IDRA_PSEXS
ID IDRA_PSEXS Reviewed; 892 AA.
AC A0A391NTR7;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Iodate reductase subunit IdrA {ECO:0000305};
DE EC=1.-.-.- {ECO:0000305|PubMed:32190953};
GN Name=idrA {ECO:0000303|PubMed:32190953};
GN ORFNames=PSCT_04485 {ECO:0000312|EMBL:GCA58265.1};
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 catalyzes the reduction of iodate (IO(3)(-)) to hypoiodous acid (HIO)
CC and H(2)O(2), using a reduced cytochrome c as the electron donor
CC (PubMed:32190953). {ECO:0000269|PubMed:32190953}.
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000250|UniProtKB:Q7SIF4};
CC Note=Binds 1 [3Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:Q7SIF4};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250|UniProtKB:Q7SIF4};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250|UniProtKB:Q7SIF4};
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}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; BDJA01000015; GCA58265.1; -; Genomic_DNA.
DR SMR; A0A391NTR7; -.
DR EnsemblBacteria; GCA58265; GCA58265; PSCT_04485.
DR Proteomes; UP000268673; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR041632; AioA_3Fe-4S.
DR InterPro; IPR014066; Arsenite_oxidase_lsu.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF18465; Rieske_3; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR02693; arsenite_ox_L; 1.
PE 1: Evidence at protein level;
KW 3Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase;
KW Periplasm.
FT CHAIN 1..892
FT /note="Iodate reductase subunit IdrA"
FT /id="PRO_0000455405"
FT REGION 431..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:Q7SIF4"
FT BINDING 30
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:Q7SIF4"
FT BINDING 34
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:Q7SIF4"
FT SITE 105
FT /note="Involved in charge transfer"
FT /evidence="ECO:0000250|UniProtKB:Q7SIF4"
SQ SEQUENCE 892 AA; 99303 MW; 4C20E00EAE5F13CE CRC64;
MSKPDEYLSS NSVPLPPQDA DVLTTACDYC IVACGYKVYR WPVGKEGGAK ASENALGADF
PHQMMMGAWA SPAQHNVVSY RDQPHHVVVI ADKDATVVNP GGNHSIRGGT LAEKCYNPSN
RTRERLQHPM IRVNGKLTPV SWDLATEVMA DISQYIIAKY GEHAWAVKSH SYQYFENVYA
ITKLAMTSIG TPAFAWHDKC SATNDATGLD DAGIDSFASS YEDWADCEVA FLSGVDPYET
KTTLFTSHMM PGDKKFVFVT PHMTMGVAWS VKAGRGLWLP IIPGTDTVLH MALARIIIEN
DWQDQPFIDK WIANSWEVDS GYGRGTRNTG WQWRTTWGTW QSDWQDYRKF ILAQEESKLD
VAAQITGLSA DDIRTAAEWI AKPKADGSHP KTSFMCEKGN YWSNNYMNSA SFASLGLICG
SGNRKGRMIS RGGGHQRGGL SAGGNSEWLS PEKYPGRRKK SFNLDLWLME GNIRFAWVIG
TTWVAAMMGS NALEAKMRSL TAESPHQIKS LDRAAIFETL KARVDSGGMV MANSDLYPVV
PVGTDFADIV YPVASWGEDN FTRCNSERRL RLYSKFYDAP GEAKPDWWIV QKFAQKMGLD
KDGGYSWKDS NDVFEEVARF SRDGVLNYHP LAEKAKASGI KAQELLRGYG TTGIQTPIRE
RGGELVGTVR LHDPDNDWGE IEGSTVHTKA LVAFNTHSGK AILLKSPWQY AGWIQFYEAI
KPRAAKGEVW VTNGRVNETW QSGFDDRRKP YLSQRWPEGF IFINPEDARK KGIESGDYVE
VVNDTVYIQT GQPQGVLDAD LTFNQLMADG HIKITTGRFK TIAVVSDEMR PGVCQANFNV
PSSPANAVVS AVPDPMTNNY RYKLGRGVLN KVGESPYKHN FTQMSLKPRN IV
