ID   CYC6_SPIMA              Reviewed;          89 AA.
AC   P00118;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   24-MAR-2009, entry version 75.
DE   RecName: Full=Cytochrome c6;
DE   AltName: Full=Soluble cytochrome f;
DE   AltName: Full=Cytochrome c553;
DE   AltName: Full=Cytochrome c-553;
GN   Name=petJ;
OS   Spirulina maxima (Arthrospira maxima).
OC   Bacteria; Cyanobacteria; Oscillatoriales; Arthrospira.
OX   NCBI_TaxID=129910;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=75100362; PubMed=803642; DOI=10.1038/253285a0;
RA   Ambler R.P., Bartsch R.G.;
RT   "Amino acid sequence similarity between cytochrome f from a blue-green
RT   bacterium and algal chloroplasts.";
RL   Nature 253:285-288(1975).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   MEDLINE=21371781; PubMed=11478889; DOI=10.1021/bi002679p;
RA   Sawaya M.R., Krogmann D.W., Serag A., Ho K.K., Yeates T.O.,
RA   Kerfeld C.A.;
RT   "Structures of cytochrome c-549 and cytochrome c6 from the
RT   cyanobacterium Arthrospira maxima.";
RL   Biochemistry 40:9215-9225(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX   MEDLINE=22071407; PubMed=12077429; DOI=10.1107/S0907444902006534;
RA   Kerfeld C.A., Sawaya M.R., Krogmann D.W., Yeates T.O.;
RT   "Structure of cytochrome c6 from Arthrospira maxima: an assembly of 24
RT   subunits in a nearly symmetric shell.";
RL   Acta Crystallogr. D 58:1104-1110(2002).
CC   -!- FUNCTION: Functions as an electron carrier between membrane-bound
CC       cytochrome b6-f and photosystem I in oxygenic photosynthesis.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is +314 mV;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid lumen (Potential).
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.
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DR   PIR; A00110; CCSG6.
DR   PDB; 1F1F; X-ray; 2.70 A; A=1-89.
DR   PDB; 1KIB; X-ray; 3.50 A; A/B/C/D/E/F/G/H=1-89.
DR   PDBsum; 1F1F; -.
DR   PDBsum; 1KIB; -.
DR   GO; GO:0031977; C:thylakoid lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:HAMAP.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:HAMAP.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_00594; -; 1.
DR   InterPro; IPR003088; Cyt_c_I.
DR   InterPro; IPR008168; Cyt_C_IC.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00605; CYTCHROMECIC.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Photosynthesis; Thylakoid; Transport.
FT   CHAIN         1     89       Cytochrome c6.
FT                                /FTId=PRO_0000208686.
FT   METAL        18     18       Iron (heme axial ligand).
FT   METAL        62     62       Iron (heme axial ligand).
FT   BINDING      14     14       Heme (covalent).
FT   BINDING      17     17       Heme (covalent).
FT   HELIX         3     13
FT   HELIX        15     18
FT   HELIX        19     21
FT   STRAND       24     26
FT   HELIX        33     39
FT   TURN         41     45
FT   HELIX        47     57
FT   TURN         66     68
FT   HELIX        71     87
SQ   SEQUENCE   89 AA;  9236 MW;  4796D56B3EA8AF85 CRC64;
     GDVAAGASVF SANCAACHMG GRNVIVANKT LSKSDLAKYL KGFDDDAVAA VAYQVTNGKN
     AMPGFNGRLS PKQIEDVAAY VVDQAEKGW
//