Reviewed,
UniProtKB/Swiss-Prot Q8X7U1 (CYSJ_ECO57)
Last modified
November 25, 2008.
Version 45.
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] flavoprotein alpha-component Short name=SIR-FP EC=1.8.1.2 | ||||
| Gene names |
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| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 83334 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 599 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 | Catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavo-protein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component By similarity. |
| Catalytic activity | H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH. |
| Cofactor | Binds 1 FAD per subunit By similarity. Binds 1 FMN per subunit By similarity. |
| Subunit structure | Alpha(8)-beta(8). The alpha component is a flavoprotein, the beta component is a hemoprotein By similarity. |
| Sequence similarities | Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain. |
Ontologies
Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Cysteine biosynthesis Electron transport Transport |
| Ligand | FAD FMN Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | cysteine biosynthetic process Inferred from electronic annotation. Source: InterPro electron transport chainInferred from electronic annotation. Source: UniProtKB-KW sulfate assimilationInferred from electronic annotation. Source: HAMAP transportInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | FMN binding Inferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro iron ion 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 – 599 | 598 | Sulfite reductase [NADPH] flavoprotein alpha-component | PRO_0000199924 | |||||
Regions | |||||||||
| Domain | 64 – 202 | 139 | Flavodoxin-like | ||||||
| Domain | 234 – 448 | 215 | FAD-binding FR-type | ||||||
| Nucleotide binding | 70 – 74 | 5 | FMN By similarity | ||||||
| Nucleotide binding | 150 – 181 | 32 | FMN By similarity | ||||||
| Nucleotide binding | 236 – 288 | 53 | FAD By similarity | ||||||
| Nucleotide binding | 472 – 599 | 128 | NADP By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| AE005174 Genomic DNA. Translation: AAG57872.1. BA000007 Genomic DNA. Translation: BAB37042.1. | |
| PIR | C91081. D85926. |
| RefSeq | NP_289314.1. NP_311646.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1DDG based on UniProtKB P38038. |
| SMR | Q8X7U1. Positions 63-208, 64-209, 225-598, 226-599. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 914659. 959221. |
| GenomeReviews | Gene locus ECs3619 in contig BA000007_GR. Gene locus Z4074 in contig AE005174_GR. |
| KEGG | ece:Z4074. ecs:ECs3619. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8X7U1. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS3619-MON. |
Family and domain databases | |
| HAMAP | MF_01541. [Tree] |
| InterPro | IPR010199. CysJ. IPR003097. FAD-binding_1. IPR001094. Flavdoxin_like. IPR008254. Flavodoxin/NO_synth. IPR001709. FPN_cyt_redctse. IPR001433. OxRdtase_FAD/NAD_bd. [Graphical view] |
| Pfam | PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. [Graphical view] |
| PRINTS | PR00369. FLAVODOXIN. PR00371. FPNCR. |
| TIGRFAMs | TIGR01931. cysJ. 1 hit. |
| PROSITE | PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CYSJ_ECO57 | ||||||||
| Accession | Primary (citable) accession number: Q8X7U1 Secondary accession number(s): Q7AB91 | ||||||||
| 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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