ID A0A1Q4F7I1_9SPHI Unreviewed; 355 AA.
AC A0A1Q4F7I1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Cytochrome-c peroxidase {ECO:0000313|EMBL:OJY88785.1};
GN ORFNames=BGP14_05805 {ECO:0000313|EMBL:OJY88785.1};
OS Sphingobacteriales bacterium 44-15.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895837 {ECO:0000313|EMBL:OJY88785.1, ECO:0000313|Proteomes:UP000186250};
RN [1] {ECO:0000313|EMBL:OJY88785.1, ECO:0000313|Proteomes:UP000186250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44-15 {ECO:0000313|EMBL:OJY88785.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR000294-1};
CC Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-1};
CC -!- PTM: Binds 2 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000294-
CC 1}.
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:OJY88785.1}.
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DR EMBL; MKWG01000015; OJY88785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4F7I1; -.
DR STRING; 1895837.BGP14_05805; -.
DR Proteomes; UP000186250; 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; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR InterPro; IPR026259; MauG/Cytc_peroxidase.
DR PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR PANTHER; PTHR30600:SF10; METHYLAMINE UTILIZATION PROTEIN; 1.
DR Pfam; PF03150; CCP_MauG; 1.
DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
PE 4: Predicted;
KW Heme {ECO:0000256|PIRSR:PIRSR000294-1};
KW Iron {ECO:0000256|PIRSR:PIRSR000294-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000294-2};
KW Oxidoreductase {ECO:0000313|EMBL:OJY88785.1};
KW Peroxidase {ECO:0000313|EMBL:OJY88785.1}.
FT DOMAIN 57..205
FT /note="Di-haem cytochrome c peroxidase"
FT /evidence="ECO:0000259|Pfam:PF03150"
FT BINDING 79
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 82
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 83
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
FT BINDING 222
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 225
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 226
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-2"
SQ SEQUENCE 355 AA; 40369 MW; 22E08B91096D50D9 CRC64;
MKTLLTILSL VISLTLLVLL QLSFTSDNGN AHPMKQRIPE GFPRPVYDYR NNPLTREGFE
LGRKLFYDGR LSRDGYTACA SCHQQFAAFS DFQHVFSHGA DSRFTRRNAP PLFNLAWQKE
FHLDGAINHL ELQPLAPMTG QNEMNNTLDS IIARIKADAA YRKMFSSAFG SELVNTQRML
WALAQFTGNI VSADSKYDRV KKGKAAFNEW EQQGYLIFKE RCADCHTEPL FTDLKYHNIG
LAVDTFLNDF GRRDITGDKS DSLKFKTPSL RNISRTDPYM HDGRYWGLST AIDHWQTRSA
SDTTADALIL RGKPLEKMEV KYLVSFLHTL LDSSFLKDPM LADPVQGNMI HGPLQ
//
