IDRP1_PSEXS
ID IDRP1_PSEXS Reviewed; 379 AA.
AC A0A391NGM7;
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 IdrP1 {ECO:0000305};
DE EC=1.11.1.5 {ECO:0000305|PubMed:32190953};
DE AltName: Full=Iodate reductase subunit IdrP1 {ECO:0000305};
DE Flags: Precursor;
GN Name=idrP1 {ECO:0000303|PubMed:32190953};
GN ORFNames=PSCT_04483 {ECO:0000312|EMBL:GCA58263.1};
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: Abundantly expressed under iodate-respiring conditions.
CC {ECO:0000269|PubMed:32190953}.
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DR EMBL; BDJA01000015; GCA58263.1; -; Genomic_DNA.
DR EnsemblBacteria; GCA58263; GCA58263; PSCT_04483.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..379
FT /note="Cytochrome-c peroxidase IdrP1"
FT /evidence="ECO:0000255"
FT /id="PRO_5017320034"
FT DOMAIN 50..158
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 204..355
FT /note="Cytochrome c 2"
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 75
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 76
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 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 222
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 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:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 379 AA; 41822 MW; 307B15B114054096 CRC64;
MNNRKPLQLS LLVASLAVAF TASATNADAH PPLAPLPPVP VPKDNPQSAE KIALGKQLFW
DYRLSGDGSM PCVSCHLPAL GWGDGGQISR GYPGTKHWRN SQTILNSAYY NKLFWEGSVN
SLEEQAPSAA EGAVAGNGDP SVMEMRLRFV PEYVDAFKNV FGSQWPRMND AYRAIASYQR
TVVSDASKVP FDRYANGDKN ALDTSQKRGM ALFNGKAGCV QCHNGPLASD QKYYDLGLPD
FAGFVDDPLY QVTHRWEHYQ KGVSEPRYRA ANMDYGLYYV TKNPKDVGKF RTPSLREAKY
TAPYMHNGVF TSLQEVVDFY DRGGGSGTSK SELLKPLKLA AQEKQDLIAF IEALSMSEPL
LHDDPTLPGE YQPLPAPIK
