Reviewed,
UniProtKB/Swiss-Prot P0A1Y2 (ASRC_SALTY)
Last modified
June 16, 2009.
Version 33.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Anaerobic sulfite reductase subunit C EC=1.8.1.- | ||||
| Gene names |
| ||||
| Organism | Salmonella typhimurium [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 90371 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
Protein attributes
| Sequence length | 337 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | This enzyme catalyzes the hydrogen sulfide production from sulfite. It is strictly anaerobic. It is regulated by electron acceptors rather than by cysteine. |
| Catalytic activity | Hydrogen sulfide + 3 NAD+ + 3 H2O = sulfite + 3 NADH. |
| Cofactor | Binds 3 4Fe-4S clusters per subunit. Binds 1 siroheme per subunit. |
| Pathway | |
| Subunit structure | The anaerobic sulfite reductase seems to consist of three subunits. |
| Subcellular location | |
| Induction | By sulfite. |
| Sequence similarities | Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. Contains 2 4Fe-4S ferredoxin-type domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Cellular component | Cytoplasm |
| Domain | Repeat |
| Ligand | 4Fe-4S Heme Iron Iron-sulfur Metal-binding NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activityInferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro oxidoreductase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 337 | 337 | Anaerobic sulfite reductase subunit C | PRO_0000199965 | |||||
Regions | |||||||||
| Domain | 171 – 200 | 30 | 4Fe-4S ferredoxin-type 1 | ||||||
| Domain | 203 – 232 | 30 | 4Fe-4S ferredoxin-type 2 | ||||||
Sites | |||||||||
| Metal binding | 115 | 1 | Iron-sulfur 1 (4Fe-4S) By similarity | ||||||
| Metal binding | 121 | 1 | Iron-sulfur 1 (4Fe-4S) By similarity | ||||||
| Metal binding | 153 | 1 | Iron-sulfur 1 (4Fe-4S) By similarity | ||||||
| Metal binding | 157 | 1 | Iron (siroheme axial ligand) By similarity | ||||||
| Metal binding | 157 | 1 | Iron-sulfur 1 (4Fe-4S) By similarity | ||||||
| Metal binding | 180 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 183 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 186 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 190 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity | ||||||
| Metal binding | 212 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity | ||||||
| Metal binding | 215 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity | ||||||
| Metal binding | 218 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity | ||||||
| Metal binding | 222 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 247 – 250 | 4 | TPRV → SGAL in AAA99277. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence analysis and expression of the Salmonella typhimurium asr operon encoding production of hydrogen sulfide from sulfite." Huang C.J., Barrett E.L. J. Bacteriol. 173:1544-1553(1991) [PubMed: 1704886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: EB303. |
| [2] | "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K.Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720. |
Cross-references
Sequence databases | |
|---|---|
| M57706 Genomic DNA. Translation: AAA99277.1. AE008816 Genomic DNA. Translation: AAL21444.1. | |
| PIR | C38453. |
| RefSeq | NP_461485.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1K0T based on UniProtKB P31087. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1254072. |
| GenomeReviews | Gene locus STM2550 in contig AE006468_GR. |
| KEGG | stm:STM2550. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P0A1Y2. |
| OMA | P0A1Y2. GRTGKQT. |
Enzyme and pathway databases | |
| BioCyc | MetaCyc:MON-12546. STYP99287:STM2550-MON. |
Family and domain databases | |
| InterPro | IPR017896. 4Fe4S_Fe-S-bd. IPR001450. 4Fe4S_Fe_S_bd_subgr. IPR017900. 4Fe4S_Fe_S_CS. IPR006066. Nir_Si_BS. IPR006067. Nir_Sir_4Fe4S. IPR005117. NiRdtase/SiRdtase_haem-b_fer. IPR014261. Sulphite_reductase_C. [Graphical view] |
| Pfam | PF00037. Fer4. 2 hits. PF01077. NIR_SIR. 1 hit. PF03460. NIR_SIR_ferr. 1 hit. [Graphical view] |
| PRINTS | PR00397. SIROHAEM. |
| TIGRFAMs | TIGR02912. sulfite_red_C. 1 hit. |
| PROSITE | PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 2 hits. PS00365. NIR_SIR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ASRC_SALTY | ||||||||
| Accession | Primary (citable) accession number: P0A1Y2 Secondary accession number(s): P26476 | ||||||||
| 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
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


