ID N4VAA4_COLOR Unreviewed; 669 AA.
AC N4VAA4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, 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 Name=AOX1-0 {ECO:0000313|EMBL:TDZ24799.1};
GN ORFNames=Cob_v002543 {ECO:0000313|EMBL:TDZ24799.1};
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ24799.1, ECO:0000313|Proteomes:UP000014480};
RN [1] {ECO:0000313|Proteomes:UP000014480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2] {ECO:0000313|Proteomes:UP000014480}
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TDZ24799.1}.
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DR EMBL; AMCV02000004; TDZ24799.1; -; Genomic_DNA.
DR AlphaFoldDB; N4VAA4; -.
DR STRING; 1213857.N4VAA4; -.
DR EnsemblFungi; ENH84998; ENH84998; Cob_06948.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_5_1_1; -.
DR OrthoDB; 2392848at2759; -.
DR Proteomes; UP000014480; 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; 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:UP000014480}.
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 574..575
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 669 AA; 74442 MW; 153C3EC906B393A0 CRC64;
MSGALPDEFD IIVCGGGSTG CVVAGRLANL DHKLSVLLIE AGENNLNNPW VFRPGIYPRN
MKLDSKTATF YESRPSKHLS GRSAIVPCAN ILGGGSSINF MMYTRASASD YDDFQAKGWS
TKELLPLMKK HETYQRASHN RDVHGFDGPI KVSFGNYTYP IKDDFLRAAE SQGIPVVDDL
QDLSTGHGAE HWLKWINRDT GRRSDSAHAY VHATRAVHSN LYLACNTKID KVIIENGRAV
GVRTIPTKPL HPNQLKGRTF RARKQIVVSG GTLSSPLILQ RSGVGDPEKL RRAGVEPIVD
LPGVGLNFQD HYLTFSTYRA KPGTESFDDF VRGDPEVQKR VFDEWNIKGT GPLATNGIEA
GVKIRPTPEE LQEFERWPTP HFKDGWKSYF ENKPDKPVMH YSVIAGWFGD HMIMPPGKFF
SMFHFLEYPF SRGSTHITSP DPYAAPDFDA GFMNDERDMV PMVWGYIKSR ETARRMDAYA
GEVANMHPFF AYDSDARARD LDLPTTNAYA LPGNLSAGIQ HGSWTQPLNE ADRKCDVKKI
LSSNRHNPRD ELKYSAEDIK AVEEWVKRHV ETTWHSLGTC SMAPREGNSI VKHGVVDERL
NVHGVKGLKV ADLSICPDNV GCNTYSTALL IGEKAATLVA EDLGYSGAAL EMRVPTYHAP
GEFVLNSRL
//
