ID   IDRB_DENS1              Reviewed;         185 AA.
AC   P0DV67;
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 IdrB {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305|PubMed:34215855};
DE   Flags: Precursor;
GN   Name=idrB {ECO:0000303|PubMed:34215855}; ORFNames=I8J34_RS03785;
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 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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00628};
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:A0A391NZA8}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC   -!- SIMILARITY: Belongs to the AOX 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:0051537; F:2 iron, 2 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   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR014067; Arsenite_oxidase_ssu.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   TIGRFAMs; TIGR02694; arsenite_ox_S; 1.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Periplasm;
KW   Signal.
FT   SIGNAL          1..46
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           47..185
FT                   /note="Iodate reductase subunit IdrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT                   /id="PRO_0000455406"
FT   DOMAIN          69..168
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         109
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         111
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         130
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         133
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   185 AA;  19532 MW;  9D25FFC007CE79E6 CRC64;
     MTTHPIHLHH DDPAHGGERA CMSRRSFLLA GGAMVTLASL PGTAVAALKA LKADYPAVKI
     GKLSRLKTGE PLEFAYPYPD VNNILVKLGA EAGGGVGPQA DVVAFNQQCT HMGGPLQGTY
     KAKHQALGPC PLHLTTFDLT RHGMVISGHA TESLPQIVLE VRGDDIYAVG VQGLIYGYSS
     NRAGR