CY550_PARDE
ID CY550_PARDE Reviewed; 155 AA.
AC P00096;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cytochrome c-550;
DE AltName: Full=Cytochrome C2;
DE AltName: Full=Cytochrome c550;
DE Flags: Precursor;
GN Name=cycA;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Pd 1222;
RX PubMed=2155830; DOI=10.1016/0014-5793(90)80609-m;
RA Raitio M., Pispa J.M., Metso T., Saraste M.;
RT "Are there isoenzymes of cytochrome c oxidase in Paracoccus
RT denitrificans?";
RL FEBS Lett. 261:431-435(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Pd 1222;
RX PubMed=2153663; DOI=10.1128/jb.172.2.986-996.1990;
RA van Spanning R.J.M., Wansell C., Harms N., Oltmann L.F., Stouthamer A.H.;
RT "Mutagenesis of the gene encoding cytochrome c550 of Paracoccus
RT denitrificans and analysis of the resultant physiological effects.";
RL J. Bacteriol. 172:986-996(1990).
RN [3]
RP ERRATUM OF PUBMED:2153663.
RX PubMed=2160949; DOI=10.1128/jb.172.6.3534.1990;
RA van Spanning R.J.M., Wansell C., Harms N., Oltmann L.F., Stouthamer A.H.;
RL J. Bacteriol. 172:3534-3534(1990).
RN [4]
RP PROTEIN SEQUENCE OF 21-149, AND PYROGLUTAMATE FORMATION AT GLN-21.
RC STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX PubMed=6270339; DOI=10.1016/0022-2836(81)90445-9;
RA Ambler R.P., Meyer T.E., Kamen M.D., Schichman S.A., Sawyer L.;
RT "A reassessment of the structure of Paracoccus cytochrome c-550.";
RL J. Mol. Biol. 147:351-356(1981).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RX PubMed=180013; DOI=10.2210/pdb155c/pdb;
RA Timkovich R., Dickerson R.E.;
RT "The structure of Paracoccus denitrificans cytochrome c550.";
RL J. Biol. Chem. 251:4033-4046(1976).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=8179333; DOI=10.1006/abbi.1994.1193;
RA Benning M.M., Meyer T.E., Holden H.M.;
RT "X-ray structure of the cytochrome c2 isolated from Paracoccus
RT denitrificans refined to 1.7-A resolution.";
RL Arch. Biochem. Biophys. 310:460-466(1994).
CC -!- PTM: Binds 1 heme c group covalently per subunit.
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DR EMBL; Y07533; CAA68820.1; -; Genomic_DNA.
DR EMBL; M27304; AAA88364.1; -; Genomic_DNA.
DR PIR; S08269; CCPC50.
DR RefSeq; WP_011748227.1; NZ_PPGA01000019.1.
DR PDB; 155C; X-ray; 2.50 A; A=23-142.
DR PDB; 1COT; X-ray; 1.70 A; A=21-149.
DR PDBsum; 155C; -.
DR PDBsum; 1COT; -.
DR AlphaFoldDB; P00096; -.
DR SMR; P00096; -.
DR TCDB; 3.D.4.6.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR OMA; MEAGMEW; -.
DR EvolutionaryTrace; P00096; -.
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 /evidence="ECO:0000269|PubMed:6270339"
FT CHAIN 21..149
FT /note="Cytochrome c-550"
FT /id="PRO_0000006523"
FT PROPEP 150..155
FT /id="PRO_0000006524"
FT BINDING 35
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:180013"
FT BINDING 38
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433,
FT ECO:0000269|PubMed:180013"
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 ECO:0000269|PubMed:180013"
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 ECO:0000269|PubMed:180013"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:6270339"
FT VARIANT 149
FT /note="Missing (in 50% of the molecules)"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:1COT"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1COT"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:1COT"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:155C"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1COT"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1COT"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:155C"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:1COT"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:1COT"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:1COT"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:1COT"
SQ SEQUENCE 155 AA; 16398 MW; CB003CA423879B03 CRC64;
MKISIYATLA AITLALPAAA QDGDAAKGEK EFNKCKACHM IQAPDGTDII KGGKTGPNLY
GVVGRKIASE EGFKYGEGIL EVAEKNPDLT WTEADLIEYV TDPKPWLVKM TDDKGAKTKM
TFKMGKNQAD VVAFLAQNSP DAGGDGEAAA EGESN
