ID   IDRB_PSEXS              Reviewed;         192 AA.
AC   A0A391NZA8;
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 IdrB {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000305|PubMed:32190953};
DE   Flags: Precursor;
GN   Name=idrB {ECO:0000303|PubMed:32190953};
GN   ORFNames=PSCT_04484 {ECO:0000312|EMBL:GCA58264.1};
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=[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:0000269|PubMed:32190953}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:32190953}.
CC   -!- INDUCTION: Specifically expressed under iodate-respiring conditions.
CC       {ECO:0000269|PubMed:32190953}.
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; BDJA01000015; GCA58264.1; -; Genomic_DNA.
DR   EnsemblBacteria; GCA58264; GCA58264; PSCT_04484.
DR   Proteomes; UP000268673; Unassembled WGS sequence.
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..52
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           53..192
FT                   /note="Iodate reductase subunit IdrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT                   /id="PRO_0000455407"
FT   DOMAIN          102..173
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         114
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         116
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         135
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         138
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   192 AA;  20535 MW;  2DEEEECCDAD6847E CRC64;
     MSENIIPVRA VPAHDHEHDG ERACMSRRRF LLFGGTSVAL LSIASLPGVA QVMQALKADY
     ARQRIGSLSA LKTGEPLDFN YPYPDVRNIL VKLGVAAGGG IGADKDIVAF NQQCTHMGGP
     LDGTYKAEHQ ILGPCPLHLT TFDLTRHGMV ASGHATESLP QIVLEVQGDD IYAIGVLGLV
     YGFDSMNDVQ PA