ID A0A135UHX0_9PEZI Unreviewed; 609 AA.
AC A0A135UHX0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:KXH59998.1};
GN ORFNames=CNYM01_08148 {ECO:0000313|EMBL:KXH59998.1};
OS Colletotrichum nymphaeae SA-01.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH59998.1, ECO:0000313|Proteomes:UP000070054};
RN [1] {ECO:0000313|EMBL:KXH59998.1, ECO:0000313|Proteomes:UP000070054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA-01 {ECO:0000313|EMBL:KXH59998.1,
RC ECO:0000313|Proteomes:UP000070054};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KXH59998.1}.
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DR EMBL; JEMN01000563; KXH59998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135UHX0; -.
DR Proteomes; UP000070054; 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; 2.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..609
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007804869"
FT DOMAIN 333..347
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 136
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 609 AA; 66382 MW; 6D4590988C1651FF CRC64;
MNSTLALLVF LSWVLLPISN ALHITDETID KFLLEEYDYI VVGGGLSGLV VANRLSEDKN
SKSFFFLIIR ALFDIADRTP ATVLVIESGE LDGRESRVIA PGYIGLTPPS PYGKSVTTAS
QTFLDGKTRG ISQGRVIGGG SVTNGMCWTR GSAADFDAWE ELGNRGWGWK SLLPYFKKVE
TYTTNVNQDT QDRLNIHPDM SVHGTEGPIN VAYPEYFYNS SDHIIHGLSE MGIHLSGDLN
TGDPTGAMMV PSSMSPTNQT RSDARTGYFD PAISRSNLHV VTGQTATRLI VGLPGSLAKE
GTRRRVVGVD FSSEPLGINR TITTKREVIL AAGAIQSPTL LQVSGIGPRK VLESLNISVQ
IDLPGVGNNF QDHPMAQFEF DYSNSSIFTS RDLTGAAFDS ALDTFVTNHT GPLTAPLINT
VAFPSLQYHA SEWKSLLQHA TNQSSFTFLP LDTPPTVQSG YTRQKRLVLA HLARSDVGAY
ELLAASWGQM SIANQKPLSR GTVRPRSGSI FDGPVVDPRY CADPLDCKII RLGLQLIQRL
MRTEAMTPLQ PVVEDPRLNS TDETELMAAL KPLVGTEYHP SGTTSMMPLE LGGVVDAQLM
VLYRIQRDT
//
