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Conserved domains on  [gi|489819473|ref|WP_003723284|]
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formate dehydrogenase accessory sulfurtransferase FdhD [Listeria monocytogenes]

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;
1-259 4.32e-125

formate dehydrogenase accessory sulfurtransferase FdhD;


:

Pssm-ID: 234823  Cd Length: 263  Bit Score: 356.03  E-value: 4.32e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473   1 MDIVSYQKIRRFEAGTFQEIESSVATEYPLTIYVNDQELVTIVCTPEYLEDLVVGFLTSEGIVRGPRDIDSVDIIEATGH 80
Cdd:PRK00724   3 GPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCNG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473  81 AKVSANFVNK-FNAKYRGKRYITSCCGKSRENFYFQSDASLVNVKQNGNLQLTTDMIFRLMEKFEQNSATFHQTGGVHNA 159
Cdd:PRK00724  83 VEVQLELSSRrFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473 160 A-LCSSAEIIYSRMDIGRHNALDKIYGRALQDGTSTEDKAIIFSGRISSEILVKTAKLGCGIILSRSAPTELAINMAEEL 238
Cdd:PRK00724 163 AlLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEEL 242
                        250       260
                 ....*....|....*....|.
gi 489819473 239 NITTVGFIRGDRLNVYSGFER 259
Cdd:PRK00724 243 GLTLVGFARGGRFNIYTHPQR 263
 
Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
1-259 4.32e-125

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 356.03  E-value: 4.32e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473   1 MDIVSYQKIRRFEAGTFQEIESSVATEYPLTIYVNDQELVTIVCTPEYLEDLVVGFLTSEGIVRGPRDIDSVDIIEATGH 80
Cdd:PRK00724   3 GPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCNG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473  81 AKVSANFVNK-FNAKYRGKRYITSCCGKSRENFYFQSDASLVNVKQNGNLQLTTDMIFRLMEKFEQNSATFHQTGGVHNA 159
Cdd:PRK00724  83 VEVQLELSSRrFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473 160 A-LCSSAEIIYSRMDIGRHNALDKIYGRALQDGTSTEDKAIIFSGRISSEILVKTAKLGCGIILSRSAPTELAINMAEEL 238
Cdd:PRK00724 163 AlLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEEL 242
                        250       260
                 ....*....|....*....|.
gi 489819473 239 NITTVGFIRGDRLNVYSGFER 259
Cdd:PRK00724 243 GLTLVGFARGGRFNIYTHPQR 263
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
25-260 4.66e-113

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: 324.50  E-value: 4.66e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473   25 ATEYPLTIYVNDQELVTIVCTPEYLEDLVVGFLTSEGIVRGPRDIDSVDIIEATGHAKVSANFVNKFNAKYRGKRYITSC 104
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGGSVEVATRRGLLKLERRFLKRTGTSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473  105 CGKSRENFYFQSDASLVNVKQNGNLQLTTDMIFRLMEKFEQNSATFHQTGGVHNAALCSSA-EIIYSRMDIGRHNALDKI 183
Cdd:pfam02634  81 CGLGVEFLEDALDALRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEgGLLLFREDIGRHNALDKL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489819473  184 YGRALQDGTSTEDKAIIFSGRISSEILVKTAKLGCGIILSRSAPTELAINMAEELNITTVGFIRGDRLNVYSGFERI 260
Cdd:pfam02634 161 IGAALLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVYTHPERI 237
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
8-260 1.07e-104

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 304.38  E-value: 1.07e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473   8 KIRRFEAGTFQEIESSVATEYPLTIYVNDQELVTIVCTPEYLEDLVVGFLTSEGIVRGPRDIDSVDIIEATGHAKVSANF 87
Cdd:COG1526    6 PVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGIVVRVEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473  88 VNKFNAKYRGKR---YITSCCGK-SRENFyfqSDASLVNVKQNGNLQLTTDMIFRLMEKFEQNSATFHQTGGVHNAALCS 163
Cdd:COG1526   86 APGAFADLKERRrrlTGTSGCGLcGTESL---DALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAALFD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473 164 SA-EIIYSRMDIGRHNALDKIYGRALQDGTSTEDKAIIFSGRISSEILVKTAKLGCGIILSRSAPTELAINMAEELNITT 242
Cdd:COG1526  163 PDgELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGLTL 242
                        250
                 ....*....|....*...
gi 489819473 243 VGFIRGDRLNVYSGFERI 260
Cdd:COG1526  243 IGFARGDRFNVYTHPERI 260
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
21-260 5.54e-67

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: 207.71  E-value: 5.54e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473   21 ESSVATEYPLTIYVNDQELVTIVCTPEYLEDLVVGFLTSEGIVRGPRDIDSVDIIEATGhAKVSANFVNKFNAKYRGKRY 100
Cdd:TIGR00129   2 EDEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNIN-IEVQIDLSSRRFMILKENRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473  101 ITSCCGKSRENfYFQSDASLVNVKQNGNLQLTtDMIFRLMEKFEqnsATFHQTGGVHNAALCSSAEIIYSRMDIGRHNAL 180
Cdd:TIGR00129  81 GCSGCGRERLN-RIPKMVGPVKATERFDLEEI-DEALNYMEKEQ---VVWRKTGGTHAAALVDLGGLVSRMEDVGRHNAV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473  181 DKIYGRALQDGTSTEDKAIIFSGRISSEILVKTAKLGCGIILSRSAPTELAINMAEELNITTVGFIRGDRLNVYSGFERI 260
Cdd:TIGR00129 156 DKLIGSALLNGANLRKGFILYSGRISSEMVQKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNIYTHPERL 235
 
Name Accession Description Interval E-value
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
1-259 4.32e-125

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 356.03  E-value: 4.32e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473   1 MDIVSYQKIRRFEAGTFQEIESSVATEYPLTIYVNDQELVTIVCTPEYLEDLVVGFLTSEGIVRGPRDIDSVDIIEATGH 80
Cdd:PRK00724   3 GPVTVRRTIVRYRDGLFSEREDTVAEEVPVAIVYNGISHAVMMATPGDLEDFAIGFLLSEGIIRSPEDIESIDIVESCNG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473  81 AKVSANFVNK-FNAKYRGKRYITSCCGKSRENFYFQSDASLVNVKQNGNLQLTTDMIFRLMEKFEQNSATFHQTGGVHNA 159
Cdd:PRK00724  83 VEVQLELSSRrFAGLKARRRNIAGRCGCGVCGVESLEDALKPVAPLPFTQTFTAEDLDRAMAQLQDAQPLFQLTGGVHAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473 160 A-LCSSAEIIYSRMDIGRHNALDKIYGRALQDGTSTEDKAIIFSGRISSEILVKTAKLGCGIILSRSAPTELAINMAEEL 238
Cdd:PRK00724 163 AlLCPDGELLAVREDVGRHNALDKLIGAALRAGIPLRDGALLVSGRASSEMVQKAAMAGIPILVAVSAPTSLAVELAEEL 242
                        250       260
                 ....*....|....*....|.
gi 489819473 239 NITTVGFIRGDRLNVYSGFER 259
Cdd:PRK00724 243 GLTLVGFARGGRFNIYTHPQR 263
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
25-260 4.66e-113

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: 324.50  E-value: 4.66e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473   25 ATEYPLTIYVNDQELVTIVCTPEYLEDLVVGFLTSEGIVRGPRDIDSVDIIEATGHAKVSANFVNKFNAKYRGKRYITSC 104
Cdd:pfam02634   1 AEEVPLTIYLNGRELATLMATPADLEDLAVGFLLSEGIIDSAEDIESIEVDEDGGSVEVATRRGLLKLERRFLKRTGTSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473  105 CGKSRENFYFQSDASLVNVKQNGNLQLTTDMIFRLMEKFEQNSATFHQTGGVHNAALCSSA-EIIYSRMDIGRHNALDKI 183
Cdd:pfam02634  81 CGLGVEFLEDALDALRALPLPSSDLRLSAETILALMDALNRAQELFRRTGGVHAAALFDAEgGLLLFREDIGRHNALDKL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489819473  184 YGRALQDGTSTEDKAIIFSGRISSEILVKTAKLGCGIILSRSAPTELAINMAEELNITTVGFIRGDRLNVYSGFERI 260
Cdd:pfam02634 161 IGAALLNGIDLSDKILVVSGRLSSEMVQKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNVYTHPERI 237
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
8-260 1.07e-104

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 304.38  E-value: 1.07e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473   8 KIRRFEAGTFQEIESSVATEYPLTIYVNDQELVTIVCTPEYLEDLVVGFLTSEGIVRGPRDIDSVDIIEATGHAKVSANF 87
Cdd:COG1526    6 PVLRIRDGGAEEREDEVAEEEPLAIVVNGREHAVMMATPGDLEDLALGFLLSEGIIRSPDDIESIEVDEDEGGIVVRVEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473  88 VNKFNAKYRGKR---YITSCCGK-SRENFyfqSDASLVNVKQNGNLQLTTDMIFRLMEKFEQNSATFHQTGGVHNAALCS 163
Cdd:COG1526   86 APGAFADLKERRrrlTGTSGCGLcGTESL---DALLRPLPPLPSDLRLSAEALLALLDALREAQPLFRRTGGVHAAALFD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473 164 SA-EIIYSRMDIGRHNALDKIYGRALQDGTSTEDKAIIFSGRISSEILVKTAKLGCGIILSRSAPTELAINMAEELNITT 242
Cdd:COG1526  163 PDgELLLVREDVGRHNALDKLIGAALLEGIDLSDGILLVSGRASSEMVQKAARAGIPILVSVSAPTSLAVELAEEAGLTL 242
                        250
                 ....*....|....*...
gi 489819473 243 VGFIRGDRLNVYSGFERI 260
Cdd:COG1526  243 IGFARGDRFNVYTHPERI 260
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
21-260 5.54e-67

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: 207.71  E-value: 5.54e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473   21 ESSVATEYPLTIYVNDQELVTIVCTPEYLEDLVVGFLTSEGIVRGPRDIDSVDIIEATGhAKVSANFVNKFNAKYRGKRY 100
Cdd:TIGR00129   2 EDEVAVEIPVTIVINGISHVVLMCSPKNLEEFAVGFLLSEGIINSPDDIEGIEIDDNIN-IEVQIDLSSRRFMILKENRT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473  101 ITSCCGKSRENfYFQSDASLVNVKQNGNLQLTtDMIFRLMEKFEqnsATFHQTGGVHNAALCSSAEIIYSRMDIGRHNAL 180
Cdd:TIGR00129  81 GCSGCGRERLN-RIPKMVGPVKATERFDLEEI-DEALNYMEKEQ---VVWRKTGGTHAAALVDLGGLVSRMEDVGRHNAV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489819473  181 DKIYGRALQDGTSTEDKAIIFSGRISSEILVKTAKLGCGIILSRSAPTELAINMAEELNITTVGFIRGDRLNVYSGFERI 260
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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