ID CYC22_MAGML Reviewed; 97 AA.
AC P00088;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Cytochrome c2 iso-2;
OS Magnetospirillum molischianum (Rhodospirillum molischianum).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1083;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 14031 / DSM 120 / KCTC 15609 / LMG 4354 / NCIMB 9957 / NTHC
RC 131;
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.
RA Ambler R.P.;
RL Submitted (JUN-1977) 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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC -!- CAUTION: Approximately 30% of the residue corresponding to Tyr-62 is
CC present as Phe, suggesting there may be more than 1 gene for this
CC protein in this organism. {ECO:0000305}.
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DR PIR; A00080; CCQFM2.
DR AlphaFoldDB; P00088; -.
DR SMR; P00088; -.
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; Cytochrome c-like domain; 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; CYTOCHROME C; 1.
DR PANTHER; PTHR11961:SF12; CYTOCHROME C; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Photosynthesis; Transport.
FT CHAIN 1..97
FT /note="Cytochrome c2 iso-2"
FT /id="PRO_0000108352"
FT BINDING 10
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 13
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 14
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:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 75
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:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 97 AA; 10222 MW; 5A1CBC489B0DBFB6 CRC64;
ADAPAGFTLC KACHSVEAGK NGVGPSLAGV YGRKAGTISG FKFSDPHIKS GLTWDEPTLT
KYLADPKTVI PGNKMVFAGL KNPDDVKAVI EYLKTLK
//
