ID   A0A094I9P1_9PEZI        Unreviewed;       687 AA.
AC   A0A094I9P1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V502_01168 {ECO:0000313|EMBL:KFZ24355.1};
OS   Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ24355.1, ECO:0000313|Proteomes:UP000029308};
RN   [1] {ECO:0000313|EMBL:KFZ24355.1, ECO:0000313|Proteomes:UP000029308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
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|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:KFZ24355.1}.
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DR   EMBL; JPKE01000447; KFZ24355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094I9P1; -.
DR   STRING; 1420915.A0A094I9P1; -.
DR   HOGENOM; CLU_002865_4_1_1; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000029308; 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:SF213; DEHYDROGENASE, PUTATIVE-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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..687
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001904182"
FT   DOMAIN          305..414
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          520..661
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   BINDING         155..158
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         320
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   687 AA;  73684 MW;  E86BFE427E547F4A CRC64;
     MLVLRTISFF AIAASLVASV PTTSDNSEKR DASAADLDSY EYIVVGSGAG GGTLAARLAV
     NGAKVLLLEA GDDQGESVQE SIPAFFAAAS EYEPMSWDFF VRHYPDDTRE QLNSKATYET
     PSGETYVGTS PPAGSTFKGI WYPRAATLGG CAAHNALVTV YPHQEDWSHI QGLTGDASWA
     PANMRKYWKL LEDNQYLANA SAIEKAGHGF DGWLGVSEAA DELLMQDPKL TAIYSAVSAV
     THGTPQKTIE TESDLDDIFP IDMNTDYVGR DSIDGVYRLP IAARNSIRSS PRDFLLATAN
     AVNADGSKKY ALEIKLNTFV TKIRFSNDTT PVAIGVDFLD GASQYSADPR ASSATAGTPG
     SIDATREVIL SAGVFNTPQI LKLSGIGPAE ELQSFGIDVV ADLPGVGTNL QDHYEISTVV
     KYESDFKFLE GCTFLSTADD ACYEQYTTGS NDAGGKGTYA TNLIPVATIR KSTVAGGQRD
     TFLFGGPIKF WGYFQGYTAA ALADHQHFSW LSLKAHEHNK AGTVTLRSTN PLDTPLINFN
     YFDAGTAGAE DLDLQPQVEG IAWMREVYKN IAAPNNDFTE IIPGPNITSD DDIKEFIKNE
     SWGHHASSTV KIGEDSDPMA VLDGKFRVRG VKGLRVVDAS VFPQVPGFFP VASVYMIGEK
     AADVILKDSA SKTETAGLAI DLSVVVG
//