Tag | Content |
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CPLM ID | CPLM-003648 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cytochrome c2 |
Protein Synonyms/Alias | |
Gene Name | cycA |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rhodospirillum rubrum |
NCBI Taxa ID | 1085 |
Lysine Modification | Position | Peptide | Type | References |
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109 | ENVIAYLKTLK**** | acetylation | [1] | 112 | IAYLKTLK******* | acetylation | [1] |
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Reference | [1] Binding of cytochrome c2 to the isolated reaction center of Rhodospirillum rubrum involves the "backside" of cytochrome c2. Rieder R, Wiemken V, Bachofen R, Bosshard HR. Biochem Biophys Res Commun. 1985 Apr 16;128(1):120-6. [ PMID: 2985069] |
Functional Description | Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria. |
Sequence Annotation | METAL 18 18 Iron (heme axial ligand). METAL 91 91 Iron (heme axial ligand). BINDING 14 14 Heme (covalent). BINDING 17 17 Heme (covalent). |
Keyword | 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding; Photosynthesis; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 112 AA |
Protein Sequence | EGDAAAGEKV SKKCLACHTF DQGGANKVGP NLFGVFENTA AHKDNYAYSE SYTEMKAKGL 60 TWTEANLAAY VKNPKAFVLE KSGDPKAKSK MTFKLTKDDE IENVIAYLKT LK 112 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |