ID A0A410UNW1_9BURK Unreviewed; 412 AA.
AC A0A410UNW1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Cytochrome-c peroxidase {ECO:0000313|EMBL:QAU33050.1};
GN ORFNames=EKL02_02030 {ECO:0000313|EMBL:QAU33050.1};
OS Janthinobacterium sp. 17J80-10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=2497863 {ECO:0000313|EMBL:QAU33050.1, ECO:0000313|Proteomes:UP000288813};
RN [1] {ECO:0000313|EMBL:QAU33050.1, ECO:0000313|Proteomes:UP000288813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17J80-10 {ECO:0000313|EMBL:QAU33050.1,
RC ECO:0000313|Proteomes:UP000288813};
RA Kim M., Maeng S., Sathiyaraj S.;
RT "genome sequence of Janthinobacteria sp. 17J80-10.";
RL Submitted (JAN-2019) 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}.
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DR EMBL; CP035311; QAU33050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410UNW1; -.
DR KEGG; jaj:EKL02_02030; -.
DR OrthoDB; 9805202at2; -.
DR Proteomes; UP000288813; Chromosome.
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; 3.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 2.
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:QAU33050.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Peroxidase {ECO:0000313|EMBL:QAU33050.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000288813};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..412
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018975062"
FT DOMAIN 64..175
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 252..405
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 86
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 89
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 90
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 267
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 270
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 271
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 412 AA; 44887 MW; 11CC572CC4D199A0 CRC64;
MHKLTGALLA AGSAALIAGA ALAGMPDYID GWTREEMAIL ASLSLKQLPP APKDPSNAYE
ALPAAVHLGE RIFADRRFSS NGAVSCASCH QPDKHFQDGA PLGLGVGTGS RRTMPVVAAD
HSPFLFWDGR KDSLWSQALG PLEDPAEHGG NRLAYAHLMQ AHYRKDYEAI FGAMPDLRHF
PKHASPAGTP LHKTTWNTMP ESARHDVSRI FANMGKALAA YQKTLQHGES RLDRYVEGVV
SGDQPSLQIL SPEEKHGLRI FIGKGNCITC HNGPLLTDQH FHNTGVPQRH EKTPDMGRYA
AIDKVMNDEF NCLGRYSDAK PELCEELNFI AAADHTTKAA FKTPGLRNVA SRPPYMHAGQ
LASLEDVVRH YANAPASAAG HSELKPINLS EQEVRDVIAF LHTLSSPIVQ RQ
//
