ID G9MRQ1_HYPVG Unreviewed; 1270 AA.
AC G9MRQ1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TRIVIDRAFT_28903 {ECO:0000313|EMBL:EHK22770.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK22770.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK22770.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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:EHK22770.1}.
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DR EMBL; ABDF02000006; EHK22770.1; -; Genomic_DNA.
DR RefSeq; XP_013956984.1; XM_014101509.1.
DR AlphaFoldDB; G9MRQ1; -.
DR STRING; 413071.G9MRQ1; -.
DR EnsemblFungi; EHK22770; EHK22770; TRIVIDRAFT_28903.
DR GeneID; 25792706; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_28903; -.
DR eggNOG; ENOG502QSPJ; Eukaryota.
DR HOGENOM; CLU_002483_0_0_1; -.
DR InParanoid; G9MRQ1; -.
DR OMA; PTGMYHL; -.
DR OrthoDB; 1945480at2759; -.
DR Proteomes; UP000007115; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT DOMAIN 60..324
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 487..583
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 212..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1270 AA; 141246 MW; 0584EA8AF0A2AEAC CRC64;
MSTYSEPLLP TAVTPTNAFP RISKPVELLR HSYDCVVIGS GYGGSVAASR MARAGESVCL
LERGEERWPG EYPTTSLETL KQYRFSGDFT PSSLGGFAVN SGNPTGMFNV FFGRDQSALL
GNGLGGTSLI NANVFLEADK DILKMGFWPP EIRQDPTLLD NYYQKVRDVL EPEPYPDNWP
TLKKSEIFRD QAQVIGLGDK FRKVPLTTRF RPGPNSSGVN MSASTLTGQD STGLNDGSKT
TTLVTYLADA WNWGAEMFCK CEVRYIEKVQ DDRGGYLIYF AWHGRGRGRF AEENTNSDLM
WVHAKKAVFL GAGAIGTTEI LLRSQQMGLS TSDWVGRGMS GNGDVLAFGH NCKQEVNALG
KPSPDPKNPV GPTITSAIDN REGLENPLSG FMIQEGCMPQ AFCQLLQCVL DLTPGSHSPD
MSLLERTREA MSLWKSRLLG PFSNKGTLEN TQVFLIMSHD GSQATLSLKN DRPVLEFQGV
GKSDRIKRFH DILEKATDAV GGTLVYTPLY HMNKQQITAH PLSGAPMSRD NTGANGATNH
IGQVFTGNNT SETHPGLIVV DGAVIPASIG VNPLATIAAL AERTVEAYAR ENGLIINEKK
NDILDLFGEP AHKPKDWHSY EPDLGFDYEV PYQLSKTEML RLKSLEFTEL MSGFIHKTSL
NAAADDKPAY ESDFRAGKGR GEVGRLLISA TVLDGSWLRE ESQPSSMLTG TFVCPTIEGS
PFMISRGELG LFKRAHETTG SSKLTYDCDM TGANGRRLRL RGYKLVDASV SLSPLQMWRS
TTTLYVTITE KDIRNEDSNE ERIVWHDDKV VARGILNIHP KDFASEMMTL SPAGSSLLTK
TINMSKFLSF FASKSLSHFL TPLGPLEYPE QGFVPYMNYT PPSQTYTIIA SDGVETELHM
WEPSPSAVAT DSRGTPVKIE NLFMIPGASV DHQIFSLPTI PFNAVNYFTR AGYRVFVTVH
RICQLKSTRE QDWTTYDSRL DIKACIKQIR RIYGRSKLYT IAHCMGAVAF ASGLLDGTIP
SKWILGITCS QVFMNPIWNT MNMIKARLPL GLDKIYYSVL GNWLDCSTST ADSLAQQTLN
QLLRFWPGTR KEMCKNAACH RATLLFGRCW NHHNLNEETH RNMDRFFGGG SMNMMNSLKR
MGSRGYVSSN APEYIEFNEP EHIERLRGIP IMSFIGQESG VISPRATEKT YERLIDAFGI
SAGLPGGGIQ YRRRVVPGYG HLDCWMGRNA WRDVYPFVRE EVDRVVRGES YQFHQPNDRF
KCFAEDHEAH
//
