IDRP2_PSEXS
ID IDRP2_PSEXS Reviewed; 368 AA.
AC A0A391NKV7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Cytochrome-c peroxidase IdrP2 {ECO:0000305};
DE EC=1.11.1.5 {ECO:0000305|PubMed:32190953};
DE AltName: Full=Iodate reductase subunit IdrP2 {ECO:0000305};
DE Flags: Precursor;
GN Name=idrP2 {ECO:0000303|PubMed:32190953};
GN ORFNames=PSCT_04482 {ECO:0000312|EMBL:GCA58262.1};
OS Pseudomonas sp. (strain SCT).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=412955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCT;
RA Harada M., Ito K., Nakajima N., Yamamura S., Tomita M., Suzuki H.,
RA Amachi S.;
RT "Genome sequencing of bacteria contributing to the geochemical cycling of
RT arsenic, bromine, and iodine.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RC STRAIN=SCT;
RX PubMed=32190953; DOI=10.1111/1462-2920.14988;
RA Yamazaki C., Kashiwa S., Horiuchi A., Kasahara Y., Yamamura S., Amachi S.;
RT "A novel dimethylsulfoxide reductase family of molybdenum enzyme, Idr, is
RT involved in iodate respiration by Pseudomonas sp. SCT.";
RL Environ. Microbiol. 22:2196-2212(2020).
CC -!- FUNCTION: Involved in iodate respiration (PubMed:32190953). Probably
CC reduces the H(2)O(2) produced by IdrA/IdrB to H(2)O, using a reduced
CC cytochrome c as the electron donor (PubMed:32190953).
CC {ECO:0000269|PubMed:32190953}.
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:32190953};
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:0000269|PubMed:32190953}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:32190953}.
CC -!- INDUCTION: Specifically expressed under iodate-respiring conditions.
CC {ECO:0000269|PubMed:32190953}.
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DR EMBL; BDJA01000015; GCA58262.1; -; Genomic_DNA.
DR EnsemblBacteria; GCA58262; GCA58262; PSCT_04482.
DR Proteomes; UP000268673; Unassembled WGS sequence.
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 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..368
FT /note="Cytochrome-c peroxidase IdrP2"
FT /evidence="ECO:0000255"
FT /id="PRO_5017308201"
FT DOMAIN 48..158
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 201..346
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 70
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 /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 /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 216
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 /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 220
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 368 AA; 40203 MW; 0543EDBB4D324D69 CRC64;
MKWHRGRLTQ TLGAMGLTAT LTVAAQAAGQ GDMLDLAPMP PAKAGNPAMI ELGKQFFFDR
RLSGDWGVSC ASCHDPAKGW GDGLALSKGY PSMEYFRNSP TVLNAAHRKR FLWDGRLDGA
DPGTLARDMI TEAHTMNMDG RLMQERLQQV PEYAALWQKW RNDDINGMRV FNAVGEFITS
LETRNAPFDD FAKGDSTAIT KEAQHGYALF KGKAGCVSCH NGPIGSDGKL HKTGVPEHPD
VLNNPLRTIT MLRHYATSGM PNYMSARSDV GAYAISKDER DVGKFQTAQL RDLKYTAPYM
HNGVFDTLEE VVAFYNQGGG EGSALSPLTL STAEQQALVA FLLTLSGDPL IVEDPGQPDM
QPRVFGKN
