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Database: UniProt
Entry: A0A3L9YZ21_9FLAO
LinkDB: A0A3L9YZ21_9FLAO
Original site: A0A3L9YZ21_9FLAO 
ID   A0A3L9YZ21_9FLAO        Unreviewed;       353 AA.
AC   A0A3L9YZ21;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Cytochrome c peroxidase {ECO:0000313|EMBL:RMA65823.1};
GN   ORFNames=BXY75_0236 {ECO:0000313|EMBL:RMA65823.1};
OS   Ulvibacter antarcticus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Ulvibacter.
OX   NCBI_TaxID=442714 {ECO:0000313|EMBL:RMA65823.1, ECO:0000313|Proteomes:UP000271339};
RN   [1] {ECO:0000313|EMBL:RMA65823.1, ECO:0000313|Proteomes:UP000271339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23424 {ECO:0000313|EMBL:RMA65823.1,
RC   ECO:0000313|Proteomes:UP000271339};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-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:RMA65823.1}.
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DR   EMBL; REFC01000011; RMA65823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L9YZ21; -.
DR   OrthoDB; 9805202at2; -.
DR   Proteomes; UP000271339; 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   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.
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:RMA65823.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Peroxidase {ECO:0000313|EMBL:RMA65823.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271339};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          208..339
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         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         228
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         229
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   353 AA;  39179 MW;  1D17820AE934E432 CRC64;
     MRYGVLICLL LSIVFTSCKK DDEYIATPMP LSIPQLFAEK LSPPIIPGDN PQTREGIALG
     RKLFYDPILS GDGTQACASC HNPQNAFSDE RRFSIGIDGL EGNRNSMPLF NMAWNFSEDF
     FWDGRAKGLE NQALEPVTNP IEMHNTWEQA TVSLQATSDY PLLFSNAFGT ENISKELVVK
     AISQFTRTLI SSNSKFDKHL AGEAELTTSE ANGLAVFLDE SRGDCFHCHG DPNTPIWTDN
     TFHNNGLDET ITDRGLGAFT GDPRDFGLFK SPSLRNLAFT APYMHDGRFQ TLDEVINHYS
     EGLVYSETID PLMKTISEGG VHLSENDKAD LKAFLLSLSD PSFINNPDFQ DPN
//
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