ID C6VVR6_DYAFD Unreviewed; 348 AA.
AC C6VVR6;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Cytochrome-c peroxidase {ECO:0000313|EMBL:ACT91372.1};
DE EC=1.11.1.5 {ECO:0000313|EMBL:ACT91372.1};
GN OrderedLocusNames=Dfer_0101 {ECO:0000313|EMBL:ACT91372.1};
OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS 52180 / NS114).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT91372.1, ECO:0000313|Proteomes:UP000002011};
RN [1] {ECO:0000313|EMBL:ACT91372.1, ECO:0000313|Proteomes:UP000002011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC {ECO:0000313|Proteomes:UP000002011};
RX PubMed=21304649; DOI=10.4056/sigs.19262;
RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL Stand. Genomic Sci. 1:133-140(2009).
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; CP001619; ACT91372.1; -; Genomic_DNA.
DR RefSeq; WP_012779720.1; NC_013037.1.
DR AlphaFoldDB; C6VVR6; -.
DR STRING; 471854.Dfer_0101; -.
DR KEGG; dfe:Dfer_0101; -.
DR eggNOG; COG1858; Bacteria.
DR HOGENOM; CLU_034652_3_3_10; -.
DR OrthoDB; 9805202at2; -.
DR Proteomes; UP000002011; Chromosome.
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:SF12; BLL6722 PROTEIN; 1.
DR PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR Pfam; PF03150; CCP_MauG; 1.
DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:ACT91372.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Peroxidase {ECO:0000313|EMBL:ACT91372.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002011};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 206..334
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 74
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 77
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 78
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 219
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 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 223
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 348 AA; 38299 MW; 1AB36F3FF0036BED CRC64;
MRLVKLGWFC IVLLISSCDK DTVAPAENAY AFEVPPHFPV PVPDAHNPMT EAGIRLGRQL
FYDRRLSANN KVSCASCHDP AKAFSDGVAL STSGVSDTQL LRHAPALFNL AWATNGLFWD
GGSTNLESQA FGPLTAHDEM AQDLYELVDE LNADASYVKG FQEAFSAGIT SQNVAKALAQ
FQRSLVSATS RYDDFRLGRN GAVLTPEEMS GLALVRQHCQ GCHSGELFTD NGYHNNGLDS
RFDNQDHEGI FMGRYRISYD EGDLGKFKTP SLRNVTLTAP YMHDGRIPTL EKVLDHYSNG
IQHSATLDGR IPQQGFAFSA VQKTQIIAFL ATLTDERFVS NPAHQKPH
//
