ID   A0A093Y2K2_9PEZI        Unreviewed;       592 AA.
AC   A0A093Y2K2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=V490_01924 {ECO:0000313|EMBL:KFX99148.1};
OS   Pseudogymnoascus sp. VKM F-3557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX99148.1, ECO:0000313|Proteomes:UP000029320};
RN   [1] {ECO:0000313|EMBL:KFX99148.1, ECO:0000313|Proteomes:UP000029320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX99148.1,
RC   ECO:0000313|Proteomes:UP000029320};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-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:KFX99148.1}.
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DR   EMBL; JPJS01000535; KFX99148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093Y2K2; -.
DR   STRING; 1437433.A0A093Y2K2; -.
DR   HOGENOM; CLU_002865_6_0_1; -.
DR   Proteomes; UP000029320; 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; 4.10.450.10; Glucose Oxidase, domain 2; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027424; Glucose_Oxidase_domain_2.
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:SF201; 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.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029320};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..592
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001889321"
FT   DOMAIN          108..131
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          301..315
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        529
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        572
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         114
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   592 AA;  63842 MW;  EB6F7030206B79F6 CRC64;
     MIAPSYLGTW AFVLVAPALL VSHCAALKSE FDFIIVGGGT AGLTLANRLT EFPHVTVAVI
     EAGGEVNNNP NVTDPNNLFV ALGTAIDWQY ESANQTHAGD RKIPFSAGKA LGGTSTINGM
     TYVRAEKAQI DAWEKLGNSG WSWDDLFPYY LKSERFDSPT SAQVKAGATY ASRYHGKKGS
     LNVGYGFGLL NGTYHEVVEQ TWNNLGLPTS LDVNGGNVRG FTVWQSTIDR DANRREDAGR
     AYYYPVQSRP NLHVFLNTIA NRITWRESKS ECAVAGGVEI TAADGTVTTL NAKREVILSA
     GSLRSPTILE LSGIGNPSIL NKAGIPVKVN LPAVGENLQD QPNSQIIMTS NTTFNGSIPY
     VAFGSASDIL DSLPKNVNLT AWAEKVAVAI DHAISVSSLE QIFRIQYKLI SNGVVDAESI
     LQTSYNLGYG PSGLVASAFW LLLPFSRGNV HISSSDPLAY PVLNPNFFLV DFDVEVQVAI
     AKWTRKFWDT APIQGLATET TPGFDVLPKD ASDEQWANWV KTTFGSNSHP LGTAAMMSRE
     LGGVVDSELR VYGTQNVRVV DASVIPTQVS GHLTSTIYAI AEKVADVIKR SI
//