ID A0A135RRD2_9PEZI Unreviewed; 608 AA.
AC A0A135RRD2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:KXH26272.1};
GN ORFNames=CSIM01_03650 {ECO:0000313|EMBL:KXH26272.1};
OS Colletotrichum simmondsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH26272.1, ECO:0000313|Proteomes:UP000070328};
RN [1] {ECO:0000313|EMBL:KXH26272.1, ECO:0000313|Proteomes:UP000070328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS122122 {ECO:0000313|EMBL:KXH26272.1,
RC ECO:0000313|Proteomes:UP000070328};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
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:KXH26272.1}.
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DR EMBL; JFBX01000876; KXH26272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135RRD2; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000070328; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..608
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007801097"
FT DOMAIN 111..134
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 292..306
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 545
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 588
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 253
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 608 AA; 64979 MW; 19EB416DD5997112 CRC64;
MLVKSSLALA SAALVLGAAS SSSFSSQPYE DTYDYIVVGG GTAGVAVAAR LSEGLPASKI
LLIEAGPAVW DEPKINVPGM KGSTLATKYD WNFTTVPQTN VNSRTFTVNR GKVLGGSSAL
NLMSYDRAAA AEYDSWEALG NPGWNWETMI AAMKKSENFT GINTDTYGSE GVGDSGPVKA
VINRIIPEHQ KTWIPTMNAL GIDSNLESLG GDPLGVMYQP SSIDPTHYNR SYSANAYVPI
AGSNLEILSD TTVIKVNLGK ATSNSTLQAA AGVTLSDGTV ISAKKEVILS AGSIQSPGLL
ELSGIGQSSV LNASGIEQVI DLPGVGENLQ DHLRIQSSYQ LKDNYTSFDI LRSNATYAAE
QLALWNAGQV SLYDYTGSGY TFTTWAQAIG NDSRLISLAK EAAGEDPSIV DQKKLEFMAD
PSIPQLEVIF SDGYTGVKGY PTSTSPLFGE GFFTLIAAIM HPMSRGNIHI NPANTTGKPV
INPNYFAHEH DLEAAIQAIK YCRKIATTEP MRYIWENEYE PGLDVVQTEE QWKQFALNTT
LSIFHPVGTC SMLPKEVGGV VDSDLKVYGT SNLRIIDASV IPLLISAHVQ TAVYGIAEIA
AERIIADA
//
