ID   IDRA_DENS1              Reviewed;         900 AA.
AC   P0DV66;
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=Iodate reductase subunit IdrA {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305|PubMed:34215855};
GN   Name=idrA {ECO:0000303|PubMed:34215855}; ORFNames=I8J34_RS03780;
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, SUBUNIT, AND
RP   DISRUPTION PHENOTYPE.
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 accept
CC       electrons from cytochrome c551, and catalyze the reduction of iodate
CC       (IO(3)(-)) to produce the chemically unstable intermediate hypoiodous
CC       acid (HIO). This intermediate then undergoes abiotic disproportionation
CC       to yield two molecules of iodide (I(-)) and one molecule of iodate. The
CC       resultant iodate subsequently cycles back into the reductive pathway
CC       (PubMed:34215855). The initial reduction of iodate may inadvertently
CC       produce low levels of incidental toxic H(2)O(2), which is detoxified by
CC       IdrP1 and IdrP2 (PubMed:34215855). {ECO:0000269|PubMed:34215855}.
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:0000305|PubMed:34215855}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:A0A391NTR7}.
CC       Note=May be co-transported with IdrB into the periplasm.
CC       {ECO:0000303|PubMed:34215855}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant is incapable of growth via iodate
CC       respiration, while growth under oxic conditions remains unimpaired.
CC       {ECO:0000269|PubMed:34215855}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000305}.
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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: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: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..900
FT                   /note="Iodate reductase subunit IdrA"
FT                   /id="PRO_0000455404"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         35
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIF4"
FT   BINDING         38
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIF4"
FT   BINDING         42
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIF4"
FT   SITE            113
FT                   /note="Involved in charge transfer"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIF4"
SQ   SEQUENCE   900 AA;  101089 MW;  95EEE6C204E8CD7E CRC64;
     MSENIKQGGA GTFMQAPQDS VPLPPKDAEV MTTACDYCTV ACGYKVYRWP VGKEGGMKAK
     DNAFNADFPH QQIFGAWASP AQHNIVNHNG RSHHVLVLPD RDTTVVNPGG NHSIRGGTLA
     QKCYNPSNRT SERLLYPMIR VRGTLMPVSW DLATEVMADI SQYILAKYGE HAWAMKTYSY
     QYFENTYAIT KLGMTSIGTP AFAWHDKASA TNDATGLDDA GVNSFASSDQ DWADCEVAFL
     SGVDPYETKT TLFTQWMMPG DKKFIFVTPH RTMGVAWAES TGRGMWLPII PGTDTVLHLA
     LARIIVENGW QDQAFIDKWV ANKWEVDSGY GRGTRNTGWQ WRTTWGKWQS DWKDYSAWIL
     KQKEGELETA AKITGLRAED IRKAAEWIAK PKADGTRVKA SFMLEKGNYW TNNYMNSASL
     ASLGLICGSG NRPGQMISRG GGHQRGGMSA GGGSGWLSPE KYPGRRKKSF NLDRWMMNGN
     VRFAWVIGTT WTAAMMASQA LQDKMFSLTR GNPHQISSLD RKAIFETLKQ RVDSGGTVIA
     NSDIYPCVPV GTEYADIVLP AATWGEDNFT RCNSERRLRL YSKFYDAPGE AKPDWWIIAK
     FAQKMGYDKD GSYQWKNSND VFEEAARFGR NGVLNYHPLV VKAKEKGVKG HELLRTYGTD
     GIQTPIRMKD GELVGTQRLH DPANDWDEVE GQEVKRKWLY AFGTHSGKAI LLKTPWDYPG
     WSQFYKAALP RKEKGEVWVT NGRVNETWQS GFDDLRKPYL SQRWPYPMLI MHPDEAKPRG
     IESGDFVQVY NDTVYIQMGE PQGVKEDDLY FDTLMKNGHI KTTDGQFVAV AIVSEEMRPG
     VVMANFNYPQ APANSVVHAV PDPMTNNYRY KLGRGVLTKV GESPYKHSFT SMTLKPRDIV