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Database: UniProt
Entry: A0A1D2V8V5_9ASCO
LinkDB: A0A1D2V8V5_9ASCO
Original site: A0A1D2V8V5_9ASCO 
ID   A0A1D2V8V5_9ASCO        Unreviewed;      1069 AA.
AC   A0A1D2V8V5;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Sterol 3-beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00017894};
DE            EC=2.4.1.173 {ECO:0000256|ARBA:ARBA00012650};
DE   AltName: Full=Autophagy-related protein 26 {ECO:0000256|ARBA:ARBA00029843};
DE   Flags: Fragment;
GN   ORFNames=ASCRUDRAFT_17082 {ECO:0000313|EMBL:ODV58064.1};
OS   Ascoidea rubescens DSM 1968.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Ascoideaceae; Ascoidea.
OX   NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV58064.1, ECO:0000313|Proteomes:UP000095038};
RN   [1] {ECO:0000313|Proteomes:UP000095038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA   Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA   Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA   Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA   Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA   Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA   Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sterol + UDP-alpha-D-glucose = a sterol 3-beta-D-glucoside +
CC         H(+) + UDP; Xref=Rhea:RHEA:22724, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15889, ChEBI:CHEBI:37424, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.173;
CC         Evidence={ECO:0000256|ARBA:ARBA00035583};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22725;
CC         Evidence={ECO:0000256|ARBA:ARBA00035583};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ergosterol + UDP-alpha-D-glucose = ergosteryl 3-beta-D-
CC         glucoside + H(+) + UDP; Xref=Rhea:RHEA:61836, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16933, ChEBI:CHEBI:52973, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; Evidence={ECO:0000256|ARBA:ARBA00035586};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61837;
CC         Evidence={ECO:0000256|ARBA:ARBA00035586};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000256|ARBA:ARBA00006962}.
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DR   EMBL; KV454495; ODV58064.1; -; Genomic_DNA.
DR   RefSeq; XP_020044371.1; XM_020189465.1.
DR   AlphaFoldDB; A0A1D2V8V5; -.
DR   STRING; 1344418.A0A1D2V8V5; -.
DR   GeneID; 30963101; -.
DR   InParanoid; A0A1D2V8V5; -.
DR   OrthoDB; 76239at2759; -.
DR   Proteomes; UP000095038; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0102203; F:brassicasterol glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102205; F:cholesterol alpha-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051506; F:ergosterol UDP-glucosyltransferase activity; IEA:RHEA.
DR   GO; GO:0102202; F:soladodine glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   CDD; cd13215; PH-GRAM1_AGT26; 1.
DR   CDD; cd13216; PH-GRAM2_AGT26; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 3.
DR   InterPro; IPR048066; ATG26_PH_GRAM1.
DR   InterPro; IPR048065; ATG26_PH_GRAM2.
DR   InterPro; IPR010610; EryCIII-like_C.
DR   InterPro; IPR004276; GlycoTrans_28_N.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   PANTHER; PTHR48050; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR48050:SF25; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF06722; EryCIII-like_C; 1.
DR   Pfam; PF03033; Glyco_transf_28; 1.
DR   Pfam; PF02893; GRAM; 2.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00568; GRAM; 2.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095038};
KW   Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955};
KW   Steroid metabolism {ECO:0000256|ARBA:ARBA00023221};
KW   Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011};
KW   Sterol metabolism {ECO:0000256|ARBA:ARBA00023166};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ODV58064.1}.
FT   DOMAIN          157..188
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          920..942
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ODV58064.1"
FT   NON_TER         1069
FT                   /evidence="ECO:0000313|EMBL:ODV58064.1"
SQ   SEQUENCE   1069 AA;  121635 MW;  60F6BA22FA4DC311 CRC64;
     IKEGFQNVNE KKLSKALSLS SKLASTFNID PDDEFLDDFS CWLLRDVLLQ GHLYITKSFI
     LFFAYLPKLT KDSTIFDGNL STKRNYNSKL KLKLISQNPI SSNNRYWCVL KNSTFSTFNN
     SSDLYFPLLT IDLRYAIRVE IIPNAPNIED DQKPCWFRIF TETKTYKFKA DNLYSARQWV
     AALKKQIFTA RNKGDIVTVK LPISNLIDLE ETSIFEDSET IRLKVLENSK TFAVDDYFFM
     FFHNGHNVIN CINQALSLNN LPNFELSSGS TESSPVILSN STIDDLIRSK NLSSILSSSR
     QIIPVEEKIQ SLVSINRRQR ALGFNISIDI DSDNDICNRD NRNEISEILN SGYEDSDVNE
     VESSNENDDL LTHKNRFLGN TGTKALQIIN PKNLVKNMFV LNTLSNVSGM WTAEPSHYEE
     KNSLERGLED EYFVASEIER KNSIRRFQSH FSLPEGEKLI STYYAHFQRN IPLYGKIYLG
     SNEICFRSLI PGTNTKMILP FNDIETCYKE KGFRFGIGYS GLVIVIHAHE ELFFEFSSSE
     SRDDCETLLL KQIDLLKNYN YRFNNYSFII NNNSGKEEED IKLAESVNNQ AEAARIKCFE
     NKLNEETGFD LPIIIEDKKF KEKLKPNKNM HFTLLTIGSR GDVQPYLALG RGLLKEGHKV
     RIATHKEFEK VVLSNGIEFR EVSGDPTKLM SFMGDHGGIS VSFIKDGKAL FSNWINELLE
     SSWEACQGTD VLIESPSAMA GIHIAEALCI PYFRAFTMPW TRTRAYPHAF IVPEQKMGGS
     YNYLTHIIFE TVFWKGISGQ VNRWRKERLG LERTNLELMQ QNKVPFLYNI SPTVFPSPVD
     FSDWVKVTGY WFLNEGTDYI PTEKLKKFIN KARRDKKKLV YIGFGSIVVN DPRELTRAIV
     EAVVDSDVRC ILNKGWSGRN SGTAGDERKE EEDGEGEGEE EEALPACIYS SGSVPHDWLF
     FQVDAAVHHG GSGTTGASLR AGLPTVVKPF FGDQFFYGNR VEDIGVGVSL KKLNSRTLGR
     AIREVTTSKR IIEKARAIGE KIRKENGVET AIGIIYGELD YARNLILAK
//
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