ID   CYC2_RHOGL              Reviewed;         106 AA.
AC   P00080;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Cytochrome c2;
OS   Rhodopila globiformis (Rhodopseudomonas globiformis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Rhodopila.
OX   NCBI_TaxID=1071;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2823792; DOI=10.1042/bj2460115;
RA   Ambler R.P., Meyer T.E., Cusanovich M.A., Kamen M.D.;
RT   "The amino acid sequence of the cytochrome c2 from the phototrophic
RT   bacterium Rhodopseudomonas globiformis.";
RL   Biochem. J. 246:115-120(1987).
RN   [2]
RP   PROTEIN SEQUENCE.
RA   Ambler R.P.;
RL   (In) Nichols J.M. (eds.);
RL   Abstracts of the 3rd international symposium on photosynthetic prokaryotes
RL   (Oxford), pp.E17-E17, Univ. Liverpool, Liverpool (1979).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX   PubMed=8809072; DOI=10.1006/abbi.1996.0400;
RA   Benning M.M., Meyer T.E., Holden H.M.;
RT   "Molecular structure of a high potential cytochrome c2 isolated from
RT   Rhodopila globiformis.";
RL   Arch. Biochem. Biophys. 333:338-348(1996).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is +450 mV.;
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   PIR; A32518; CCRF2G.
DR   PDB; 1HRO; X-ray; 2.20 A; A/B=1-106.
DR   PDBsum; 1HRO; -.
DR   AlphaFoldDB; P00080; -.
DR   SMR; P00080; -.
DR   EvolutionaryTrace; P00080; -.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   PANTHER; PTHR11961; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW   Metal-binding; Photosynthesis; Transport.
FT   CHAIN           1..106
FT                   /note="Cytochrome c2"
FT                   /id="PRO_0000108344"
FT   BINDING         19
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:2823792"
FT   BINDING         22
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT                   ECO:0000269|PubMed:2823792"
FT   BINDING         23
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         84
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   HELIX           8..15
FT                   /evidence="ECO:0007829|PDB:1HRO"
FT   TURN            16..18
FT                   /evidence="ECO:0007829|PDB:1HRO"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:1HRO"
FT   STRAND          30..33
FT                   /evidence="ECO:0007829|PDB:1HRO"
FT   HELIX           54..59
FT                   /evidence="ECO:0007829|PDB:1HRO"
FT   HELIX           65..73
FT                   /evidence="ECO:0007829|PDB:1HRO"
FT   HELIX           75..78
FT                   /evidence="ECO:0007829|PDB:1HRO"
FT   HELIX           92..102
FT                   /evidence="ECO:0007829|PDB:1HRO"
SQ   SEQUENCE   106 AA;  11610 MW;  703F12633400E519 CRC64;
     GSAPPGDPVE GKHLFHTICI LCHTDIKGRN KVGPSLYGVV GRHSGIEPGY NYSEANIKSG
     IVWTPDVLFK YIEHPQKIVP GTKMGYPGQP DPQKRADIIA YLETLK