ID   ALOX2_KOMPG             Reviewed;         663 AA.
AC   C4R702;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Alcohol oxidase 2;
DE            Short=AO 2;
DE            Short=AOX 2;
DE            EC=1.1.3.13;
DE   AltName: Full=Methanol oxidase 2;
DE            Short=MOX 2;
GN   Name=AOX2; OrderedLocusNames=PAS_chr4_0152;
OS   Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=644223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GS115 / ATCC 20864;
RX   PubMed=19465926; DOI=10.1038/nbt.1544;
RA   De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA   Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT   "Genome sequence of the recombinant protein production host Pichia
RT   pastoris.";
RL   Nat. Biotechnol. 27:561-566(2009).
CC   -!- FUNCTION: Minor isoform of alcohol oxidase, which catalyzes the
CC       oxidation of methanol to formaldehyde and hydrogen peroxide, the first
CC       step in the methanol utilization pathway of methylotrophic yeasts.
CC       {ECO:0000250}.
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; Evidence={ECO:0000250};
CC   -!- PATHWAY: Energy metabolism; methane degradation.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
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; FN392322; CAY71377.1; -; Genomic_DNA.
DR   RefSeq; XP_002493556.1; XM_002493511.1.
DR   AlphaFoldDB; C4R702; -.
DR   SMR; C4R702; -.
DR   STRING; 644223.C4R702; -.
DR   CAZy; AA3; Auxiliary Activities 3.
DR   EnsemblFungi; CAY71377; CAY71377; PAS_chr4_0152.
DR   GeneID; 8201062; -.
DR   KEGG; ppa:PAS_chr4_0152; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_5_1_1; -.
DR   InParanoid; C4R702; -.
DR   OMA; SHASEVW; -.
DR   UniPathway; UPA00147; -.
DR   Proteomes; UP000000314; Chromosome 4.
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.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Methanol utilization; Oxidoreductase; Peroxisome;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..663
FT                   /note="Alcohol oxidase 2"
FT                   /id="PRO_0000425714"
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..38
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   663 AA;  73952 MW;  9A9D2C84161991B2 CRC64;
     MAIPEEFDIL VLGGGSSGSC IAGRLANLDH SLKVGLIEAG ENNLNNPWVY LPGIYPRNMK
     LDSKTASFYT SNPSPHLNGR RAIVPCANIL GGGSSINFMM YTRGSASDYD DFEAEGWKTK
     DLLPLMKKTE TYQRACNNPE IHGFEGPIKV SFGNYTYPVC QDFLRATESQ GIPYVDDLED
     LVTAHGAEHW LKWINRDTGR RSDSAHAFVH STMRNHDNLY LICNTKVDKI IVEDGRAAAV
     RTVPSKPLNA KKPTHKVYRA RKQIVLSCGT ISSPLVLQRS GFGDPIKLRA AGVKPLVNLP
     GVGRNFQDHY CFFSPYRIKP QYESFDDFVR GDANIQKKVF DQWYANGTGP LATNGIEAGV
     KIRPTPEELS QMDESFQEGY REYFEDKPDK PVMHYSIIAG FFGDHTKIPP GKYMTMFHFL
     EYPFSRGSIH ITSPDPYATP DFDPGFMNDE RDMAPMVWSY KKSRETARKM DHFAGEVTSH
     HPLFPYSSEA RAYEMDLETS NAYGGPLNLT AGLAHGSWTQ PLKKPAGRNE GHVTSNQVEL
     HPDIEYDEED DKAIENYIRE HTETTWHCLG TCSIGPREGS KIVKWGGVLD HRSNVYGVKG
     LKVGDLSVCP DNVGCNTYTT ALLIGEKTAT LVGEDLGYTG EALDMTVPQF KLGTYEKTGL
     ARF