Reviewed,
UniProtKB/Swiss-Prot P45574 (DSVA_DESVH)
Last modified
November 25, 2008.
Version 56.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Sulfite reductase, dissimilatory-type subunit alpha EC=1.8.99.3 Alternative name(s): Desulfoviridin subunit alpha Hydrogensulfite reductase alpha subunit | ||||
| Gene names |
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| Organism | Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 882 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio |
Protein attributes
| Sequence length | 437 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the reduction of sulfite to sulfide. This is the terminal oxidation reaction in sulfate respiration, a process catalyzed by the sulfate-reducing bacteria. |
| Catalytic activity | (O(3)S.S.SO(3))(2-) + acceptor + 2 H(2)O + OH(-) = 3 HSO(3)(-) + reduced acceptor. |
| Cofactor | Binds 1 4Fe-4S cluster per subunit. Binds 2 sirohemes per subunit. |
| Subunit structure | Heterohexamer of two alpha, two beta and two gamma subunits. |
| Sequence similarities | Contains 1 4Fe-4S ferredoxin-type domain. |
Ontologies
Keywords | |
|---|---|
| Ligand | 4Fe-4S Heme Iron Iron-sulfur Metal-binding |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro hydrogensulfite reductase activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||
| Chain | 2 – 437 | 436 | Sulfite reductase, dissimilatory-type subunit alpha | PRO_0000080030 | |||||
Regions | |||||||||
| Domain | 294 – 322 | 29 | 4Fe-4S ferredoxin-type | ||||||
Sites | |||||||||
| Metal binding | 177 | 1 | Iron (heme axial ligand) Potential | ||||||
| Metal binding | 183 | 1 | Iron (heme axial ligand) Potential | ||||||
| Metal binding | 221 | 1 | Iron (heme axial ligand) Potential | ||||||
| Metal binding | 225 | 1 | Iron (heme axial ligand) Potential | ||||||
| Metal binding | 284 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 303 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 306 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
| Metal binding | 309 | 1 | Iron-sulfur (4Fe-4S) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 22 | 1 | S → V AA sequence Ref.3 | ||||||
| Sequence conflict | 26 | 1 | Q → K AA sequence Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Conservation of the genes for dissimilatory sulfite reductase from Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their detection by PCR." Karkhoff-Schweizer R.R., Huber D.P.W., Voordouw G. Appl. Environ. Microbiol. 61:290-296(1995) [PubMed: 7887608] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough." Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Fouts D.E. Fraser C.M.Nat. Biotechnol. 22:554-559(2004) [PubMed: 15077118] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "The third subunit of desulfoviridin-type dissimilatory sulfite reductases." Pierik A.J., Duyvis M.G., van Helvoort J.M.L.M., Wolbert R.B.G., Hagen W.R. Eur. J. Biochem. 205:111-115(1992) [PubMed: 1555572] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-26. |
Cross-references
Sequence databases | |
|---|---|
| U16723 Genomic DNA. Translation: AAA70107.1. AE017285 Genomic DNA. Translation: AAS94885.1. | |
| PIR | S21197. |
| RefSeq | YP_009626.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2796152. |
| GenomeReviews | Gene locus DVU_0402 in contig AE017285_GR. |
| KEGG | dvu:DVU0402. |
| TIGR | DVU_0402. |
Phylogenomic databases | |
| HOGENOM | P45574. |
Enzyme and pathway databases | |
| BioCyc | DVUL882:DVU_0402-MON. MetaCyc:MON-12511. |
Family and domain databases | |
| InterPro | IPR011806. DsrA. IPR006067. Nir_Sir_4Fe4S. [Graphical view] |
| Pfam | PF01077. NIR_SIR. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02064. dsrA. 1 hit. |
| PROSITE | PS51379. 4FE4S_FER_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DSVA_DESVH | ||||||||
| Accession | Primary (citable) accession number: P45574 Secondary accession number(s): Q46581 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

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