Reviewed,
UniProtKB/Swiss-Prot P17845 (CYSI_SALTY)
Last modified
November 3, 2009.
Version 78.
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 [NADPH] hemoprotein beta-component Short name=SiR-HP Short name=SiRHP EC=1.8.1.2 | ||||
| Gene names |
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| Organism | Salmonella typhimurium [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 90371 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
Protein attributes
| Sequence length | 570 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. HAMAP MF_01540 |
| Catalytic activity | H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP MF_01540 |
| Cofactor | Binds 1 siroheme per subunit. HAMAP MF_01540 Binds 1 4Fe-4S cluster per subunit. HAMAP MF_01540 |
| Pathway | Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. HAMAP MF_01540 |
| Subunit structure | Alpha(8)-beta8. The alpha component is a flavoprotein, the beta component is a hemoprotein. HAMAP MF_01540 |
| Sequence similarities | Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Cysteine biosynthesis |
| Ligand | 4Fe-4S Heme Iron Iron-sulfur Metal-binding NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cysteine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW sulfate assimilationInferred from electronic annotation. Source: HAMAP |
| Cellular component | sulfite reductase complex (NADPH) Inferred from electronic annotation. Source: InterPro |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADP or NADPH bindingInferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro sulfite reductase (NADPH) activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 570 | 569 | Sulfite reductase [NADPH] hemoprotein beta-component HAMAP MF_01540 | PRO_0000199908 | |||||
Sites | |||||||||
| Metal binding | 434 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 440 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 479 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 483 | 1 | Iron (siroheme axial ligand) By similarity | ||||||
| Metal binding | 483 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase." Ostrowski J., Wu J.-Y., Rueger D.C., Miller B.E., Siegel L.M., Kredich N.M. J. Biol. Chem. 264:15726-15737(1989) [PubMed: 2670946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LT2. |
| [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 | |
|---|---|
| M23007 Genomic DNA. Translation: AAA27047.1. AE006468 Genomic DNA. Translation: AAL21827.1. | |
| PIR | A34354. |
| RefSeq | NP_461868.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 7GEP based on UniProtKB P17846. |
| SMR | P17845. Positions 81-570. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P17845. |
Genome annotation databases | |
| GeneID | 1254470. |
| GenomeReviews | Gene locus STM2947 in contig AE006468_GR. |
| KEGG | stm:STM2947. |
| NMPDR | fig|99287.1.peg.2843. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P17845. |
| OMA | ITTTQWQ. |
Enzyme and pathway databases | |
| BioCyc | STYP99287:STM2947-MON. |
| BRENDA | 1.8.1.2. 2. |
Family and domain databases | |
| HAMAP | MF_01540. [Tree] |
| InterPro | IPR011786. CysI. IPR005117. NiRdtase/SiRdtase_haem-b_fer. IPR006067. NO2/SO3_Rdtase_4Fe4S. IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS. [Graphical view] |
| Pfam | PF01077. NIR_SIR. 1 hit. PF03460. NIR_SIR_ferr. 2 hits. [Graphical view] |
| PRINTS | PR00397. SIROHAEM. |
| TIGRFAMs | TIGR02041. CysI. 1 hit. |
| PROSITE | PS00365. NIR_SIR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CYSI_SALTY | ||||||||
| Accession | Primary (citable) accession number: P17845 | ||||||||
| 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 |

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