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Database: UniProt
Entry: A0A2Z6GAD6_9PROT
LinkDB: A0A2Z6GAD6_9PROT
Original site: A0A2Z6GAD6_9PROT 
ID   A0A2Z6GAD6_9PROT        Unreviewed;       345 AA.
AC   A0A2Z6GAD6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Cytochrome c551 peroxidase {ECO:0000313|EMBL:BBE50309.1};
GN   ORFNames=OYT1_ch0743 {ECO:0000313|EMBL:BBE50309.1};
OS   Ferriphaselus amnicola.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Ferriphaselus.
OX   NCBI_TaxID=1188319 {ECO:0000313|EMBL:BBE50309.1, ECO:0000313|Proteomes:UP000033070};
RN   [1] {ECO:0000313|EMBL:BBE50309.1, ECO:0000313|Proteomes:UP000033070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OYT1 {ECO:0000313|EMBL:BBE50309.1,
RC   ECO:0000313|Proteomes:UP000033070};
RA   Kato S., Itoh T., Ohkuma M.;
RT   "OYT1 Genome Sequencing.";
RL   Submitted (JUN-2018) 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; AP018738; BBE50309.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z6GAD6; -.
DR   STRING; 1188319.OYT1_00008; -.
DR   KEGG; fam:OYT1_ch0743; -.
DR   Proteomes; UP000033070; Chromosome.
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   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:BBE50309.1};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Peroxidase {ECO:0000313|EMBL:BBE50309.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033070};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          67..198
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          218..337
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         89
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         92
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         93
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         232
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         235
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         236
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         312
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   345 AA;  37788 MW;  3D9425662CB04341 CRC64;
     MTKSKISLKN ILLGALLGVL VLVVSFSWQL YRTQLALNAG APLDPYAITV SLGYTQPLPR
     EIKLDADKVL LGRKLFNDPR LSADNSISCA SCHSLDKGGA DGRVHAIGIN GAEGVINTPT
     VLNSGFNFAQ FWDGRAATLE EQIEGPINNP KEMGSNWGQI TDKLKQDSDY RSAFSKLYRA
     DISAENIKDA IATFERSLVT PDSPFDRYLQ GDNSAMSEQA QRGYELFQSY GCIACHQGVN
     LGGNMFEKMG LMGDYFEARG NLTEADLGRF NVTHKEEARY EFKVPGLRNV ALTAPYFHDG
     SVATLPDAVA VMVRYQLGRT MPQQDLDDIV QFLNSLTGEL GGQAQ
//
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