CYC21_RHOPL
ID CYC21_RHOPL Reviewed; 114 AA.
AC P00090;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cytochrome c2;
GN Name=cycA;
OS Rhodopseudomonas palustris.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=1076;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 17001 / ATH 2.1.6 / DSM 123 / NBRC 100419;
RX PubMed=221822; DOI=10.1038/278659a0;
RA Ambler R.P., Daniel M., Hermoso J., Meyer T.E., Bartsch R.G., Kamen M.D.;
RT "Cytochrome c2 sequence variation among the recognised species of purple
RT nonsulphur photosynthetic bacteria.";
RL Nature 278:659-660(1979).
RN [2]
RP PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC STRAIN=ATCC 17001 / ATH 2.1.6 / DSM 123 / NBRC 100419;
RA Ambler R.P., Meyer T.E., Murray S.;
RL Submitted (DEC-1974) to the PIR data bank.
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.
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; B00086; CCRF2P.
DR AlphaFoldDB; P00090; -.
DR SMR; P00090; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProt.
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 Photosynthesis; Pyrrolidone carboxylic acid; Transport.
FT CHAIN 1..114
FT /note="Cytochrome c2"
FT /id="PRO_0000380714"
FT BINDING 13
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 16
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 17
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 93
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 MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 114 AA; 12208 MW; 13657331CC0D4464 CRC64;
QDAAKGEAVF KQCMTCHRAD KNMVGPALGG VVGRKAGTAA GFTYSPLNHN SGEAGLVWTQ
ENIIAYLPDP NAYLKKFLTD KGQADKATGS TKMTFKLAND QQRKDVAAYL ATLK