ID   IDRP1_DENS1             Reviewed;         376 AA.
AC   P0DV68;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 1.
DT   03-AUG-2022, entry version 2.
DE   RecName: Full=Cytochrome-c peroxidase IdrP1 {ECO:0000305};
DE            EC=1.11.1.5 {ECO:0000305|PubMed:34215855};
DE   AltName: Full=Iodate reductase subunit IdrP1 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=idrP1 {ECO:0000303|PubMed:34215855}; ORFNames=I8J34_RS03790;
OS   Denitromonas sp. (strain IR12).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Denitromonas; unclassified Denitromonas.
OX   NCBI_TaxID=2795389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC   STRAIN=IR12;
RX   PubMed=34215855; DOI=10.1038/s41396-021-01034-5;
RA   Reyes-Umana V., Henning Z., Lee K., Barnum T.P., Coates J.D.;
RT   "Genetic and phylogenetic analysis of dissimilatory iodate-reducing
RT   bacteria identifies potential niches across the world's oceans.";
RL   ISME J. 16:38-49(2022).
CC   -!- FUNCTION: Involved in iodate respiration (PubMed:34215855). May play a
CC       critical role in detoxification of inadvertent H(2)O(2) generated by
CC       the iodate reductase IdrA/IdrB (PubMed:34215855).
CC       {ECO:0000269|PubMed:34215855}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-
CC         [cytochrome c] + 2 H2O; Xref=Rhea:RHEA:16581, Rhea:RHEA-COMP:10350,
CC         Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.11.1.5;
CC         Evidence={ECO:0000305|PubMed:34215855};
CC   -!- COFACTOR:
CC       Name=heme c; Xref=ChEBI:CHEBI:61717;
CC         Evidence={ECO:0000250|UniProtKB:P14532};
CC       Note=Binds 2 heme c groups. {ECO:0000250|UniProtKB:P14532};
CC   -!- SUBUNIT: The iodate reductase (Idr) complex is composed of a
CC       molybdopterin-dependent iodate reductase (IdrA and IdrB subunits) and
CC       two associated peroxidases (IdrP1 and IdrP2).
CC       {ECO:0000305|PubMed:34215855}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:A0A391NGM7}.
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DR   EMBL; JAEKFT010000003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 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   Pfam; PF03150; CCP_MauG; 1.
DR   PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR   SUPFAM; SSF46626; SSF46626; 2.
DR   PROSITE; PS51007; CYTC; 2.
PE   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; Repeat; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..376
FT                   /note="Cytochrome-c peroxidase IdrP1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000455408"
FT   DOMAIN          49..157
FT                   /note="Cytochrome c 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   DOMAIN          203..354
FT                   /note="Cytochrome c 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         71
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         74
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         75
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:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         218
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         221
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         222
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:0000255|PROSITE-ProRule:PRU00433"
SQ   SEQUENCE   376 AA;  40712 MW;  6DE5D03663DDF7DB CRC64;
     MGHIRSIRLA LAVAAVCTAA SAAAGDAKFP PLGPLPPVPV PADNPMTADK VALGKQLFWD
     NRLSGDGSTP CVSCHLPALG WGDGGAISRG YPGTKHWRNS QTIVNSAYYN KLFWAGSVTS
     LEAQAPSAAE GGVAGNGDRS LMEMRLRFIP EYVAAFKNVF GADWPRMTQA YAAIAAYQRT
     VVSDATRVPF DRWQAGDKAA MSAEAQRGYA LFSGKAGCIA CHNGPLASDQ RFYNLGLPEH
     PDLAEDPLLQ ITHRWEQYQK GTTEDGYRHA DRDKGYYYQT KNPKDIGKFR TPSLREVKYT
     GPYMHNGTLA TLDEVVAFYN AGGGTAPGKT DKLKPLGLTE QESKDLVAFV EALSMTEPLI
     HDDPKLPGDY QPLATQ