ID   CYC5_AZOVI     STANDARD;      PRT;    83 AA.
AC   P11732;
DT   01-OCT-1989 (Rel. 12, Created)
DT   01-OCT-1989 (Rel. 12, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   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   MEDLINE=85293097; PubMed=2993632;
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 group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
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DR   PDB; 1CC5; X-ray; @=1-83.
DR   InterPro; IPR002323; Cyt_CIE.
DR   InterPro; IPR000345; CytC_heme_BS.
DR   InterPro; IPR009056; Cytochrome_c.
DR   PRINTS; PR00607; CYTCHROMECIE.
DR   PROSITE; PS51007; CYTC; 1.
KW   3D-structure; Direct protein sequencing; Electron transport; Heme.
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        59     59       Iron (heme axial ligand).
FT   DISULFID     65     68
FT   HELIX         8     13
FT   TURN         14     15
FT   HELIX        16     19
FT   TURN         20     25
FT   TURN         29     30
FT   HELIX        32     42
FT   TURN         43     43
FT   TURN         46     48
FT   HELIX        49     54
FT   STRAND       56     56
FT   TURN         57     58
FT   STRAND       59     59
FT   HELIX        70     81
SQ   SEQUENCE   83 AA;  8178 MW;  0B00EB8DBECC2691 CRC64;
     GGGARSGDDV VAKYCNACHG TGLLNAPKVG DSAAWKTRAD AKGGLDGLLA QSLSGLNAMP
     PKGTCADCSD DELKAAIGKM SGL
//