ID Q5FPR9_GLUOX Unreviewed; 492 AA.
AC Q5FPR9;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Cytochrome c peroxidase {ECO:0000313|EMBL:AAW61627.1};
DE EC=1.11.1.5 {ECO:0000313|EMBL:AAW61627.1};
GN OrderedLocusNames=GOX1889 {ECO:0000313|EMBL:AAW61627.1};
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW61627.1, ECO:0000313|Proteomes:UP000006375};
RN [1] {ECO:0000313|EMBL:AAW61627.1, ECO:0000313|Proteomes:UP000006375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H {ECO:0000313|EMBL:AAW61627.1,
RC ECO:0000313|Proteomes:UP000006375};
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000009; AAW61627.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5FPR9; -.
DR STRING; 290633.GOX1889; -.
DR PeroxiBase; 5080; GoDiHCcP.
DR KEGG; gox:GOX1889; -.
DR eggNOG; COG1858; Bacteria.
DR HOGENOM; CLU_034652_2_0_5; -.
DR Proteomes; UP000006375; Chromosome.
DR GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:UniProtKB-EC.
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; Cytochrome c-like domain; 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; IPR025992; Haem-bd.
DR PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR PANTHER; PTHR30600:SF7; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR Pfam; PF03150; CCP_MauG; 1.
DR Pfam; PF14376; Haem_bd; 1.
DR SMART; SM01235; Haem_bd; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Oxidoreductase {ECO:0000313|EMBL:AAW61627.1};
KW Peroxidase {ECO:0000313|EMBL:AAW61627.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006375}.
FT DOMAIN 190..318
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 343..464
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT REGION 471..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 53965 MW; DA15683D77C7D640 CRC64;
MVRSSTITKG IAGLVALGVV AWGGTVTYLE HFDHAGAPQL PASSPTRQDP TAMAAFAALR
EVRCDYCHTQ NVELPFYFKL PLANQIMKRD LVQGQRHFEY APVLTALQDG KPPSVEQLSR
IEEVITQNRM PPSAYLLMHP HAHLDEKQRA DILKWVREQR ERYYATPGVA AQFRGEPIQP
IPESVDVNWK KAELGRALFF DKGLSGDGTL NCASCHGLNK GGVDNLTTAT GIGGQKGPIN
VPTVYNAVFS MAQFWNGRAK DLAEQAAGPV MNPLEMGSHD WNTVADHVRS TPGYAEQFTA
AFGSEQIDKD TITAAIAEYE KTLITPDSRF DLYLKGDAKA ITAPEKRGYE RFKEIGCSGC
HSGLAVGGDA YEILGLEGPY FENRHTKLTD ADEGRMAVTH KEGDRERFKV PNLRNVELTG
PWLHDGSATT LEQVVREMAR YETPDHDIAD QDVTDIVAFL KTLTGKYEGI PLKDVPADQP
LQAPVSGSGS SN
//
