ALOX1_KOMPG
ID ALOX1_KOMPG Reviewed; 663 AA.
AC P04842; C4R917;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Alcohol oxidase 1;
DE Short=AO 1;
DE Short=AOX 1;
DE EC=1.1.3.13;
DE AltName: Full=Methanol oxidase 1;
DE Short=MOX 1;
GN Name=AOX1; OrderedLocusNames=PAS_chr4_0821;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 2-19, AND INDUCTION
RP BY METHANOL.
RX PubMed=3889590; DOI=10.1128/mcb.5.5.1111-1121.1985;
RA Ellis S.B., Brust P.F., Koutz P.J., Waters A.F., Harpold M.M.,
RA Gingeras T.R.;
RT "Isolation of alcohol oxidase and two other methanol regulatable genes from
RT the yeast Pichia pastoris.";
RL Mol. Cell. Biol. 5:1111-1121(1985).
RN [2]
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).
RN [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1, and
RC GS115 / ATCC 20864;
RX PubMed=9396748; DOI=10.1083/jcb.139.6.1419;
RA Waterham H.R., Russell K.A., Vries Y., Cregg J.M.;
RT "Peroxisomal targeting, import, and assembly of alcohol oxidase in Pichia
RT pastoris.";
RL J. Cell Biol. 139:1419-1431(1997).
CC -!- FUNCTION: Major 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:0000269|PubMed:9396748}.
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. Assembles only after import into the peroxisomal
CC matrix, fails to assemble in the cytoplasm.
CC {ECO:0000269|PubMed:9396748}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:9396748}.
CC -!- INDUCTION: Induced by methanol. Subject to strong carbon catabolite
CC repression. {ECO:0000269|PubMed:3889590}.
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:0000269|PubMed:9396748}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; X02646; CAA26484.1; -; Genomic_DNA.
DR EMBL; FN392322; CAY72092.1; -; Genomic_DNA.
DR PIR; A23483; A23483.
DR RefSeq; XP_002494271.1; XM_002494226.1.
DR PDB; 5I68; EM; 3.37 A; A=1-663.
DR PDBsum; 5I68; -.
DR AlphaFoldDB; P04842; -.
DR SMR; P04842; -.
DR STRING; 644223.P04842; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR EnsemblFungi; CAY72092; CAY72092; PAS_chr4_0821.
DR GeneID; 8201223; -.
DR KEGG; ppa:PAS_chr4_0821; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_5_1_1; -.
DR OMA; RACNNRD; -.
DR BRENDA; 1.1.3.13; 4827.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein;
KW Methanol utilization; Oxidoreductase; Peroxisome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3889590"
FT CHAIN 2..663
FT /note="Alcohol oxidase 1"
FT /id="PRO_0000205582"
FT MOTIF 661..663
FT /note="Microbody targeting signal"
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"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:5I68"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:5I68"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:5I68"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 256..266
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:5I68"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:5I68"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 310..318
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:5I68"
FT TURN 328..331
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 392..400
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 413..422
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 454..467
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 497..504
FT /evidence="ECO:0007829|PDB:5I68"
FT TURN 534..536
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 548..561
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:5I68"
FT STRAND 599..603
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:5I68"
FT HELIX 618..635
FT /evidence="ECO:0007829|PDB:5I68"
FT TURN 655..657
FT /evidence="ECO:0007829|PDB:5I68"
SQ SEQUENCE 663 AA; 73898 MW; 2206F9319CDC96ED CRC64;
MAIPEEFDIL VLGGGSSGSC IAGRLANLDH SLKVGLIEAG ENNLNNPWVY LPGIYPRNMK
LDSKTASFYT SNPSPHLNGR RAIVPCANVL GGGSSINFMM YTRGSASDYD DFQAEGWKTK
DLLPLMKKTE TYQRACNNPD IHGFEGPIKV SFGNYTYPVC QDFLRASESQ GIPYVDDLED
LVTAHGAEHW LKWINRDTGR RSDSAHAFVH STMRNHDNLY LICNTKVDKI IVEDGRAAAV
RTVPSKPLNP KKPSHKIYRA RKQIVLSCGT ISSPLVLQRS GFGDPIKLRA AGVKPLVNLP
GVGRNFQDHY CFFSPYRIKP QYESFDDFVR GDAEIQKRVF DQWYANGTGP LATNGIEAGV
KIRPTPEELS QMDESFQEGY REYFEDKPDK PVMHYSIIAG FFGDHTKIPP GKYMTMFHFL
EYPFSRGSIH ITSPDPYAAP DFDPGFMNDE RDMAPMVWAY KKSRETARRM DHFAGEVTSH
HPLFPYSSEA RALEMDLETS NAYGGPLNLS AGLAHGSWTQ PLKKPTAKNE GHVTSNQVEL
HPDIEYDEED DKAIENYIRE HTETTWHCLG TCSIGPREGS KIVKWGGVLD HRSNVYGVKG
LKVGDLSVCP DNVGCNTYTT ALLIGEKTAT LVGEDLGYSG EALDMTVPQF KLGTYEKTGL
ARF
