AIOA_ALCFA
ID AIOA_ALCFA Reviewed; 826 AA.
AC Q7SIF4; Q6WB60; Q9R5F9;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Arsenite oxidase subunit AioA;
DE Short=AOI;
DE EC=1.20.9.1;
DE AltName: Full=Arsenite oxidase Mo-pterin subunit;
GN Name=aioA; Synonyms=aoxB, asoA;
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] {ECO:0007744|PDB:1G8J, ECO:0007744|PDB:1G8K}
RP PROTEIN SEQUENCE OF 2-826, X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) IN
RP COMPLEX WITH MO-BIS-MGD AND IRON-SULFUR CLUSTER, AND COFACTOR.
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 2-18.
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=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000269|PubMed:11250197};
CC Note=Binds 1 [3Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:11250197};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000269|PubMed:11250197};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000269|PubMed:11250197};
CC -!- SUBUNIT: Heterodimer consisting of a large and a small subunit.
CC {ECO:0000269|PubMed:11250197}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AY297781; AAQ19838.1; -; Genomic_DNA.
DR PIR; B45138; B45138.
DR PDB; 1G8J; X-ray; 2.03 A; A/C=4-825.
DR PDB; 1G8K; X-ray; 1.64 A; A/C/E/G=4-825.
DR PDBsum; 1G8J; -.
DR PDBsum; 1G8K; -.
DR AlphaFoldDB; Q7SIF4; -.
DR SMR; Q7SIF4; -.
DR TCDB; 5.A.3.6.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR KEGG; ag:AAQ19838; -.
DR BioCyc; MetaCyc:MON-10727; -.
DR BRENDA; 1.20.9.1; 232.
DR EvolutionaryTrace; Q7SIF4; -.
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 1: Evidence at protein level;
KW 3D-structure; 3Fe-4S; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Molybdenum; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11250197,
FT ECO:0000269|PubMed:1331097"
FT CHAIN 2..826
FT /note="Arsenite oxidase subunit AioA"
FT /id="PRO_0000063240"
FT BINDING 22
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000269|PubMed:11250197,
FT ECO:0007744|PDB:1G8J, ECO:0007744|PDB:1G8K"
FT BINDING 25
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000269|PubMed:11250197,
FT ECO:0007744|PDB:1G8J, ECO:0007744|PDB:1G8K"
FT BINDING 29
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000269|PubMed:11250197,
FT ECO:0007744|PDB:1G8J, ECO:0007744|PDB:1G8K"
FT BINDING 196
FT /ligand="substrate"
FT BINDING 204
FT /ligand="substrate"
FT BINDING 420
FT /ligand="substrate"
FT BINDING 424
FT /ligand="substrate"
FT SITE 100
FT /note="Involved in charge transfer"
FT /evidence="ECO:0000305"
FT CONFLICT 2..3
FT /note="SR -> GC (in Ref. 2; AA sequence and 3; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="V -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78..83
FT /note="NGRRYN -> DGARYD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="K -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="K -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="E -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 826
FT /note="A -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1G8K"
FT TURN 93..97
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1G8K"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 137..154
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:1G8K"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 241..246
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:1G8K"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 283..292
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 307..321
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 326..332
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 336..342
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 394..407
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 441..446
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 467..486
FT /evidence="ECO:0007829|PDB:1G8K"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:1G8J"
FT HELIX 493..504
FT /evidence="ECO:0007829|PDB:1G8K"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 510..517
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 520..523
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 526..531
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 539..542
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 564..581
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 585..590
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 599..605
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 607..609
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 623..628
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 631..637
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 642..645
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:1G8K"
FT TURN 651..653
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:1G8J"
FT STRAND 672..675
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 686..694
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 696..702
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 714..716
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 718..723
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 728..731
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 733..738
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 745..750
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 755..762
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 770..774
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 778..780
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 782..785
FT /evidence="ECO:0007829|PDB:1G8K"
FT STRAND 802..810
FT /evidence="ECO:0007829|PDB:1G8K"
FT HELIX 812..817
FT /evidence="ECO:0007829|PDB:1G8K"
SQ SEQUENCE 826 AA; 92395 MW; 56AFA94C70E82575 CRC64;
MSRPNDRITL PPANAQRTNM TCHFCIVGCG YHVYKWPELQ EGGRAPEQNA LGLDFRKQLP
PLAVTLTPAM TNVVTEHNGR RYNIMVVPDK ACVVNSGLSS TRGGKMASYM YTPTGDGKQR
LKAPRLYAAD QWVDTTWDHA MALYAGLIKK TLDKDGPQGV FFSCFDHGGA GGGFENTWGT
GKLMFSAIQT PMVRIHNRPA YNSECHATRE MGIGELNNAY EDAQLADVIW SIGNNPYESQ
TNYFLNHWLP NLQGATTSKK KERFPNENFP QARIIFVDPR ETPSVAIARH VAGNDRVLHL
AIEPGTDTAL FNGLFTYVVE QGWIDKPFIE AHTKGFDDAV KTNRLSLDEC SNITGVPVDM
LKRAAEWSYK PKASGQAPRT MHAYEKGIIW GNDNYVIQSA LLDLVIATHN VGRRGTGCVR
MGGHQEGYTR PPYPGDKKIY IDQELIKGKG RIMTWWGCNN FQTSNNAQAL REAILQRSAI
VKQAMQKARG ATTEEMVDVI YEATQNGGLF VTSINLYPTK LAEAAHLMLP AAHPGEMNLT
SMNGERRIRL SEKFMDPPGT AMADCLIAAR IANALRDMYQ KDGKAEMAAQ FEGFDWKTEE
DAFNDGFRRA GQPGAPAIDS QGGSTGHLVT YDRLRKSGNN GVQLPVVSWD ESKGLVGTEM
LYTEGKFDTD DGKAHFKPAP WNGLPATVQQ QKDKYRFWLN NGRNNEVWQT AYHDQYNSLM
QERYPMAYIE MNPDDCKQLD VTGGDIVEVY NDFGSTFAMV YPVAEIKRGQ TFMLFGYVNG
IQGDVTTDWT DRNIIPYYKG TWGDIRKVGS MEEFKRTVSF KSRRFA
