ID H1V6Z9_COLHI Unreviewed; 507 AA.
AC H1V6Z9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=alcohol oxidase {ECO:0000256|ARBA:ARBA00013077};
DE EC=1.1.3.13 {ECO:0000256|ARBA:ARBA00013077};
GN ORFNames=CH063_00212 {ECO:0000313|EMBL:CCF36001.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF36001.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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 Evidence={ECO:0000256|ARBA:ARBA00001411};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- PATHWAY: Energy metabolism; methane degradation.
CC {ECO:0000256|ARBA:ARBA00005144}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix
CC {ECO:0000256|ARBA:ARBA00004253}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; CACQ02001791; CCF36001.1; -; Genomic_DNA.
DR AlphaFoldDB; H1V6Z9; -.
DR STRING; 759273.H1V6Z9; -.
DR EnsemblFungi; CCF36001; CCF36001; CH063_00212.
DR VEuPathDB; FungiDB:CH63R_13520; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_5_1_1; -.
DR Proteomes; UP000007174; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF119; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Methanol utilization {ECO:0000256|ARBA:ARBA00023095};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT DOMAIN 109..123
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 412..413
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCF36001.1"
SQ SEQUENCE 507 AA; 56591 MW; 9BFE909D5438C20A CRC64;
DDFLRAASSQ GIPVVDDLQD LTTGHGAEHW LKWINRDTGR RSDSAHAYIH ATRAKHSNLY
LACNTKVDKV IIENGRAVAV HTIPSKPLDP NELKGRTFRA RKQIVISGGT LSSPLILQRS
GVGDPEKLRR AGVKPIVDLP GVGLNFQDHY LTFSTYRAKP GTESFDDFVR GDPEVQKRVF
DEWNIKGTGP LATNGIEAGV KIRPTPEELK EFERWPTPHF KDGWKSYFEN KPDKPVMHYS
VIAGWFGDHM VMPPGNFFTM FHFLEYPFSR GSTHIVSPNP YDAPDFDAGF MNDERDMVPM
VWGYIKSRET ARRMDAYAGE VANMHPVFAY DSPARARDLN LADTNKYALP GNLTAGIQHG
SWTQPLNEAE RKADIKRTLN AHCVDGREPL KYSDADIKEV EEWVKRHVET TWHSLGTCSM
APKEGNSIVK HGVLDERLNV HGVKGLKVAD LSICPDNVGC NTYSTALLIG EKAAVLVAED
LGYSGEALEM KVPTYHAPGE FVLNSRL
//
