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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//