ID A0A0F4Z5T4_TALEM Unreviewed; 564 AA.
AC A0A0F4Z5T4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glucose-methanol-choline (Gmc) oxidoreductase {ECO:0000313|EMBL:KKA25461.1};
GN ORFNames=T310_0485 {ECO:0000313|EMBL:KKA25461.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA25461.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA25461.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA25461.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) 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, 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:KKA25461.1}.
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DR EMBL; LASV01000020; KKA25461.1; -; Genomic_DNA.
DR RefSeq; XP_013332073.1; XM_013476619.1.
DR AlphaFoldDB; A0A0F4Z5T4; -.
DR STRING; 1408163.A0A0F4Z5T4; -.
DR GeneID; 25312539; -.
DR OrthoDB; 3073733at2759; -.
DR Proteomes; UP000053958; 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:SF134; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958}.
FT DOMAIN 83..106
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT ACT_SITE 497
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT ACT_SITE 541
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT BINDING 93..96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 230
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 496..497
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 564 AA; 62295 MW; 35A11B953EB21C84 CRC64;
MASTFDFIVV GSGPAGSVIA SGLARTPKSP KVLLLEAGGK NDDRNLRVDG QRWLTFQNKP
MNFGYKTTAQ ENLNNREIDY SRGKGIGGSS AINFGVYSVG ARDDYEEWAR IVGDDDYRWE
HIQARYKSLE TFHGDIPPGV DKKYAAPKAS DHGSSGPLHV GFAAEWERDL PPLLDVFEQA
GFPLNPDHNS GNPIGMSVLI NSAYKGVRST AGDLLASPPE NLTIVTDAPV QRVILEGKKA
VGVESNGKKY FASKEVILSA GALDAPRILM HSGIGPAEQL EKYNIPVVHN VPAIGKGLRD
HSFIPLVYTR KDNSTDRAAF FGDQKAMDDA LEQWKREGTG PWAKFACELG VGWFKLDRLV
ASKEFQELPA EEKNYLLQET VPHYEILTHF PVHWFIPNFP KDALSYSCLL VFLYNAQSRG
EVTLQSSDPN VPLRFDPKFL THPFDRRAAI ESLRDAFRIA KHDAYTKDNV AEMVAPKSDS
DEDLLEYWRQ NMSSSWHMTG TVKMGKPGDA DAAVDNNFRL MGIEGLRVAD MSVVPVLASC
HVQAVAYVTG ATCAEKLIKE YNLA
//