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Database: UniProt
Entry: A0A0F4Z5T4_TALEM
LinkDB: A0A0F4Z5T4_TALEM
Original site: A0A0F4Z5T4_TALEM 
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
//
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