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Database: UniProt
Entry: H0IYN3_9GAMM
LinkDB: H0IYN3_9GAMM
Original site: H0IYN3_9GAMM 
ID   H0IYN3_9GAMM            Unreviewed;       329 AA.
AC   H0IYN3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Cytochrome-c peroxidase {ECO:0000313|EMBL:EHK62053.1};
GN   ORFNames=MOY_02379 {ECO:0000313|EMBL:EHK62053.1};
OS   Halomonas sp. GFAJ-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1118153 {ECO:0000313|EMBL:EHK62053.1, ECO:0000313|Proteomes:UP000004512};
RN   [1] {ECO:0000313|EMBL:EHK62053.1, ECO:0000313|Proteomes:UP000004512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GFAJ-1 {ECO:0000313|EMBL:EHK62053.1,
RC   ECO:0000313|Proteomes:UP000004512};
RX   PubMed=22408239; DOI=10.1128/JB.06664-11;
RA   Phung le T., Silver S., Trimble W.L., Gilbert J.A.;
RT   "Draft Genome of Halomonas Species Strain GFAJ-1 (ATCC BAA-2256).";
RL   J. Bacteriol. 194:1835-1836(2012).
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:EHK62053.1}.
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DR   EMBL; AHBC01000008; EHK62053.1; -; Genomic_DNA.
DR   RefSeq; WP_009096112.1; NZ_CP016490.1.
DR   AlphaFoldDB; H0IYN3; -.
DR   STRING; 1118153.MOY_02379; -.
DR   KEGG; hag:BB497_13270; -.
DR   PATRIC; fig|1118153.6.peg.473; -.
DR   eggNOG; COG1858; Bacteria.
DR   OrthoDB; 9805202at2; -.
DR   Proteomes; UP000004512; 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   Pfam; PF00034; Cytochrom_C; 1.
DR   PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS51007; CYTC; 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:EHK62053.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Peroxidase {ECO:0000313|EMBL:EHK62053.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004512};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..329
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003534784"
FT   DOMAIN          208..317
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         76
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         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         80
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         96
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"
FT   BINDING         292
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;  36041 MW;  5EAF9073208CE587 CRC64;
     MKMTKKILPG IIASAALIST GAMAAEDGFE DYRDRFEALP YLPPIPAHNS LTKEKVELGN
     MLFFEPRISS SGVISCATCH NPALGWADRI PRAVGHDGQV GERNTPTVLN SGFFEAQFWD
     GREPDLEGQA LGPIEADVEM AMDLEMALER LTEFDLYQEK FAEAYPDDAD PINADNLAKA
     LASFQRTLNT PNSPFDRYLR GDLSAISDQA KDGMAAFVNN GCIACHSGPA LTDSRFHAIQ
     VPGSTDLGRY LVTGEESDKY RFKTPTLRNV AVTYPYMNNG ATETLEEAVA IMGEEMLGRE
     FDDATINDIT AFLHTLTGEM PDFEIPALP
//
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