGQLTGCTHAAAWI 176
Cdd:PRK00724  86 QLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHAAALL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427 177 NPEGELLGGCEDVGRHVALDKLLG--IRAKQPWQQGAVLVSSRASYEMVQKTAMCGAEILFAVSAATTLAVEVAERCNLT 254
Cdd:PRK00724 166 CPDGELLAVREDVGRHNALDKLIGaaLRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEELGLT 245
                        250
                 ....*....|....*...
gi 238691427 255 LVGFSKPGRATVYTHPQR 272
Cdd:PRK00724 246 LVGFARGGRFNIYTHPQR 263
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
26-273 3.66e-134

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 379.50  E-value: 3.66e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  26 RHKLAEPQQDWLAEEVPVALVYNGISHVVMMATPKDLAAFALGFSLSEGIISSPQDIYAIEMTPGCNGIEVNIELSSRRF 105
Cdd:COG1526   11 RDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGIVVRVELAPGAF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427 106 AGLKERRRAMAGRTGCGVCGIEQLDDIFRPITPLPFTQAFNLEHLDTALAQLKQVQPVGQLTGCTHAAAWINPEGELLGG 185
Cdd:COG1526   91 ADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAALFDPDGELLLV 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427 186 CEDVGRHVALDKLLG--IRAKQPWQQGAVLVSSRASYEMVQKTAMCGAEILFAVSAATTLAVEVAERCNLTLVGFSKPGR 263
Cdd:COG1526  171 REDVGRHNALDKLIGaaLLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGLTLIGFARGDR 250
                        250
                 ....*....|
gi 238691427 264 ATVYTHPQRI 273
Cdd:COG1526  251 FNVYTHPERI 260
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
35-273 2.35e-105

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: 305.55  E-value: 2.35e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427   35 DWLAEEVPVALVYNGISHVVMMATPKDLAAFALGFSLSEGIISSPQDIYAIEMTPGCNgIEVNIELSSRRFAGLKERRra 114
Cdd:TIGR00129   3 DEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNIN-IEVQIDLSSRRFMILKENR-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  115 magrTGCGVCGIEQLDDIFRPITPLPFTQAFNLEHLDTALAQLKQVQPVGQLTGCTHAAAWINPeGELLGGCEDVGRHVA 194
Cdd:TIGR00129  80 ----TGCSGCGRERLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDL-GGLVSRMEDVGRHNA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  195 LDKLLGIRAKQ--PWQQGAVLVSSRASYEMVQKTAMCGAEILFAVSAATTLAVEVAERCNLTLVGFSKPGRATVYTHPQR 272
Cdd:TIGR00129 155 VDKLIGSALLNgaNLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIYTHPER 234

                  .
gi 238691427  273 I 273
Cdd:TIGR00129 235 L 235
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
38-273 3.23e-95

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: 279.82  E-value: 3.23e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427   38 AEEVPVALVYNGISHVVMMATPKDLAAFALGFSLSEGIISSPQDIYAIEMTPGCNGIEVnielSSRRFAGLKERRRAM-A 116
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGGSVEV----ATRRGLLKLERRFLKrT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  117 GRTGC--GVCGIEQLDDIFRPITPLPFTQAFNLEHLDTALAQLKQVQPVGQLTGCTHAAAWINPEGELLGGCEDVGRHVA 194
Cdd:pfam02634  77 GTSGCglGVEFLEDALDALRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRHNA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238691427  195 LDKLLG--IRAKQPWQQGAVLVSSRASYEMVQKTAMCGAEILFAVSAATTLAVEVAERCNLTLVGFSKPGRATVYTHPQR 272
Cdd:pfam02634 157 LDKLIGaaLLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVYTHPER 236

                  .
gi 238691427  273 I 273
Cdd:pfam02634 237 I 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH