Reviewed,
UniProtKB/Swiss-Prot A8A3P4 (CYSI_ECOHS)
Last modified
June 16, 2009.
Version 11.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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 | Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 331112 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 570 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | This enzyme catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate By similarity. |
| Catalytic activity | H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP MF_01540 |
| Cofactor | Binds 1 siroheme per subunit By similarity. Binds 1 4Fe-4S cluster per subunit By similarity. |
| Subunit structure | Alpha(8)-beta4. The alpha component is a flavoprotein, the beta component is a hemoprotein By similarity. |
| 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 570 | 570 | Sulfite reductase [NADPH] hemoprotein beta-component HAMAP MF_01540 | PRO_1000068759 | |||||
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
| [1] | "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000802 Genomic DNA. Translation: ABV07148.1. | |
| RefSeq | YP_001459531.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5592257. |
| GenomeReviews | Gene locus EcHS_A2903 in contig CP000802_GR. |
| KEGG | ecx:EcHS_A2903. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | A8A3P4. ITTTQWQ. |
Family and domain databases | |
| HAMAP | MF_01540. [Tree] |
| InterPro | IPR011786. CysI. IPR006066. Nir_Si_BS. IPR006067. Nir_Sir_4Fe4S. IPR005117. NiRdtase/SiRdtase_haem-b_fer. [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_ECOHS | ||||||||
| Accession | Primary (citable) accession number: A8A3P4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


