CY550_PARVE
ID CY550_PARVE Reviewed; 154 AA.
AC Q00499;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cytochrome c-550;
DE AltName: Full=Cytochrome c550;
DE Flags: Precursor;
GN Name=cyc;
OS Paracoccus versutus (Thiobacillus versutus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=34007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25364 / DSM 582 / JCM 20754 / NBRC 14567 / VKM B-2163;
RX PubMed=1339423; DOI=10.1128/jb.174.11.3707-3714.1992;
RA Ubbink M., van Beeumen J., Canters G.W.;
RT "Cytochrome c550 from Thiobacillus versutus: cloning, expression in
RT Escherichia coli, and purification of the heterologous holoprotein.";
RL J. Bacteriol. 174:3707-3714(1992).
RN [2]
RP PROTEIN SEQUENCE OF 37-42.
RX PubMed=8898909; DOI=10.1111/j.1432-1033.1996.0215t.x;
RA Spee J.H., Boersma M.G., Veeger C., Samyn B., Van Beeumen J., Warmerdam G.,
RA Canters G.W., Van Dongen W.M.A.M., Rietjens I.M.C.M.;
RT "The influence of the peptide chain on the kinetics and stability of
RT microperoxidases.";
RL Eur. J. Biochem. 241:215-220(1996).
CC -!- PTM: Binds 1 heme c group covalently per subunit.
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DR EMBL; X62808; CAA44627.1; -; Genomic_DNA.
DR PIR; S23630; S23630.
DR RefSeq; WP_036751693.1; NZ_QUMX01000057.1.
DR PDB; 2BGV; X-ray; 1.90 A; X=21-154.
DR PDB; 2BH4; X-ray; 1.55 A; X=21-154.
DR PDB; 2BH5; X-ray; 1.95 A; X=21-154.
DR PDBsum; 2BGV; -.
DR PDBsum; 2BH4; -.
DR PDBsum; 2BH5; -.
DR AlphaFoldDB; Q00499; -.
DR SMR; Q00499; -.
DR STRING; 34007.IT40_05935; -.
DR eggNOG; COG3474; Bacteria.
DR OrthoDB; 1853490at2; -.
DR EvolutionaryTrace; Q00499; -.
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 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Pyrrolidone carboxylic acid; Signal; Transport.
FT SIGNAL 1..20
FT CHAIN 21..149
FT /note="Cytochrome c-550"
FT /id="PRO_0000006525"
FT PROPEP 150..154
FT /evidence="ECO:0000250"
FT /id="PRO_0000006526"
FT BINDING 35
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 38
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 39
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 120
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 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:2BH4"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:2BH4"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:2BH4"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2BH4"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2BH4"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:2BH4"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:2BH4"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:2BH4"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:2BH4"
SQ SEQUENCE 154 AA; 16138 MW; C9ADE6C82B7E3625 CRC64;
MKISIYATLA ALSLALPAVA QEGDAAKGEK EFNKCKACHM VQAPDGTDIV KGGKTGPNLY
GVVGRKIASV EGFKYGDGIL EVAEKNPDMV WSEADLIEYV TDPKPWLVEK TGDSAAKTKM
TFKLGKNQAD VVAFLAQHSP DAGAEAAPAE GAAN
