AIOB_ALCFA
ID AIOB_ALCFA Reviewed; 175 AA.
AC Q7SIF3; Q6WB59; Q9R5G0;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Arsenite oxidase subunit AioB;
DE Short=AOII;
DE EC=1.20.9.1;
DE AltName: Full=Arsenite oxidase Rieske subunit;
DE Flags: Precursor;
GN Name=aioB; Synonyms=aoxA, asoB;
OS Alcaligenes faecalis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Alcaligenes.
OX NCBI_TaxID=511;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CCUG 2071 / LMG 3368 / NCIMB 8687;
RA Silver S., Phung L.T., Malo B.J.;
RT "Genes for arsenite oxidation from Alcaligenes faecalis.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), AND PROTEIN SEQUENCE OF 43-175.
RC STRAIN=CCUG 2071 / LMG 3368 / NCIMB 8687;
RX PubMed=11250197; DOI=10.1016/s0969-2126(01)00566-4;
RA Ellis P.J., Conrads T., Hille R., Kuhn P.;
RT "Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes
RT faecalis in two crystal forms at 1.64 A and 2.03 A.";
RL Structure 9:125-132(2001).
RN [3]
RP PROTEIN SEQUENCE OF 44-61.
RC STRAIN=CCUG 2071 / LMG 3368 / NCIMB 8687;
RX PubMed=1331097; DOI=10.1016/s0021-9258(18)35891-5;
RA Anderson G.L., Williams J., Hille R.;
RT "The purification and characterization of arsenite oxidase from Alcaligenes
RT faecalis, a molybdenum-containing hydroxylase.";
RL J. Biol. Chem. 267:23674-23682(1992).
RN [4]
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 Note=Binds 1 [2Fe-2S] cluster per subunit.;
CC -!- SUBUNIT: Heterodimer consisting of a large and a small subunit.
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; AY297781; AAQ19839.1; -; Genomic_DNA.
DR PIR; A45138; A45138.
DR PDB; 1G8J; X-ray; 2.03 A; B/D=43-175.
DR PDB; 1G8K; X-ray; 1.64 A; B/D/F/H=43-175.
DR PDBsum; 1G8J; -.
DR PDBsum; 1G8K; -.
DR AlphaFoldDB; Q7SIF3; -.
DR SMR; Q7SIF3; -.
DR TCDB; 5.A.3.6.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR KEGG; ag:AAQ19839; -.
DR BioCyc; MetaCyc:MON-10728; -.
DR BRENDA; 1.20.9.1; 232.
DR EvolutionaryTrace; Q7SIF3; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; IPR005805; Rieske_Fe-S_prot_C.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR PRINTS; PR00162; RIESKE.
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 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Direct protein sequencing; Disulfide bond; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase; Signal.
FT SIGNAL 1..32
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 33..175
FT /note="Arsenite oxidase subunit AioB"
FT /id="PRO_0000127798"
FT DOMAIN 62..158
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 102
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 120
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 123
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT DISULFID 107..122
FT CONFLICT 45
FT /note="T -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="Q -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="T -> C (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="Q -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="A -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="K -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="V -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="S -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..93
FT /note="NN -> DD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="K -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="K -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..143
FT /note="EN -> AD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="E -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1G8K"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1G8K"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1G8K"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1G8K"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1G8K"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1G8K"
SQ SEQUENCE 175 AA; 18275 MW; 9284053031A809E7 CRC64;
MSDTINLTRR GFLKVSGSGV AVAATLSPIA SANAQKAPAD AGRTTLQYPA TQVSVAKNLK
ANEPVSFTYP DTSSPCVAVK LGSPVPGGVG PNNDIVAYSV LCTHMGCPTS YDKSSKTFKC
PCHFTEFDAE KAGQMICGQA TENLPRVLLR YDEASDALTA VGVDGLIYGR QANVI
