ALOX_PICAN
ID ALOX_PICAN Reviewed; 664 AA.
AC P04841;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=MOX;
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=2582370; DOI=10.1093/nar/13.9.3063;
RA Ledeboer A.M., Edens L., Maat J., Visser C., Bos J.W., Verrips C.T.;
RT "Molecular cloning and characterization of a gene coding for methanol
RT oxidase in Hansenula polymorpha.";
RL Nucleic Acids Res. 13:3063-3082(1985).
RN [2]
RP SIMILARITY TO DROSOPHILA GLUCOSE DEHYDROGENASE.
RX PubMed=2002763; DOI=10.1093/oxfordjournals.molbev.a040634;
RA Cavener D.R., Krasney P.;
RT "Drosophila glucose dehydrogenase and yeast alcohol oxidase are homologous
RT and share N-terminal homology with other flavoenzymes.";
RL Mol. Biol. Evol. 8:144-150(1991).
RN [3]
RP COFACTOR.
RC STRAIN=ATCC 26012 / NRRL Y-7560 / DL-1, and
RC ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL Y-5445;
RX PubMed=1770353; DOI=10.1099/00221287-137-10-2381;
RA Bystrykh L.V., Dijkhuizen L., Harder W.;
RT "Modification of flavin adenine dinucleotide in alcohol oxidase of the
RT yeast Hansenula polymorpha.";
RL J. Gen. Microbiol. 137:2381-2386(1991).
RN [4]
RP REVIEW.
RX PubMed=1882546; DOI=10.1002/yea.320070302;
RA van der Klei I.J., Harder W., Veenhuis M.;
RT "Biosynthesis and assembly of alcohol oxidase, a peroxisomal matrix protein
RT in methylotrophic yeasts: a review.";
RL Yeast 7:195-209(1991).
RN [5]
RP COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 200838;
RX PubMed=8873445;
RX DOI=10.1002/(sici)1097-0061(199608)12:10<917::aid-yea984>3.0.co;2-4;
RA Evers M.E., Titorenko V., Harder W., ven der Klei I., Veenhuis M.;
RT "Flavin adenine dinucleotide binding is the crucial step in alcohol oxidase
RT assembly in the yeast Hansenula polymorpha.";
RL Yeast 12:917-923(1996).
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:2582370}.
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 Evidence={ECO:0000269|PubMed:1770353, ECO:0000269|PubMed:8873445};
CC Note=May possess two different forms of flavin adenine dinucleotide,
CC classical FAD and so-called modified FAD (mFAD), a stereochemical FAD
CC analog, in which the C2 carbon of the ribityl chain has changed from
CC the R to the S configuration. Conversion of FAD into mFAD was observed
CC both in purified preparations of the enzyme and in cells grown in batch
CC and continuous culture. The relative amount of mFAD in the enzyme
CC varied from 5 to 95%, depending on the growth or storage conditions.
CC The presence of mFAD led to a slight decrease in Vmax and a significant
CC decrease in the KM of alcohol oxidase with respect to methanol.
CC {ECO:0000269|PubMed:1770353, ECO:0000269|PubMed:8873445};
CC -!- PATHWAY: Energy metabolism; methane degradation.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:8873445}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250}.
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; X02425; CAA26278.1; -; Genomic_DNA.
DR PIR; A23010; OXHQAP.
DR AlphaFoldDB; P04841; -.
DR SMR; P04841; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR PhylomeDB; P04841; -.
DR BRENDA; 1.1.3.13; 2587.
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 FAD; Flavoprotein; Methanol utilization; Oxidoreductase; Peroxisome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..664
FT /note="Alcohol oxidase"
FT /id="PRO_0000205581"
FT MOTIF 662..664
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 568
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:0000305"
SQ SEQUENCE 664 AA; 74089 MW; 6A4E3AFD6688BD5D CRC64;
MAIPDEFDII VVGGGSTGCC IAGRLANLDD QNLTVALIEG GENNINNPWV YLPGVYPRNM
RLDSKTATFY SSRPSKALNG RRAIVPCANI LGGGSSINFL MYTRASASDY DDWESEGWST
DELLPLIKKI ETYQRPCNNR DLHGFDGPIK VSFGNYTYPT CQDFLRAAES QGIPVVDDLE
DFKTSHGAEH WLKWINRDLG RRSDSAHAYV HPTMRNKQSL FLITSTKCDK VIIEDGKAVA
VRTVPMKPLN PKKPVSRTFR ARKQIVISCG TISSPLVLQR SGIGAAHHLR SVGVKPIVDL
PGVGENFQDH YCFFTPYYVK PDVPTFDDFV RGDPVAQKAA FDQWYSNKDG PLTTNGIEAG
VKIRPTEEEL ATADEDFRRG YAEYFENKPD KPLMHYSVIS GFFGDHTKIP NGKFMTMFHF
LEYPFSRGFV RITSANPYDA PDFDPGFLND ERDLWPMVWA YKKSRETARR MESFAGEVTS
HHPLFKVDSP ARARDLDLET CSAYAGPKHL TANLYHGSWT VPIDKPTPKN DFHVTSNQVQ
LHSDIEYTEE DDEAIVNYIK EHTETTWHCL GTCSMAPREG SKIAPKGGVL DARLNVYGVQ
NLKVADLSVC PDNVGCNTYS TALTIGEKAA TLVAEDLGYS GSDLDMTIPN FRLGTYEETG
LARF
