ID T0M818_COLGC Unreviewed; 621 AA.
AC T0M818;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:EQB59471.1};
GN ORFNames=CGLO_00131 {ECO:0000313|EMBL:EQB59471.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB59471.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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:EQB59471.1}.
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DR EMBL; AMYD01000037; EQB59471.1; -; Genomic_DNA.
DR AlphaFoldDB; T0M818; -.
DR STRING; 1237896.T0M818; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_6_1_1; -.
DR OMA; AHMSGSC; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000015530; 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; 1.
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:SF115; DEHYDROGENASE XPTC-RELATED; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..621
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004567535"
FT DOMAIN 42..348
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 474..614
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT ACT_SITE 559
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 602
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 119
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 621 AA; 66767 MW; CB77DA0670C0392B CRC64;
MDVTRSFKAA AFAALISSQL AIAEPVSAKF AKRSTAELAD AYDYVIVGGG LSGLVVANRL
TEDPDVSVLV VEYGEFDGSW DVMIPYYASN THPNDMRQLL SIPQPGLNNR TSGVQTGTVV
GGGSTVNGMA FDRGSKADYD AWEELGNPGW NWESLFEYFK KSTTFHLPAQ EYVDKYNFSY
DPSTYGDGPI QVGFPSWQWP DVGIQRDAWI KDLGIPVLND HGAGGNNVGV AQLPQNSEGK
NVTRSTARTG YYDPIAGTRA NINLLIKHYA SKVEFENKKA IGVNVVSRDT GETSLIKANK
EVLLAAGGVQ TPRILQQSGV GPAALLESLN IEVVADLPGV GANYQDHPWM LMLYNYGNPP
ELGSDAMNDP AFFNASEAEY FANRTGPFTH ARGNNIVFLS LQDLTPEYEN LTASIEAQNA
GDFLPEIYSK HPELVEGFLA QRKALAKLYR NPEAGVLEVP FGGFAGAGIA FQKPVSRGTV
SINTTDPDPA TTPVIDFGVL QNPADLEMLV LSIKAMRKFM GSKSIAVRQP LEILPGANIT
SDAAIAEAVR NSLYASFAHP SGTASLQPLE HGGVVDPTLR VYGLEGLRVV DASVIPLIPA
CHLQSTVYAV AEKAADLIKT T
//
