ID A0A2V4BTZ7_9FLAO Unreviewed; 352 AA.
AC A0A2V4BTZ7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Cytochrome-c peroxidase {ECO:0000313|EMBL:PXY42127.1};
GN ORFNames=DMB65_02510 {ECO:0000313|EMBL:PXY42127.1};
OS Flavobacterium cheongpyeongense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2212651 {ECO:0000313|EMBL:PXY42127.1, ECO:0000313|Proteomes:UP000247903};
RN [1] {ECO:0000313|EMBL:PXY42127.1, ECO:0000313|Proteomes:UP000247903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC34759 {ECO:0000313|EMBL:PXY42127.1,
RC ECO:0000313|Proteomes:UP000247903};
RA Joung Y., Cho J.;
RT "Flavobacterium sp. strain IMCC34759, incomplete genome.";
RL Submitted (MAY-2018) 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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:PXY42127.1}.
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DR EMBL; QJHK01000002; PXY42127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V4BTZ7; -.
DR OrthoDB; 9805202at2; -.
DR Proteomes; UP000247903; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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 InterPro; IPR026259; MauG/Cytc_peroxidase.
DR PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR Pfam; PF03150; CCP_MauG; 1.
DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000294-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000294-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000294-2};
KW Oxidoreductase {ECO:0000313|EMBL:PXY42127.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Peroxidase {ECO:0000313|EMBL:PXY42127.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000247903};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 55..188
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 77
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 80
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 81
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 352 AA; 39353 MW; 37D52CCB1DE29FDF CRC64;
MLNRIIKLGS ITGLAFLSFS CNDFDDNYQE PLPLVLVPDN FPEFVDSKTN PLTSDGVLLG
KKLFFDKRLS GNNKVSCATC HQQSLAFSDG FALTKQGISG NALERNSPAL INLAWANNGL
FWDGGSTNLE SQAFAPLAHV DEMHQNLDEL LDELKEDTDY PKMFQRAFGK TINQADIVKA
IAQFERTLIS SNSRYDKYVR GESGGILDQE ELEGLKLAEQ FCFSCHAGSL MTDNLYHNNG
IDNDFTDDSE LMMRRGRARI TGSSEDLGKF RTPTLRNIEK TGPYMHDGRL GTLEAVLEHY
SNSVLFSSTL DPLLRKNGNL GIPLSETEKK QLIAFLKTLT DYAYINDKRF SE
//
