Q06473 (COX1_SYNY3) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 105.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cytochrome c oxidase subunit 1 EC=1.9.3.1 Alternative name(s): Cytochrome aa3 subunit 1 Cytochrome c oxidase polypeptide I Oxidase aa(3) subunit 1 | ||||
| Gene names |
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| Organism | Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 1111708 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › ![]() |
Protein attributes
| Sequence length | 551 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. |
| Catalytic activity | 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O. |
| Cofactor | Binds 1 copper B ion per subunit. Binds 2 heme groups per subunit. |
| Pathway | |
| Subcellular location | |
| Sequence similarities | Belongs to the heme-copper respiratory oxidase family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 551 | 551 | Cytochrome c oxidase subunit 1 | PRO_0000183461 | |||||||
Regions | |||||||||||
| Transmembrane | 29 – 49 | 21 | Helical; Potential | ||||||||
| Transmembrane | 79 – 99 | 21 | Helical; Potential | ||||||||
| Transmembrane | 113 – 133 | 21 | Helical; Potential | ||||||||
| Transmembrane | 156 – 176 | 21 | Helical; Potential | ||||||||
| Transmembrane | 205 – 225 | 21 | Helical; Potential | ||||||||
| Transmembrane | 245 – 265 | 21 | Helical; Potential | ||||||||
| Transmembrane | 283 – 303 | 21 | Helical; Potential | ||||||||
| Transmembrane | 313 – 333 | 21 | Helical; Potential | ||||||||
| Transmembrane | 348 – 368 | 21 | Helical; Potential | ||||||||
| Transmembrane | 382 – 402 | 21 | Helical; Potential | ||||||||
| Transmembrane | 424 – 444 | 21 | Helical; Potential | ||||||||
| Transmembrane | 466 – 486 | 21 | Helical; Potential | ||||||||
Sites | |||||||||||
| Metal binding | 76 | 1 | Iron (heme A axial ligand) Probable | ||||||||
| Metal binding | 251 | 1 | Copper B Probable | ||||||||
| Metal binding | 255 | 1 | Copper B Probable | ||||||||
| Metal binding | 300 | 1 | Copper B Probable | ||||||||
| Metal binding | 301 | 1 | Copper B Probable | ||||||||
| Metal binding | 386 | 1 | Iron (heme A3 axial ligand) Probable | ||||||||
| Metal binding | 388 | 1 | Iron (heme A axial ligand) Probable | ||||||||
Amino acid modifications | |||||||||||
| Cross-link | 251 ↔ 255 | 1'-histidyl-3'-tyrosine (His-Tyr) By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 191 – 197 | 7 | SMPLFCW → VCPCFAG in CAA37777. Ref.1 | ||||||||
| Sequence conflict | 212 | 1 | V → L in CAA37777. Ref.1 | ||||||||
| Sequence conflict | 233 | 1 | P → R in CAA37777. Ref.1 | ||||||||
| Sequence conflict | 305 | 1 | S → H in CAA37777. Ref.1 | ||||||||
| Sequence conflict | 329 – 336 | 8 | KIFSWCGT → QNFQLVRY in CAA37777. Ref.1 | ||||||||
| Sequence conflict | 432 | 1 | N → D in CAA37777. Ref.1 | ||||||||
| Sequence conflict | 520 – 551 | 32 | VLWCG…DAAGS → CSGVVPTILVLTRS in CAA37777. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of a cta/CDE operon-like genomic region encoding subunits I-III of the cytochrome c oxidase of the cyanobacterium Synechocystis PCC 6803." Alge D., Peschek G.A. Biochem. Mol. Biol. Int. 29:511-525(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S.DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X53746 Genomic DNA. Translation: CAA37777.1. BA000022 Genomic DNA. Translation: BAA17289.1. |
| PIR | S77442. |
| RefSeq | NP_440609.1. NC_000911.1. YP_005650667.1. NC_017277.1. YP_007450492.1. NC_020286.1. |
3D structure databases | |
| ProteinModelPortal | Q06473. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 1148.slr1137. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAA17289; BAA17289; BAA17289. |
| GeneID | 12256359. 14616142. 953912. |
| KEGG | syn:slr1137. syy:SYNGTS_0714. |
| PATRIC | 23838412. VBISynSp132158_0773. |
Phylogenomic databases | |
| eggNOG | COG0843. |
| HOGENOM | HOG000085274. |
| KO | K02274. |
| OMA | TVTMVLT. |
| ProtClustDB | CLSK892772. |
Enzyme and pathway databases | |
| UniPathway | UPA00705. |
Family and domain databases | |
| Gene3D | 1.20.210.10. 1 hit. |
| InterPro | IPR000883. Cyt_c_Oxase_su1. IPR023615. Cyt_c_Oxase_su1_BS. IPR023616. Cyt_c_Oxase_su1_dom. IPR014241. Cyt_c_oxidase_su1_bac. [Graphical view] |
| PANTHER | PTHR10422. PTHR10422. 1 hit. |
| Pfam | PF00115. COX1. 1 hit. [Graphical view] |
| PRINTS | PR01165. CYCOXIDASEI. |
| SUPFAM | SSF81442. COX1. 1 hit. |
| TIGRFAMs | TIGR02891. CtaD_CoxA. 1 hit. |
| PROSITE | PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | COX1_SYNY3 | ||||||||
| Accession | Primary (citable) accession number: Q06473 Secondary accession number(s): P73261 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Synechocystis PCC 6803 Synechocystis (strain PCC 6803): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
