ID W2SG37_9EURO Unreviewed; 1268 AA.
AC W2SG37;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1541_01148 {ECO:0000313|EMBL:ETN46958.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN46958.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN46958.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN46958.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; KB822711; ETN46958.1; -; Genomic_DNA.
DR RefSeq; XP_008711670.1; XM_008713448.1.
DR AlphaFoldDB; W2SG37; -.
DR STRING; 1220924.W2SG37; -.
DR GeneID; 19968487; -.
DR VEuPathDB; FungiDB:HMPREF1541_01148; -.
DR eggNOG; ENOG502QSPJ; Eukaryota.
DR HOGENOM; CLU_002483_0_0_1; -.
DR InParanoid; W2SG37; -.
DR OrthoDB; 1945480at2759; -.
DR Proteomes; UP000030752; 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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1.
DR PANTHER; PTHR47470:SF1; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030752}.
FT DOMAIN 82..114
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
FT DOMAIN 146..399
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 578..644
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 138806 MW; 1E1D0ED3439EAC56 CRC64;
MAALDGPSTS MPDEVQNGEA SPDSSDGVHK VSERVQSWAV GTTEPGGFTK APSKLRPRDY
SSSHNTFPRI SKPVELLRHK YDVVVIGSGY GGGVAASRMA RAGQSVCVLE RGKERWPGEY
PDNLADATPE VSISGLFAPN NRTGRHISIG DPTKLYQLVV GEGQNAFVAS GLGGTSLLNA
NVFLEADAGT MSLPKWPQDL QEEGALDEYY DRAREMLQPE EYPEDFPRLR KLDLLERQAH
VVKEELALEK QPSGRPLGEP EFRRVPQTTR FEDGPNHAGV QMQASTLTGM DSTGVNDGSK
SSTLVTYLSD AWNWGAEIFC ECEVRHVKKH PDSRIGGYLV CFAWHGSKRA CFQDNIYQDL
MWVHAKVVFF GAGALGTTEI LLRSKSLGLK MSGRVGKNMS GNGDILAFGY NTDEEVNGLG
RPFSDPLHPV GPTITGVIDC RQQANPLDGF VIEEGAIAAP LVPVLQAMLE AMPGKVFPRT
YGLLEMLRHF ASRRLSRVSK YAPWGALQRM QTYLIMSHDS NQAIMTLEND KPTLRWLGVG
RSEHVKFLND LLASITGKFG GTYINSPFYA SLGKQEITVH AIGGASMAAD GTGQTGATDS
LGRLFKGSEK DSGVYEGLVV VDGAVVPTAL GVNPFATITA LAERSAAAAA HRAGLHINYA
EKNGTLELYG APKHTFRMDA SLERAQRTIQ DATESSAQGI EFTEVMSGFM NIGDDIDDFD
IAYDSASAAG SSAQFFLSVH AWNTDRLVAA EDHPAMLTGT FTCAGLRGSP FMVLRGDFAL
FSTDQRTPDT TNLKYEFDMR STFGDIIHFS GYKVVDPSIA LQPWATWKAT STLHCMLASD
GKVLGRGKLC IKPHDFLSEL KTFTPAGHAV LSKLASTAKF LTFFTGQVAS KFFGPLGAEE
WPRTTSQGYE TDTAPPHKTR KITSSDGIVS TLQHWLPTAR YEHDVSPRVL FIPGASVDHQ
IFALPTIETN AVEYFQSQGF EVFCVTHRVG KTPNAIRDFT TFDARFDIQA AFTEIHKLHG
SDDPIYVIAH CAGSVALSAG LLDGTIPARW LRGLTASQVF FNPIFGSVNW LKASLPMPLT
KLYRVAAGKW FSCISSQHDT LVQRLINQFV KLYPVGSARE LCNSVVCHRS ELVFGRLWSH
KKLNAATHAN LSKFLGGTSM HSLEHLMHMG THGFVTNNYN ESLVTSRNID RLKDLPILFI
SGSENVVYSP ETTDKSFTTL INHFQQEGYE REVIQGYGHL DCWMSPDAVN DVYPLVRDHA
VRCMTAAN
//
