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Database: UniProt
Entry: A0A094AS15_9PEZI
LinkDB: A0A094AS15_9PEZI
Original site: A0A094AS15_9PEZI 
ID   A0A094AS15_9PEZI        Unreviewed;       763 AA.
AC   A0A094AS15;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=V493_04368 {ECO:0000313|EMBL:KFY25920.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY25920.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY25920.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
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   -!- 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:KFY25920.1}.
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DR   EMBL; JPJV01001698; KFY25920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094AS15; -.
DR   STRING; 1420906.A0A094AS15; -.
DR   HOGENOM; CLU_002865_5_1_1; -.
DR   OrthoDB; 2392848at2759; -.
DR   Proteomes; UP000029327; 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:SF78; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000029327}.
FT   DOMAIN          284..298
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   763 AA;  82658 MW;  A46F9A5085D22AB4 CRC64;
     MGLHTKLAEG IDEVDVIIAG GGTASCIIAA RLAEADPNLS ILVIEGGANN YNVATVVHPA
     LFLQNLAPNS TTAIFYKGNK AKQLADREPI VPSGGILGGG SSINFMMYAR AQRADLDSWK
     TPGWSADELL PFMKKLETYH GPGEKDHHGF DGPIHVSNGT YRASRPETDF IDAAQKCGYP
     EIKDLQNLDA NNGVERWLRY VSPDGKRQDT AHTYLHPKLQ DSSAYPKLHV LVEAKVIRVV
     IDDSGRAVGV EYTPNPDFQA AGINLTQHPK RTVKARRLVV VSCGACGTPA VLERSGVGNA
     KVLERAGVPV VVDLPGVGND YQDHHLVLYP YRTNLAPDET IDGILSGRTD AAELIAKNDK
     IMGWNSVDIS SKLRPTDDEV SALGPEFQAA WDRDFKNAPN KPLMLMGLVS CFLGDPGSIP
     AGQYVTIGNY TAYPYSRGHM HITGSDHSDR LDFDVGFFTD PHDIDLKKQI WAYKKQREIM
     RRTKMYRGEL ALGHPRFPAE SNAACVETDG PLNEVCDLKY SAEDDKAIEQ WLRENVNTTW
     HSLGTAKMAP LEEMGVVKPN LDVHGVKGLK VADMSIAPEN VGANTNNTAL VIGFNTFFHP
     RYQIECGASN DPNTIYATDR PVAKKGLTPT QTEQGASVNG VAPQQPAAAQ AKAAAAKEAE
     SFDLSTMIAS KMHSAGNRTV PHNRGTAVSA RDMPNVWAAV TLFSGDTDVT YQLRGDLIQS
     PIEGCFYFSG LTIHEQGVGC VDSSVIIIGP RPDGRQSVDP LGI
//
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