ID   ALOX_CANBO              Reviewed;         663 AA.
AC   Q00922;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Alcohol oxidase;
DE            Short=AO;
DE            Short=AOX;
DE            EC=1.1.3.13;
DE   AltName: Full=Methanol oxidase;
DE            Short=MOX;
GN   Name=AOD1;
OS   Candida boidinii (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea; Ogataea/Candida clade.
OX   NCBI_TaxID=5477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11; 13-18 AND
RP   20-35, AND FUNCTION.
RC   STRAIN=S2;
RX   PubMed=1587486; DOI=10.1016/0378-1119(92)90708-w;
RA   Sakai Y., Tani Y.;
RT   "Cloning and sequencing of the alcohol oxidase-encoding gene (AOD1) from
RT   the formaldehyde-producing asporogeneous methylotrophic yeast, Candida
RT   boidinii S2.";
RL   Gene 114:67-73(1992).
RN   [2]
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=11683419; DOI=10.1242/jcs.114.15.2863;
RA   Stewart M.Q., Esposito R.D., Gowani J., Goodman J.M.;
RT   "Alcohol oxidase and dihydroxyacetone synthase, the abundant peroxisomal
RT   proteins of methylotrophic yeasts, assemble in different cellular
RT   compartments.";
RL   J. Cell Sci. 114:2863-2868(2001).
CC   -!- FUNCTION: Catalyzes the oxidation of methanol to formaldehyde and
CC       hydrogen peroxide, the first step in the methanol utilization pathway
CC       of methylotrophic yeasts. {ECO:0000269|PubMed:1587486}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + O2 = an aldehyde + H2O2;
CC         Xref=Rhea:RHEA:19829, ChEBI:CHEBI:15379, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17478; EC=1.1.3.13;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Energy metabolism; methane degradation.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:11683419}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:11683419}.
CC   -!- INDUCTION: Induced by methanol. Subject to strong carbon catabolite
CC       repression (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal peroxisomal targeting signal (PTS) is essential
CC       for the efficient targeting and import of AOX into peroxisomes via the
CC       PTS1 pathway. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   EMBL; M81702; AAA34321.1; -; Genomic_DNA.
DR   PIR; JC1117; JC1117.
DR   AlphaFoldDB; Q00922; -.
DR   SMR; Q00922; -.
DR   CAZy; AA3; Auxiliary Activities 3.
DR   BioCyc; MetaCyc:MON-13165; -.
DR   BRENDA; 1.1.3.13; 1100.
DR   UniPathway; UPA00147; -.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0047639; F:alcohol oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046188; P:methane catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; PTHR11552; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Methanol utilization;
KW   Oxidoreductase; Peroxisome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1587486"
FT   CHAIN           2..663
FT                   /note="Alcohol oxidase"
FT                   /id="PRO_0000205580"
FT   MOTIF           661..663
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        567
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
FT   BINDING         8..39
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   663 AA;  74082 MW;  BC2E2F595B326AA6 CRC64;
     MAIPEEFDVI VCGGGSTGCV IAGRLANVDE NLKVLLIENG ENNLNNPWVY LPGIYPRNMR
     LDSKTATFYN SRPSKHLNGR RAIVPQANIL GGGSSINFMM YTRASASDYD DWESEGWTTD
     ELLPLMKKFE TYQRPCNNRD VHGFDGPIKV SFGNYTYPQC QDFLRACETQ GIPYVDDLED
     LKTSHGAEQW LKWINRDFGR RSDTAHAFIH STMRNKENLF LMTNTKVDKV IIEDGRAVAV
     RTVPSKPIGD SKVSRTFKAR KQIVVSCGTV SSPMVLQRSG IGEPSKLRAA GVKPIVELPG
     VGRNFQDHFC YFVPYRIKQD SESFDAFVSG DKEAQKSAFD QWYATGAGPL ATNGIEAGVK
     IRPTEAELAT ADKAFQQGWE SYFENKPDKP LMHYSVISGF FGDHTRLPPG KYMTMFHFLE
     YPFSRGWLHI SSDDPYAAPD FDPGFMNDDR DMWPMVWAFK KSRETARRME CFAGEPTAFH
     PHYKVDSPAR ALEQSAEDTK KVAGPLHLTA NLYHGSWSTP IGEADKHDPN HVTSSHINVY
     SKDIQYTKED DEAIENYIKE HAETTWHCLG TNSMAPREGN KNAPEGGVLD PRLNVHGVKG
     LKVADLSVCP DNVGCNTFST ALTIGEKAAV LVAEDLGYSG SELDMEVPQH KLKTYEQTGA
     ARY