ID A9DJR8_9GAMM Unreviewed; 329 AA.
AC A9DJR8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 03-MAY-2023, entry version 63.
DE SubName: Full=Cytochrome c551 peroxidase {ECO:0000313|EMBL:EDP98965.1};
GN ORFNames=KT99_09493 {ECO:0000313|EMBL:EDP98965.1};
OS Shewanella benthica KT99.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=314608 {ECO:0000313|EMBL:EDP98965.1, ECO:0000313|Proteomes:UP000005839};
RN [1] {ECO:0000313|EMBL:EDP98965.1, ECO:0000313|Proteomes:UP000005839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT99 {ECO:0000313|EMBL:EDP98965.1,
RC ECO:0000313|Proteomes:UP000005839};
RA Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (OCT-2007) 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:EDP98965.1}.
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DR EMBL; ABIC01000058; EDP98965.1; -; Genomic_DNA.
DR RefSeq; WP_005502933.1; NZ_ABIC01000058.1.
DR AlphaFoldDB; A9DJR8; -.
DR STRING; 314608.KT99_09493; -.
DR Proteomes; UP000005839; 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:SF7; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR Pfam; PF03150; CCP_MauG; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
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:EDP98965.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Peroxidase {ECO:0000313|EMBL:EDP98965.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..329
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002734062"
FT DOMAIN 37..145
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT DOMAIN 189..303
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 59
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 62
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 63
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 79
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 203
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 206
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 207
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"
FT BINDING 278
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 329 AA; 35534 MW; 3386D9D8F6CD29D5 CRC64;
MKQLSCVSLA ILAAISTAAM AQEPIQIIEP AKITAPKKVE LGKMLFFEPR LSKSGFISCN
SCHNLSLGGV DALPTSIGHN WQQGPINSPT VLNAEYGLAQ FWDGRAKDLQ AQAGGPIANP
GEMGYTHELA VLTVNSMPAY QEKFAAIYGK DAVNIDNITN AIAEFEKTLV TPNSPFDLYL
QGDKSAISAE VKSGYQLFKD KGCTSCHNGP AVGGTMYMKM GLVKPFHTKN PAQGRKAVTG
NEADKFVFKV PTLRNIELTY PYFHDGATWT LEEAVNTMAE IQLGQELTAA ETKEMVAFLK
SLTGEQPQIV LPILPPSNAK TPRPVPFAD
//