ALOX1_KOMPC
ID ALOX1_KOMPC Reviewed; 663 AA.
AC F2QY27; Q9URI8;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=PP7435_Chr4-0130;
OS Komagataella phaffii (strain ATCC 76273 / CBS 7435 / CECT 11047 / NRRL
OS Y-11430 / Wegner 21-1) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=981350;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1;
RX PubMed=2660463; DOI=10.1002/yea.320050306;
RA Koutz P., Davis G.R., Stillman C., Barringer K., Cregg J., Thill G.;
RT "Structural comparison of the Pichia pastoris alcohol oxidase genes.";
RL Yeast 5:167-177(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1;
RX PubMed=21575661; DOI=10.1016/j.jbiotec.2011.04.014;
RA Kueberl A., Schneider J., Thallinger G.G., Anderl I., Wibberg D., Hajek T.,
RA Jaenicke S., Brinkrolf K., Goesmann A., Szczepanowski R., Puehler A.,
RA Schwab H., Glieder A., Pichler H.;
RT "High-quality genome sequence of Pichia pastoris CBS7435.";
RL J. Biotechnol. 154:312-320(2011).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1;
RX PubMed=27388471; DOI=10.1093/femsyr/fow051;
RA Valli M., Tatto N.E., Peymann A., Gruber C., Landes N., Ekker H.,
RA Thallinger G.G., Mattanovich D., Gasser B., Graf A.B.;
RT "Curation of the genome annotation of Pichia pastoris (Komagataella
RT phaffii) CBS7435 from gene level to protein function.";
RL FEMS Yeast Res. 16:0-0(2016).
RN [4]
RP FUNCTION, AND INDUCTION BY METHANOL.
RC STRAIN=ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1;
RX PubMed=2657390; DOI=10.1128/mcb.9.3.1316-1323.1989;
RA Cregg J.M., Madden K.R., Barringer K.J., Thill G.P., Stillman C.A.;
RT "Functional characterization of the two alcohol oxidase genes from the
RT yeast Pichia pastoris.";
RL Mol. Cell. Biol. 9:1316-1323(1989).
RN [5]
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:2657390, 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; Evidence={ECO:0000250};
CC -!- PATHWAY: Energy metabolism; methane degradation.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:9396748}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250}.
CC -!- INDUCTION: Induced by methanol. Subject to strong carbon catabolite
CC repression. {ECO:0000269|PubMed:2657390}.
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; U96967; AAB57849.1; -; Genomic_DNA.
DR EMBL; FR839631; CCA40305.1; -; Genomic_DNA.
DR PDB; 5HSA; X-ray; 2.35 A; A/B/C/D/E/F/G/H=1-663.
DR PDBsum; 5HSA; -.
DR AlphaFoldDB; F2QY27; -.
DR SMR; F2QY27; -.
DR CAZy; AA3; Auxiliary Activities 3.
DR EnsemblFungi; CCA40305; CCA40305; PP7435_CHR4-0130.
DR HOGENOM; CLU_002865_5_1_1; -.
DR BRENDA; 1.1.3.13; 4827.
DR UniPathway; UPA00147; -.
DR Proteomes; UP000006853; 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; FAD; Flavoprotein; Methanol utilization; Oxidoreductase;
KW Peroxisome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..663
FT /note="Alcohol oxidase 1"
FT /id="PRO_0000425715"
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"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 106..110
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:5HSA"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:5HSA"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 236..246
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 256..266
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:5HSA"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 310..318
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 326..330
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 333..346
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:5HSA"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 392..400
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 413..422
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 453..468
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 497..504
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 548..561
FT /evidence="ECO:0007829|PDB:5HSA"
FT STRAND 599..603
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 618..635
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 640..644
FT /evidence="ECO:0007829|PDB:5HSA"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:5HSA"
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
