(data stored in ACNUC7421 zone)

SWISSPROT: Q5LXC2_RUEPO

ID   Q5LXC2_RUEPO            Unreviewed;       349 AA.
AC   Q5LXC2;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   SubName: Full=Cytochrome c peroxidase {ECO:0000313|EMBL:AAV93648.1};
DE            EC=1.11.1.5 {ECO:0000313|EMBL:AAV93648.1};
GN   Name=ccpA {ECO:0000313|EMBL:AAV93648.1};
GN   OrderedLocusNames=SPO0330 {ECO:0000313|EMBL:AAV93648.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93648.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93648.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93648.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000294-2};
CC       Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-2};
CC   -!- PTM: Binds 2 heme groups per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000294-1}.
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DR   EMBL; CP000031; AAV93648.1; -; Genomic_DNA.
DR   RefSeq; WP_011046091.1; NC_003911.12.
DR   STRING; 246200.SPO0330; -.
DR   PeroxiBase; 5055; SpoDiHCcP.
DR   EnsemblBacteria; AAV93648; AAV93648; SPO0330.
DR   KEGG; sil:SPO0330; -.
DR   eggNOG; ENOG4105CA0; Bacteria.
DR   eggNOG; COG1858; LUCA.
DR   HOGENOM; HOG000173945; -.
DR   KO; K00428; -.
DR   OMA; EMGSHDW; -.
DR   OrthoDB; 52724at2; -.
DR   BioCyc; RPOM246200:G1G48-337-MONOMER; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0004130; F:cytochrome-c peroxidase activity; ISS:TIGR.
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; -; 2.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR   InterPro; IPR026259; MauG/Cytc_peroxidase.
DR   Pfam; PF03150; CCP_MauG; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR   SUPFAM; SSF46626; SSF46626; 2.
DR   PROSITE; PS51007; CYTC; 2.
PE   4: Predicted;
DR   PRODOM; Q5LXC2.
DR   SWISS-2DPAGE; Q5LXC2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Heme {ECO:0000256|PIRSR:PIRSR000294-1, ECO:0000256|PROSITE-
KW   ProRule:PRU00433};
KW   Iron {ECO:0000256|PIRSR:PIRSR000294-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000294-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Oxidoreductase {ECO:0000313|EMBL:AAV93648.1};
KW   Peroxidase {ECO:0000313|EMBL:AAV93648.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    349       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5004259943.
FT   DOMAIN       52    163       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   DOMAIN      205    322       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
FT   METAL        78     78       Iron (heme 1 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000294-2}.
FT   METAL        94     94       Iron (heme 1 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000294-2}.
FT   METAL       223    223       Iron (heme 2 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000294-2}.
FT   METAL       297    297       Iron (heme 2 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000294-2}.
FT   BINDING      74     74       Heme 1 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000294-1}.
FT   BINDING      77     77       Heme 1 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000294-1}.
FT   BINDING     219    219       Heme 2 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000294-1}.
FT   BINDING     222    222       Heme 2 (covalent). {ECO:0000256|PIRSR:
FT                                PIRSR000294-1}.
SQ   SEQUENCE   349 AA;  36854 MW;  CD8524A38B0F75FD CRC64;
     MSPKSLFSFS LTALSCTAGL AAANPLREQA LELFQPLPST VPAVKDNPIT PEKIDLGKAL
     FFDPRMSASG VFSCNSCHNL ATGGDDNLET SIGHGWQKGP RNAPTVLNAV FNAAQFWDGR
     APDLAEQAKG PVQAGVEMAN TPGQVVATLN SMPEYVAWFQ AAFPDQPDPV SFDSFAKAIE
     AYEATLITPA PFDAWLNGDD AALSGEQKQG LSLFIDAGCA SCHGGVNLGG QDYYPFGLVE
     TPDAEVLPSG DKGRFAVTAT EDDEYVFRAA PLRNIAVTAP YFHSGKVWEL EAAVSIMASS
     QLGADLSEEE TAAITAFLHS LTGEVPQVVY PVLPAETSGT PRPDGAVQR
//

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