IDRP2_DENS1
ID IDRP2_DENS1 Reviewed; 367 AA.
AC P0DV69;
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 IdrP2 {ECO:0000305};
DE EC=1.11.1.5 {ECO:0000305|PubMed:34215855};
DE AltName: Full=Iodate reductase subunit IdrP2 {ECO:0000305};
DE Flags: Precursor;
GN Name=idrP2 {ECO:0000303|PubMed:34215855}; ORFNames=I8J34_RS03795;
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:A0A391NKV7}.
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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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..367
FT /note="Cytochrome-c peroxidase IdrP2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455409"
FT DOMAIN 47..157
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 200..345
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 69
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 72
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 73
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 215
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 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 219
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 367 AA; 39941 MW; 0C96309D2E081815 CRC64;
MTTHQSIRRL SRIAALVGLA FVAGTVAAAD GKAELQALPE AKAGNADMVE LGKHLFFDTR
LSGDMGVSCA SCHDPAKGFS DGMPLSAGYP SVEYFRNAPT LINSRFKNVF MWDGRLDGAD
MGTLVRDMLT EAHTMNMDSR LMQERLSQVP EYVAMWQKFR KDDINGMRVY GVVGEYVKTL
VSQNAPIDRF LKGDGSALTS QQKDGYEIFT GKGGCVACHN GPLGSDGQVH NTGVPENPEV
LKNPNRTVTL LRHYATSGMP NYMNARTDLG HYAISKDPAD MNKFATPSLR ELKYTAPYMH
NGMLTTLDQV VDFYNQGGGQ GSELTPLGLS GSEKKALVAF LEALSGEPLN VVAPTLPDYQ
PRQFGKN
