ID   CY550_PARPN             Reviewed;         134 AA.
AC   P80288;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cytochrome c-550;
DE   AltName: Full=Cytochrome c550;
OS   Paracoccus pantotrophus (Thiosphaera pantotropha).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=82367;
RN   [1]
RP   PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC   STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 / NCCB
RC   82005 / GB17;
RX   PubMed=7508392; DOI=10.1111/j.1432-1033.1994.tb19974.x;
RA   Samyn B., Berks B.C., Page M.L.D., Ferguson S.J., van Beeumen J.J.;
RT   "Characterisation and amino acid sequence of cytochrome c-550 from
RT   Thiosphaera pantotropha.";
RL   Eur. J. Biochem. 219:585-594(1994).
CC   -!- FUNCTION: Electron donor for nitrous-oxide reductase.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is about +265 mV.;
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
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DR   PIR; S41108; S41108.
DR   AlphaFoldDB; P80288; -.
DR   SMR; P80288; -.
DR   STRING; 935565.JAEM01000045_gene646; -.
DR   eggNOG; COG3474; Bacteria.
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   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   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   Pyrrolidone carboxylic acid; Transport.
FT   CHAIN           1..134
FT                   /note="Cytochrome c-550"
FT                   /id="PRO_0000108386"
FT   BINDING         15
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         18
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT   BINDING         19
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         100
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   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:7508392"
SQ   SEQUENCE   134 AA;  14201 MW;  19BFCAB4FC43AE93 CRC64;
     QEGDAAKGEK EFNKCKACHM VQAPDGTDIV KGGKTGPNLY GVVGRKIASE EGFKYGDGIL
     EVAEKNPDLV WTEADLIEYV TDPKPWLVEK TGDSAAKTKM TFKLGKNQAD VVAFLAQNSP
     DAGAEAAPAE DAAD