ID A0A0P6WFH0_9SPHN Unreviewed; 365 AA.
AC A0A0P6WFH0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Cytochrome C peroxidase {ECO:0000313|EMBL:KPL66775.1};
GN ORFNames=SZ64_00845 {ECO:0000313|EMBL:KPL66775.1};
OS Erythrobacter sp. SG61-1L.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL66775.1, ECO:0000313|Proteomes:UP000049978};
RN [1] {ECO:0000313|EMBL:KPL66775.1, ECO:0000313|Proteomes:UP000049978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG61-1L {ECO:0000313|EMBL:KPL66775.1,
RC ECO:0000313|Proteomes:UP000049978};
RA Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA Pandey G.;
RT "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL Appl. Environ. Microbiol. 0:0-0(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPL66775.1}.
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DR EMBL; JXQC01000003; KPL66775.1; -; Genomic_DNA.
DR RefSeq; WP_054529098.1; NZ_JXQC01000003.1.
DR AlphaFoldDB; A0A0P6WFH0; -.
DR STRING; 1603897.SZ64_00845; -.
DR PATRIC; fig|1603897.4.peg.48; -.
DR Proteomes; UP000049978; Unassembled WGS sequence.
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 GO; GO:0004601; F:peroxidase activity; 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 PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR Pfam; PF03150; CCP_MauG; 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:KPL66775.1};
KW Peroxidase {ECO:0000313|EMBL:KPL66775.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000049978};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..365
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006132334"
FT DOMAIN 77..178
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 218..365
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 365 AA; 40378 MW; 8552E571B2ECDA29 CRC64;
MNSRHGKWIR LASLLGAGLL LAGAAGEPEP VPPASELRML YAGKPQDWPR PTLHDGAVFE
EFGPLPARPT LEGRDAQMAQ LGEELFNERR LSGSGQFACA SCHNRELGMG DGLRTAFGHD
RQRGSRNSQQ IFTAGLMHEW FWDGRAATLE DQAIAAMTNP IEMAGEPARI EEWINSDDHY
REKFAALQGE GRITLQQIVG AIAAFQKSLR PPRSKWDRML EDGPQVFTDE ELTGLHLFRT
KAGCANCHNG PLFSDQRYHN IGLTYYGRKY EDLGRYLLTG KAEDVGRFRT PSLRAAGRTG
PYMHNGLFPS LLGIVNLYNA GGVTEKREAS LADPAAPRPA LDPLVKELNL TAEERRALVA
FLETL
//
