ID   CYC5_AZOVI              Reviewed;          83 AA.
AC   P11732;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Cytochrome c5;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=2993632; DOI=10.1016/0022-2836(85)90380-8;
RA   Carter D.C., Melis K.A., O'Donnell S.E., Burgess B.K., Furey W.F. Jr.,
RA   Wang B.-C., Stout C.D.;
RT   "Crystal structure of Azotobacter cytochrome c5 at 2.5-A resolution.";
RL   J. Mol. Biol. 184:279-295(1985).
CC   -!- FUNCTION: It is unreactive with cytochrome c reductase or oxidase.
CC   -!- SUBUNIT: Homodimer.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
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DR   PDB; 1CC5; X-ray; 2.50 A; A=1-83.
DR   PDBsum; 1CC5; -.
DR   AlphaFoldDB; P11732; -.
DR   SMR; P11732; -.
DR   EvolutionaryTrace; P11732; -.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002323; Cyt_CIE.
DR   PANTHER; PTHR40942; PTHR40942; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PRINTS; PR00607; CYTCHROMECIE.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Heme; Iron; Metal-binding; Transport.
FT   CHAIN           1..83
FT                   /note="Cytochrome c5"
FT                   /id="PRO_0000108366"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   BINDING         59
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   DISULFID        65..68
FT   HELIX           8..13
FT                   /evidence="ECO:0007829|PDB:1CC5"
FT   HELIX           16..19
FT                   /evidence="ECO:0007829|PDB:1CC5"
FT   TURN            20..25
FT                   /evidence="ECO:0007829|PDB:1CC5"
FT   HELIX           32..41
FT                   /evidence="ECO:0007829|PDB:1CC5"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:1CC5"
FT   HELIX           49..54
FT                   /evidence="ECO:0007829|PDB:1CC5"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:1CC5"
FT   HELIX           70..81
FT                   /evidence="ECO:0007829|PDB:1CC5"
SQ   SEQUENCE   83 AA;  8178 MW;  0B00EB8DBECC2691 CRC64;
     GGGARSGDDV VAKYCNACHG TGLLNAPKVG DSAAWKTRAD AKGGLDGLLA QSLSGLNAMP
     PKGTCADCSD DELKAAIGKM SGL