ID A0A1Z5TTF4_HORWE Unreviewed; 639 AA.
AC A0A1Z5TTF4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=BTJ68_00941 {ECO:0000313|EMBL:OTA39201.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA39201.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA39201.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA39201.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) 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:OTA39201.1}.
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DR EMBL; MUNK01000005; OTA39201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5TTF4; -.
DR STRING; 1157616.A0A1Z5TTF4; -.
DR VEuPathDB; FungiDB:BTJ68_00941; -.
DR InParanoid; A0A1Z5TTF4; -.
DR OrthoDB; 858083at2759; -.
DR Proteomes; UP000194280; 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:SF138; DEHYDROGENASE PKFF-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.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..639
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012532176"
FT DOMAIN 339..353
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT ACT_SITE 572
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 616
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 617..618
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 639 AA; 69220 MW; 0C2FB8A7F055B834 CRC64;
MLCDFVRRAV LTSLFAVAVN AQYEPRFASN GSSAFHERLE ALGLLGSHFG TVDVPQTFDY
IVVGGGTAGL TIARRLAEHH SVAVIEAGSF YEINNANLTE IPAQASYYLG KDPALRNPLI
DWNQHTTPQE GLLGDPVLYP QGRTLGGGST RNFLWYQRGS AGSYSKWADE VGDDSYAFEN
FLEYFKKSVD FTPLANGTRP ANATPKYDES YFSSYGGPLQ VSFPEFASPS ASWLALGLDA
IGLSELPACM MDGNLLGWAW ITNTIDPYLQ IRSTSERSFL REAIRKTYNL LVYQNTLAKK
IHFTSDGVAN AVEIEAAAYG SGSVTYNLNA KKEVIVSAGT FRSPQLLMVS GIGPAENLRE
NNIDVIADRP GVGQNLWDHL FFGPAYEVNT VTHSWLANPE YAAQAANEYI TNHTGILTNV
GGDLIAFEKL PNGTISDATR MDLDDTFGSD WPDIELLSLD AYTGTLNDFL GGAPDMKNYT
AMCVALVAPF SRGNVSISSN DTAVHPLVNP NWLTDTRDQE VAVAGFKRAR SLFEAPGVQP
VLVGSEAYPG QNVSSDEEIL SMLRASSDTI HHAAGTCRMG KSDDSMAVLD SHARVIGVHG
LRVVDASAFP LLPPGHPQST VYALAEKIAA DILRENESI
//
