AIOA_HERAR
ID AIOA_HERAR Reviewed; 826 AA.
AC Q8GGJ6; A4G2F3;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Arsenite oxidase subunit AioA;
DE EC=1.20.9.1;
DE AltName: Full=Arsenite oxidase Mo-pterin subunit;
GN Name=aioA; Synonyms=aoxB; OrderedLocusNames=HEAR0478;
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=[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: Heterodimer consisting of a large and a small subunit.
CC {ECO:0000250|UniProtKB:Q7SIF4}.
CC -!- INDUCTION: Induced in the presence of arsenite.
CC {ECO:0000269|PubMed:12486049}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AF509588; AAN05581.1; -; Genomic_DNA.
DR EMBL; CU207211; CAL60690.1; -; Genomic_DNA.
DR RefSeq; WP_011870033.1; NC_009138.1.
DR AlphaFoldDB; Q8GGJ6; -.
DR SMR; Q8GGJ6; -.
DR STRING; 204773.HEAR0478; -.
DR EnsemblBacteria; CAL60690; CAL60690; HEAR0478.
DR KEGG; har:HEAR0478; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_328691_0_0_4; -.
DR OMA; GCGYKAY; -.
DR OrthoDB; 323168at2; -.
DR Proteomes; UP000006697; Chromosome.
DR GO; GO:0051538; F:3 iron, 4 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 GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
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 2: Evidence at transcript level;
KW 3Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..826
FT /note="Arsenite oxidase subunit AioA"
FT /id="PRO_0000063241"
FT BINDING 22
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:Q7SIF4"
FT BINDING 25
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:Q7SIF4"
FT BINDING 29
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250|UniProtKB:Q7SIF4"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 100
FT /note="Involved in charge transfer"
FT /evidence="ECO:0000250|UniProtKB:Q7SIF4"
FT CONFLICT 318
FT /note="V -> L (in Ref. 1; AAN05581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 826 AA; 91627 MW; EE690A8B31A7C010 CRC64;
MSKNRDRVAL PPVNAQKTNM TCHFCIVGCG YHVYKWDENK EGGRAANQNA LGLDFTKQLP
PFATTLTPAM TNVITAKNGK RSNIMIIPDK ECVVNQGLSS TRGGKMAGYM YAADGMTADR
LKYPRFYAGD QWLDTSWDHA MAIYAGLTKK ILDQGNVRDI MFATFDHGGA GGGFENTWGS
GKLMFSAIQT PTVRIHNRPA YNSECHATRE MGIGELNNSY EDAQVADVIW SIGNNPYETQ
TNYFLNHWLP NLNGSTEEKK KQWFAGEPVG PGLMIFVDPR RTTSIAIAEQ TAKDRVLHLD
INPGTDVALF NGLLTYVVQQ GWIAKEFIAQ HTVGFEDAVK TNQMSLADCS RITGVSEDKL
RQAAEWSYKP KAAGKMPRTM HAYEKGIIWG NDNYNIQSSL LDLVIATQNV GRRGTGCVRM
GGHQEGYVRP PHPTGEKIYV DQEIIQGKGR MMTWWGCNNF QTSNNAQALR EVSLRRSQIV
KDAMSKARGA SAAEMVDIIY DATSKGGLFV TSINLYPTKL SEAAHLMLPA AHPGEMNLTS
MNGERRMRLS EKFMDAPGDA LPDCLIAAKA ANTLKAMYEA EGKPEMVKRF SGFDWKTEED
AFNDGFRSAG QPGAEPIDSQ GGSTGVLATY TLLRAAGTNG VQLPIKRVEN GKMIGTAIHY
DDNKFDTKDG KAHFKPAPWN GLPKPVEEQK AKHKFWLNNG RANEVWQSAY HDQYNDFVKS
RYPLAYIELN PGDAQSLGVA AGDVVEVFND YGSTFAMAYP VKDMKPSHTF MLFGYVNGIQ
GDVTTDWVDR NIIPYYKGTW GSVRRIGSIE QYKKTVSTKR RAFDNV
