Reviewed,
UniProtKB/Swiss-Prot Q9JUD9 (CYSI_NEIMA)
Last modified
June 16, 2009.
Version 43.
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 | Neisseria meningitidis serogroup A [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 65699 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Protein attributes
| Sequence length | 589 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 – 589 | 589 | Sulfite reductase [NADPH] hemoprotein beta-component HAMAP MF_01540 | PRO_0000199901 | |||||
Sites | |||||||||
| Metal binding | 443 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 449 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 488 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 492 | 1 | Iron (siroheme axial ligand) By similarity | ||||||
| Metal binding | 492 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
Sequences
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References
| [1] | "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491." Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M., Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S. Barrell B.G.Nature 404:502-506(2000) [PubMed: 10761919] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Z2491 / Serogroup A / Serotype 4A. |
Cross-references
Sequence databases | |
|---|---|
| AL157959 Genomic DNA. Translation: CAM08535.1. | |
| PIR | D81905. |
| RefSeq | YP_002342716.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 7GEP based on UniProtKB P17846. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 907769. |
| GenomeReviews | Gene locus NMA1362 in contig AL157959_GR. |
| KEGG | nma:NMA1362. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9JUD9. |
| OMA | Q9JUD9. TRQAFQM. |
Enzyme and pathway databases | |
| BioCyc | NMEN122587:NMA1362-MON. |
| BRENDA | 1.8.1.2. 292829. |
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_NEIMA | ||||||||
| Accession | Primary (citable) accession number: Q9JUD9 Secondary accession number(s): A1IRY7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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