CYC2_AFIMA
ID CYC2_AFIMA Reviewed; 124 AA.
AC P86321;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Cytochrome c2 {ECO:0000250|UniProtKB:P00083};
OS Afifella marina (Rhodobium marinum) (Rhodopseudomonas marina).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Afifellaceae; Afifella.
OX NCBI_TaxID=1080;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RX PubMed=20697695; DOI=10.1007/s00203-010-0608-2;
RA Meyer T., Van Driessche G., Ambler R., Kyndt J., Devreese B.,
RA Van Beeumen J., Cusanovich M.;
RT "Evidence from the structure and function of cytochromes c(2) that
RT nonsulfur purple bacterial photosynthesis followed the evolution of oxygen
RT respiration.";
RL Arch. Microbiol. 192:855-865(2010).
CC -!- FUNCTION: Cytochrome c2 is found mainly in purple, non-sulfur,
CC photosynthetic bacteria where it functions as the electron donor to the
CC oxidized bacteriochlorophyll in the photophosphorylation pathway.
CC However, it may also have a role in the respiratory chain and is found
CC in some non-photosynthetic bacteria. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:20697695}.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC {ECO:0000250|UniProtKB:P00083}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000255}.
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DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
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 Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Periplasm; Photosynthesis; Pyrrolidone carboxylic acid; Transport.
FT CHAIN 1..124
FT /note="Cytochrome c2"
FT /id="PRO_0000380710"
FT BINDING 16
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P00083,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 19
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P00083,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 20
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 /evidence="ECO:0000250|UniProtKB:P00083,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 85
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 /evidence="ECO:0000250|UniProtKB:P00083,
FT ECO:0000255|PROSITE-ProRule:PRU00433"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P0C0X8"
SQ SEQUENCE 124 AA; 13529 MW; 3F62B5A95DF51D3A CRC64;
QXGDLVAAGK KVYRQCHACH SVGEGAKNRV GPEQNNLFGR VAGSLPDFRY SKAMKSAGEN
GLVWTDKSLH EYLKNPRAYV PKTKMIFAGL KKPEDIDAVV AYLKTFDTDG MPDPDASTYT
PPNG
