NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|291333226|gb|ADD92936|]
View 

hypothetical protein [uncultured archaeon MedDCM-OCT-S04-C14]

Protein Classification

formate dehydrogenase accessory sulfurtransferase FdhD( domain architecture ID 844)

formate dehydrogenase accessory sulfurtransferase FdhD is involved in the production or activity of formate dehydrogenase-H

Gene Ontology:  GO:0016783|GO:0097163|GO:0008863|GO:0015942

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FdhD-NarQ super family cl00659
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
 1-123 6.71e-43

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.


The actual alignment was detected with superfamily member COG1526:

Pssm-ID: 469863  Cd Length: 260  Bit Score: 141.83  E-value: 6.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333226   1 MDLKTVVQALYEMRSHQQDFSQTGGVHAAGLLVADGTPLRVREDIGRHNAVDKVYGLWSRTG-DETPLALLLSGRCGWDI 79
Cdd:COG1526  130 LSAEALLALLDALREAQPLFRRTGGVHAAALFDPDGELLLVREDVGRHNALDKLIGAALLEGiDLSDGILLVSGRASSEM 209

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 291333226  80 VAKAASMNTPIIASFGAASSLAVDAARWANITLVSFVRDGKAVV 123
Cdd:COG1526  210 VQKAARAGIPILVSVSAPTSLAVELAEEAGLTLIGFARGDRFNV 253
 
Name Accession Description Interval E-value
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
 1-123 6.71e-43

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 141.83  E-value: 6.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333226   1 MDLKTVVQALYEMRSHQQDFSQTGGVHAAGLLVADGTPLRVREDIGRHNAVDKVYGLWSRTG-DETPLALLLSGRCGWDI 79
Cdd:COG1526  130 LSAEALLALLDALREAQPLFRRTGGVHAAALFDPDGELLLVREDVGRHNALDKLIGAALLEGiDLSDGILLVSGRASSEM 209

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 291333226  80 VAKAASMNTPIIASFGAASSLAVDAARWANITLVSFVRDGKAVV 123
Cdd:COG1526  210 VQKAARAGIPILVSVSAPTSLAVELAEEAGLTLIGFARGDRFNV 253
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
2-123 1.21e-42

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 141.08  E-value: 1.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333226   2 DLKTVVQALYEMRSHQQDFSQTGGVHAAGLLVADGTPLRVREDIGRHNAVDKVYGLWSRTG-DETPLALLLSGRCGWDIV 80
Cdd:PRK00724 135 TAEDLDRAMAQLQDAQPLFQLTGGVHAAALLCPDGELLAVREDVGRHNALDKLIGAALRAGiPLRDGALLVSGRASSEMV 214

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 291333226  81 AKAASMNTPIIASFGAASSLAVDAARWANITLVSFVRDGKAVV 123
Cdd:PRK00724 215 QKAAMAGIPILVAVSAPTSLAVELAEELGLTLVGFARGGRFNI 257
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
 2-123 6.95e-42

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: 138.45  E-value: 6.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333226    2 DLKTVVQALYEMRSHQQDFSQTGGVHAAGLLVADGTPLRVREDIGRHNAVDKVYGLWSRTG-DETPLALLLSGRCGWDIV 80
Cdd:pfam02634 108 SAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRHNALDKLIGAALLNGiDLSDKILVVSGRLSSEMV 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 291333226   81 AKAASMNTPIIASFGAASSLAVDAARWANITLVSFVRDGKAVV 123
Cdd:pfam02634 188 QKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNV 230
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
 2-123 1.42e-28

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: 104.47  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333226    2 DLKTVVQALYEMRSHQQDFSQTGGVHAAGLLVADGTpLRVREDIGRHNAVDKVYGLWSRTGDETP-LALLLSGRCGWDIV 80
Cdd:TIGR00129 107 DLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLGGL-VSRMEDVGRHNAVDKLIGSALLNGANLRkGFILYSGRISSEMV 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 291333226   81 AKAASMNTPIIASFGAASSLAVDAARWANITLVSFVRDGKAVV 123
Cdd:TIGR00129 186 QKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNI 228
 
Name Accession Description Interval E-value
FdhD COG1526
Formate dehydrogenase assembly factor FdhD, a sulfurtransferase [Energy production and ...
 1-123 6.71e-43

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


Pssm-ID: 441135  Cd Length: 260  Bit Score: 141.83  E-value: 6.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333226   1 MDLKTVVQALYEMRSHQQDFSQTGGVHAAGLLVADGTPLRVREDIGRHNAVDKVYGLWSRTG-DETPLALLLSGRCGWDI 79
Cdd:COG1526  130 LSAEALLALLDALREAQPLFRRTGGVHAAALFDPDGELLLVREDVGRHNALDKLIGAALLEGiDLSDGILLVSGRASSEM 209

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 291333226  80 VAKAASMNTPIIASFGAASSLAVDAARWANITLVSFVRDGKAVV 123
Cdd:COG1526  210 VQKAARAGIPILVSVSAPTSLAVELAEEAGLTLIGFARGDRFNV 253
PRK00724 PRK00724
formate dehydrogenase accessory sulfurtransferase FdhD;
2-123 1.21e-42

formate dehydrogenase accessory sulfurtransferase FdhD;


Pssm-ID: 234823  Cd Length: 263  Bit Score: 141.08  E-value: 1.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333226   2 DLKTVVQALYEMRSHQQDFSQTGGVHAAGLLVADGTPLRVREDIGRHNAVDKVYGLWSRTG-DETPLALLLSGRCGWDIV 80
Cdd:PRK00724 135 TAEDLDRAMAQLQDAQPLFQLTGGVHAAALLCPDGELLAVREDVGRHNALDKLIGAALRAGiPLRDGALLVSGRASSEMV 214

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 291333226  81 AKAASMNTPIIASFGAASSLAVDAARWANITLVSFVRDGKAVV 123
Cdd:PRK00724 215 QKAAMAGIPILVAVSAPTSLAVELAEELGLTLVGFARGGRFNI 257
FdhD-NarQ pfam02634
FdhD/NarQ family; A pan-bacterial lineage of proteins. Nitrate assimilation protein, NarQ, and ...
 2-123 6.95e-42

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: 138.45  E-value: 6.95e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333226    2 DLKTVVQALYEMRSHQQDFSQTGGVHAAGLLVADGTPLRVREDIGRHNAVDKVYGLWSRTG-DETPLALLLSGRCGWDIV 80
Cdd:pfam02634 108 SAETILALMDALNRAQELFRRTGGVHAAALFDAEGGLLLFREDIGRHNALDKLIGAALLNGiDLSDKILVVSGRLSSEMV 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 291333226   81 AKAASMNTPIIASFGAASSLAVDAARWANITLVSFVRDGKAVV 123
Cdd:pfam02634 188 QKAARAGIPVLVSRSAPTSLAVELAEELGITLIGFARGGRFNV 230
fdhD_narQ TIGR00129
formate dehydrogenase family accessory protein FdhD; FdhD in E. coli and NarQ in B. subtilis ...
 2-123 1.42e-28

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: 104.47  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333226    2 DLKTVVQALYEMRSHQQDFSQTGGVHAAGLLVADGTpLRVREDIGRHNAVDKVYGLWSRTGDETP-LALLLSGRCGWDIV 80
Cdd:TIGR00129 107 DLEEIDEALNYMEKEQVVWRKTGGTHAAALVDLGGL-VSRMEDVGRHNAVDKLIGSALLNGANLRkGFILYSGRISSEMV 185

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 291333226   81 AKAASMNTPIIASFGAASSLAVDAARWANITLVSFVRDGKAVV 123
Cdd:TIGR00129 186 QKAARCGVPIIASKSAPTDLAIEVAEESNITLIGFARNGRFNI 228
 
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