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Database: UniProt
Entry: B6B8N8_9RHOB
LinkDB: B6B8N8_9RHOB
Original site: B6B8N8_9RHOB 
ID   B6B8N8_9RHOB            Unreviewed;       332 AA.
AC   B6B8N8;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Cytochrome C peroxidase {ECO:0000313|EMBL:EDZ46518.1};
DE            EC=1.11.1.5 {ECO:0000313|EMBL:EDZ46518.1};
GN   Name=yhjA {ECO:0000313|EMBL:EDZ46518.1};
GN   ORFNames=RBY4I_1733 {ECO:0000313|EMBL:EDZ46518.1};
OS   Rhodobacterales bacterium Y4I.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX   NCBI_TaxID=439496 {ECO:0000313|EMBL:EDZ46518.1, ECO:0000313|Proteomes:UP000005133};
RN   [1] {ECO:0000313|EMBL:EDZ46518.1, ECO:0000313|Proteomes:UP000005133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4I {ECO:0000313|EMBL:EDZ46518.1,
RC   ECO:0000313|Proteomes:UP000005133};
RA   Moran M.A., Buchan A., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) 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; DS995281; EDZ46518.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6B8N8; -.
DR   STRING; 439496.RBY4I_1733; -.
DR   eggNOG; COG1858; Bacteria.
DR   HOGENOM; CLU_034652_3_1_5; -.
DR   OrthoDB; 9805202at2; -.
DR   Proteomes; UP000005133; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004130; F:cytochrome-c peroxidase activity; IEA:UniProtKB-EC.
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   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   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:EDZ46518.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Peroxidase {ECO:0000313|EMBL:EDZ46518.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005133};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..332
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002842855"
FT   DOMAIN          46..147
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          198..318
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         68
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         71
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         72
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         213
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         216
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         217
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   332 AA;  35626 MW;  9ADDBC0CC28339EF CRC64;
     MQWKAAAAVV PLLFWAVQSL AQPAGLDAFR RPDTVPFPDN APYDRGIATL GKMLFFDPRL
     SGAQNISCSS CHNPSFGWET PVPKAIGAGD NPVHRHAPTI LNAAWITPLF WDGRAASLEE
     QAVGPITAPN EMNASFEDIT ARLTAVTEYK AWFERLFPGQ GIRKETILTA LATYQRTIVS
     GVAGFDRWVS GDDTAVPEAA KRGFALFTGR ANCVSCHSGW MFTDNKMHDI GLPASDLGSG
     GVSPQTPAGY FRFKTPGLRN IALRAPYMHD GSLPSLPAVL RHYADGGAAG VERQTDIAGF
     AASEGDIADL IAFLETLTDN ETNVPTPILP AN
//
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