AIOB_HERAR
ID AIOB_HERAR Reviewed; 173 AA.
AC Q8GGJ7; A4G2F4;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Arsenite oxidase subunit AioB;
DE EC=1.20.9.1;
DE AltName: Full=Arsenite oxidase Rieske subunit;
DE Flags: Precursor;
GN Name=aioB; Synonyms=aoxA; OrderedLocusNames=HEAR0479;
OS Herminiimonas arsenicoxydans.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ULPAs1;
RX PubMed=12486049; DOI=10.1128/jb.185.1.135-141.2003;
RA Muller D., Lievremont D., Simeonova D.D., Hubert J.C., Lett M.C.;
RT "Arsenite oxidase aox genes from a metal-resistant beta-Proteobacterium.";
RL J. Bacteriol. 185:135-141(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1;
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.-C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
RN [3]
RP NOMENCLATURE.
RX PubMed=22056935; DOI=10.1128/jb.06391-11;
RA Lett M.C., Muller D., Lievremont D., Silver S., Santini J.;
RT "Unified nomenclature for genes involved in prokaryotic aerobic arsenite
RT oxidation.";
RL J. Bacteriol. 194:207-208(2012).
CC -!- FUNCTION: Involved in the detoxification of arsenic. Oxidizes
CC As(III)O3(3-) (arsenite) to the somewhat less toxic As(V)O4(3-)
CC (arsenate).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=arsenite + H2O + 2 oxidized [azurin] = arsenate + 3 H(+) + 2
CC reduced [azurin]; Xref=Rhea:RHEA:18701, Rhea:RHEA-COMP:11034,
CC Rhea:RHEA-COMP:11035, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29036, ChEBI:CHEBI:29242, ChEBI:CHEBI:48597,
CC ChEBI:CHEBI:49552; EC=1.20.9.1;
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: Heterodimer consisting of a large and a small subunit.
CC -!- INDUCTION: Induced in the presence of arsenite.
CC {ECO:0000269|PubMed:12486049}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the AOX family. {ECO:0000305}.
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DR EMBL; AF509588; AAN05580.1; -; Genomic_DNA.
DR EMBL; CU207211; CAL60691.1; -; Genomic_DNA.
DR RefSeq; WP_011870034.1; NC_009138.1.
DR AlphaFoldDB; Q8GGJ7; -.
DR SMR; Q8GGJ7; -.
DR STRING; 204773.HEAR0479; -.
DR EnsemblBacteria; CAL60691; CAL60691; HEAR0479.
DR KEGG; har:HEAR0479; -.
DR eggNOG; COG0723; Bacteria.
DR HOGENOM; CLU_055690_1_3_4; -.
DR OMA; CHYSMFD; -.
DR OrthoDB; 1632945at2; -.
DR Proteomes; UP000006697; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050611; F:arsenate reductase (azurin) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03476; Rieske_ArOX_small; 1.
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; IPR014349; Rieske_Fe-S_prot.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF10518; TAT_signal; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR TIGRFAMs; TIGR02694; arsenite_ox_S; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS51318; TAT; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Disulfide bond; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..35
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 36..173
FT /note="Arsenite oxidase subunit AioB"
FT /id="PRO_0000030698"
FT DOMAIN 60..156
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 100
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 102
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 118
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 121
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 105..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 173 AA; 17821 MW; 5A9EE75C825380BF CRC64;
MEHQTSRRNF LKIAGSSAAV AGAGLVSGNA NAAPAKVNVG ASTLPYPITA VGKAKGLKVD
APVSFNYPDA SSPCVAIKMG QPTPGGVGPN NDIVAHSILC THMGCPVSYD ASAKTFKCPC
HFSVFDPDNH GQMVCGQATE NLPQIQLSYN AANDTFTAIG VTGLIYGRQS NIL
