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Conserved domains on  [gi|2096200996|emb|CAG9433379|]
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Sulfur carrier protein FdhD [Providencia alcalifaciens]

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;
13-273 6.02e-148

formate dehydrogenase accessory sulfurtransferase FdhD;


:

Pssm-ID: 234823  Cd Length: 263  Bit Score: 414.58  E-value: 6.02e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996  13 SKMIGVQSTTVQQKNNLGSLVNDFVAEEIPIALVYNGISHVVMMATPKDLDDFAVGFSLSEGIIQSRDEIRGIDIVQGCH 92
Cdd:PRK00724    2 MGPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996  93 rGIEVHIELSSRRFMALKERRRNLTGRTGCGICGTEQLDEIFKPITPLPFTQTFSLSYLDNALQELKTVQEIGALTGCTH 172
Cdd:PRK00724   82 -GVEVQLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 173 AAAWISPEGRLVGGCEDVGRHVALDKLLGMKSRS--DWQQGAILVSSRASYEMVQKAASCGAEILFAVSAATSLAIEVAE 250
Cdd:PRK00724  161 AAALLCPDGELLAVREDVGRHNALDKLIGAALRAgiPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAE 240
                         250       260
                  ....*....|....*....|...
gi 2096200996 251 KANLTLVGFCRQGKATVFTHPSR 273
Cdd:PRK00724  241 ELGLTLVGFARGGRFNIYTHPQR 263
 
Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
13-273 6.02e-148

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 414.58  E-value: 6.02e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996  13 SKMIGVQSTTVQQKNNLGSLVNDFVAEEIPIALVYNGISHVVMMATPKDLDDFAVGFSLSEGIIQSRDEIRGIDIVQGCH 92
Cdd:PRK00724    2 MGPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996  93 rGIEVHIELSSRRFMALKERRRNLTGRTGCGICGTEQLDEIFKPITPLPFTQTFSLSYLDNALQELKTVQEIGALTGCTH 172
Cdd:PRK00724   82 -GVEVQLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 173 AAAWISPEGRLVGGCEDVGRHVALDKLLGMKSRS--DWQQGAILVSSRASYEMVQKAASCGAEILFAVSAATSLAIEVAE 250
Cdd:PRK00724  161 AAALLCPDGELLAVREDVGRHNALDKLIGAALRAgiPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAE 240
                         250       260
                  ....*....|....*....|...
gi 2096200996 251 KANLTLVGFCRQGKATVFTHPSR 273
Cdd:PRK00724  241 ELGLTLVGFARGGRFNIYTHPQR 263
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
21-274 3.17e-130

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 369.48  E-value: 3.17e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996  21 TTVQQKNNLGSLVNDFVAEEIPIALVYNGISHVVMMATPKDLDDFAVGFSLSEGIIQSRDEIRGIDIVQGCHrGIEVHIE 100
Cdd:COG1526     6 PVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEG-GIVVRVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 101 LSSRRFMALKERRRNLTGRTGCGICGTEQLDEIFKPITPLPFTQTFSLSYLDNALQELKTVQEIGALTGCTHAAAWISPE 180
Cdd:COG1526    85 LAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAALFDPD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 181 GRLVGGCEDVGRHVALDKLLG--MKSRSDWQQGAILVSSRASYEMVQKAASCGAEILFAVSAATSLAIEVAEKANLTLVG 258
Cdd:COG1526   165 GELLLVREDVGRHNALDKLIGaaLLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGLTLIG 244
                         250
                  ....*....|....*.
gi 2096200996 259 FCRQGKATVFTHPSRV 274
Cdd:COG1526   245 FARGDRFNVYTHPERI 260
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
33-275 4.35e-100

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: 292.45  E-value: 4.35e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996  33 VNDFVAEEIPIALVYNGISHVVMMATPKDLDDFAVGFSLSEGIIQSRDEIRGIDIVQGChrGIEVHIELSSRRFMALKER 112
Cdd:TIGR00129   1 VEDEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNI--NIEVQIDLSSRRFMILKEN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 113 RrnltgrTGCGICGTEQLDEIFKPITPLPFTQTFSLSYLDNALQELKTVQEIGALTGCTHAAAWISPEGrLVGGCEDVGR 192
Cdd:TIGR00129  79 R------TGCSGCGRERLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLGG-LVSRMEDVGR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 193 HVALDKLLG--MKSRSDWQQGAILVSSRASYEMVQKAASCGAEILFAVSAATSLAIEVAEKANLTLVGFCRQGKATVFTH 270
Cdd:TIGR00129 152 HNAVDKLIGsaLLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIYTH 231

                  ....*
gi 2096200996 271 PSRVR 275
Cdd:TIGR00129 232 PERLL 236
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
38-275 4.79e-93

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: 274.43  E-value: 4.79e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996  38 AEEIPIALVYNGISHVVMMATPKDLDDFAVGFSLSEGIIQSRDEIRGIDIVQGCHrgievHIELSSRRFmALKERRRNL- 116
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGG-----SVEVATRRG-LLKLERRFLk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 117 -TGRTGCGIcGTEQLDEIFKPITPLPF---TQTFSLSYLDNALQELKTVQEIGALTGCTHAAAWISPEGRLVGGCEDVGR 192
Cdd:pfam02634  75 rTGTSGCGL-GVEFLEDALDALRALPLpssDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 193 HVALDKLLG--MKSRSDWQQGAILVSSRASYEMVQKAASCGAEILFAVSAATSLAIEVAEKANLTLVGFCRQGKATVFTH 270
Cdd:pfam02634 154 HNALDKLIGaaLLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVYTH 233

                  ....*
gi 2096200996 271 PSRVR 275
Cdd:pfam02634 234 PERII 238
 
Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
13-273 6.02e-148

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 414.58  E-value: 6.02e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996  13 SKMIGVQSTTVQQKNNLGSLVNDFVAEEIPIALVYNGISHVVMMATPKDLDDFAVGFSLSEGIIQSRDEIRGIDIVQGCH 92
Cdd:PRK00724    2 MGPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996  93 rGIEVHIELSSRRFMALKERRRNLTGRTGCGICGTEQLDEIFKPITPLPFTQTFSLSYLDNALQELKTVQEIGALTGCTH 172
Cdd:PRK00724   82 -GVEVQLELSSRRFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 173 AAAWISPEGRLVGGCEDVGRHVALDKLLGMKSRS--DWQQGAILVSSRASYEMVQKAASCGAEILFAVSAATSLAIEVAE 250
Cdd:PRK00724  161 AAALLCPDGELLAVREDVGRHNALDKLIGAALRAgiPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAE 240
                         250       260
                  ....*....|....*....|...
gi 2096200996 251 KANLTLVGFCRQGKATVFTHPSR 273
Cdd:PRK00724  241 ELGLTLVGFARGGRFNIYTHPQR 263
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
21-274 3.17e-130

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 369.48  E-value: 3.17e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996  21 TTVQQKNNLGSLVNDFVAEEIPIALVYNGISHVVMMATPKDLDDFAVGFSLSEGIIQSRDEIRGIDIVQGCHrGIEVHIE 100
Cdd:COG1526     6 PVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEG-GIVVRVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 101 LSSRRFMALKERRRNLTGRTGCGICGTEQLDEIFKPITPLPFTQTFSLSYLDNALQELKTVQEIGALTGCTHAAAWISPE 180
Cdd:COG1526    85 LAPGAFADLKERRRRLTGTSGCGLCGTESLDALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAALFDPD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 181 GRLVGGCEDVGRHVALDKLLG--MKSRSDWQQGAILVSSRASYEMVQKAASCGAEILFAVSAATSLAIEVAEKANLTLVG 258
Cdd:COG1526   165 GELLLVREDVGRHNALDKLIGaaLLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGLTLIG 244
                         250
                  ....*....|....*.
gi 2096200996 259 FCRQGKATVFTHPSRV 274
Cdd:COG1526   245 FARGDRFNVYTHPERI 260
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
33-275 4.35e-100

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: 292.45  E-value: 4.35e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996  33 VNDFVAEEIPIALVYNGISHVVMMATPKDLDDFAVGFSLSEGIIQSRDEIRGIDIVQGChrGIEVHIELSSRRFMALKER 112
Cdd:TIGR00129   1 VEDEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNI--NIEVQIDLSSRRFMILKEN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 113 RrnltgrTGCGICGTEQLDEIFKPITPLPFTQTFSLSYLDNALQELKTVQEIGALTGCTHAAAWISPEGrLVGGCEDVGR 192
Cdd:TIGR00129  79 R------TGCSGCGRERLNRIPKMVGPVKATERFDLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLGG-LVSRMEDVGR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 193 HVALDKLLG--MKSRSDWQQGAILVSSRASYEMVQKAASCGAEILFAVSAATSLAIEVAEKANLTLVGFCRQGKATVFTH 270
Cdd:TIGR00129 152 HNAVDKLIGsaLLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIYTH 231

                  ....*
gi 2096200996 271 PSRVR 275
Cdd:TIGR00129 232 PERLL 236
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
38-275 4.79e-93

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: 274.43  E-value: 4.79e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996  38 AEEIPIALVYNGISHVVMMATPKDLDDFAVGFSLSEGIIQSRDEIRGIDIVQGCHrgievHIELSSRRFmALKERRRNL- 116
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGG-----SVEVATRRG-LLKLERRFLk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 117 -TGRTGCGIcGTEQLDEIFKPITPLPF---TQTFSLSYLDNALQELKTVQEIGALTGCTHAAAWISPEGRLVGGCEDVGR 192
Cdd:pfam02634  75 rTGTSGCGL-GVEFLEDALDALRALPLpssDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096200996 193 HVALDKLLG--MKSRSDWQQGAILVSSRASYEMVQKAASCGAEILFAVSAATSLAIEVAEKANLTLVGFCRQGKATVFTH 270
Cdd:pfam02634 154 HNALDKLIGaaLLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVYTH 233

                  ....*
gi 2096200996 271 PSRVR 275
Cdd:pfam02634 234 PERII 238
 
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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