ID E3QV85_COLGM Unreviewed; 669 AA.
AC E3QV85;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=alcohol oxidase {ECO:0000256|ARBA:ARBA00013077};
DE EC=1.1.3.13 {ECO:0000256|ARBA:ARBA00013077};
GN ORFNames=GLRG_09919 {ECO:0000313|EMBL:EFQ34775.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
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, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; GG697383; EFQ34775.1; -; Genomic_DNA.
DR RefSeq; XP_008098795.1; XM_008100604.1.
DR AlphaFoldDB; E3QV85; -.
DR STRING; 645133.E3QV85; -.
DR EnsemblFungi; EFQ34775; EFQ34775; GLRG_09919.
DR GeneID; 24415284; -.
DR VEuPathDB; FungiDB:GLRG_09919; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_5_1_1; -.
DR OrthoDB; 2392848at2759; -.
DR Proteomes; UP000008782; 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; 1.
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; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Methanol utilization {ECO:0000256|ARBA:ARBA00023095};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782}.
FT DOMAIN 89..112
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 271..285
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 229
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 574..575
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 669 AA; 74497 MW; 9FA3A926BFD3F175 CRC64;
MSGSIPDEFD IIVCGGGSCG CVVAGRLANL DHNLKVLLIE NGESNLNNPW VFRPGIYPRN
MKLDSKTATF YESRPSKHLS GRSAIVPCAN ILGGGSSINF MMYTRASASD YDDFQAKGWS
TKELLPLMKK HETYQRASHN RDIHGFDGPI KVSFGNYTYP IKDDFLRAAS SQGIPVVDDL
QDLTTGHGAE HWLKWINRDT GRRSDSAHAY IHATRAKHSN LYLACNTKVD KVIIENGRAV
AVQTVPSKPL DPSELKGRTF RARKQIVVSG GTLSSPLILQ RSGVGDPEKL RRAGVEPIVD
LPGVGLNFQD HYLTFSTYRA KPGTESFDDF VRGDPEVQKR VFDEWNIKGT GPLATNGIEA
GVKIRPTPEE LREFERWPTP HFKDGWKSYF ENKPDKPVMH YSVIAGWFGD HMVMPPGNFF
TMFHFLEYPF SRGSTHIVSP NPYDSPDFDA GFMNDERDMV PMVWGYIKSR ETARRMDAYA
GEVANMHPFF SYDSDACARD LNLPDTNKYA LPGNLSAGIQ HGSWTQPLNE ADRKADLKKT
LSAHCVDVRE PLKYSNEDIK AVEEWVKRHV ETTWHSLGTC SMAPKEGNSI VKHGVLDERL
NVHGVKGLKV ADLSICPDNV GCNTYSTALL IGEKAAILVA EDLGYSGEAL EMKVPTYHAP
GEFVLHSRL
//
