ID   ATG26_VANPO             Reviewed;        1217 AA.
AC   A7TF84;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   04-NOV-2026, entry version 93.
DE   RecName: Full=Sterol 3-beta-glucosyltransferase {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000250|UniProtKB:Q06321};
DE            EC=2.4.1.173 {ECO:0000250|UniProtKB:Q06321};
DE   AltName: Full=Autophagy-related protein 26 {ECO:0000250|UniProtKB:Q06321};
GN   Name=ATG26 {ECO:0000250|UniProtKB:Q06321}; ORFNames=Kpol_2000p77;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- FUNCTION: Sterol glycosyltransferase responsible for the glycosylation
CC       of ergosterol to form ergosterol-glucoside.
CC       {ECO:0000250|UniProtKB:Q06321}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sterol + UDP-alpha-D-glucose = a sterol 3-beta-D-glucoside +
CC         UDP + H(+); 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:0000250|UniProtKB:Q06321};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22725;
CC         Evidence={ECO:0000250|UniProtKB:Q06321};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ergosterol + UDP-alpha-D-glucose = ergosteryl 3-beta-D-
CC         glucoside + UDP + H(+); Xref=Rhea:RHEA:61836, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16933, ChEBI:CHEBI:52973, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; Evidence={ECO:0000250|UniProtKB:Q06321};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61837;
CC         Evidence={ECO:0000250|UniProtKB:Q06321};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q06321}.
CC       Membrane {ECO:0000250|UniProtKB:Q06321}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q06321}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; DS480382; EDO19109.1; -; Genomic_DNA.
DR   RefSeq; XP_001646967.1; XM_001646917.1.
DR   AlphaFoldDB; A7TF84; -.
DR   SMR; A7TF84; -.
DR   FunCoup; A7TF84; 127.
DR   STRING; 436907.A7TF84; -.
DR   GeneID; 5547438; -.
DR   KEGG; vpo:Kpol_2000p77; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   HOGENOM; CLU_000537_6_0_1; -.
DR   InParanoid; A7TF84; -.
DR   OMA; AADPVHF; -.
DR   OrthoDB; 10261837at2759; -.
DR   PhylomeDB; A7TF84; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0016906; F:sterol 3-beta-glucosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0032120; P:ascospore-type prospore membrane formation; IEA:EnsemblFungi.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016125; P:sterol metabolic process; IEA:EnsemblFungi.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   CDD; cd13215; PH-GRAM1_AGT26; 1.
DR   CDD; cd13216; PH-GRAM2_AGT26; 1.
DR   FunFam; 3.40.50.2000:FF:000029; Sterol 3-beta-glucosyltransferase; 1.
DR   FunFam; 3.40.50.2000:FF:000009; Sterol 3-beta-glucosyltransferase UGT80A2; 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); 2.
DR   InterPro; IPR048066; ATG26_PH_GRAM1.
DR   InterPro; IPR048065; ATG26_PH_GRAM2.
DR   InterPro; IPR010610; EryCIII-like_C.
DR   InterPro; IPR050426; Glycosyltransferase_28.
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; 1.
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; Glycosyltransferase; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Reference proteome; Repeat; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT   CHAIN           1..1217
FT                   /note="Sterol 3-beta-glucosyltransferase"
FT                   /id="PRO_0000318049"
FT   DOMAIN          195..232
FT                   /note="GRAM 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          246..343
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          590..656
FT                   /note="GRAM 2"
FT                   /evidence="ECO:0000255"
FT   BINDING         766
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q06321"
FT   BINDING         767
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q06321"
FT   BINDING         769
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q06321"
FT   BINDING         1042
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q06321"
FT   BINDING         1072
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q06321"
FT   BINDING         1074
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q06321"
FT   BINDING         1087
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q06321"
FT   BINDING         1090
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q06321"
FT   BINDING         1091
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q06321"
FT   BINDING         1092
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q06321"
FT   BINDING         1111
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q06321"
FT   BINDING         1112
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:Q06321"
SQ   SEQUENCE   1217 AA;  138412 MW;  57C553A3F01C3653 CRC64;
     MIRNSTNTNN IMETEVALKD WILYYHKLCE VNSGEIFSGN EIITDFDDPV LSDPLLNLKP
     LPKNEVTVNK DNVIKDNDYS SNGCDFAKSK FHIKGLVGLL TTASVYIGLD NSTNPSYDIS
     QACEFDLEDN TVQQGTGRSA NMNPACKVAG FNKSSVRDTI FNIFKIPKKD EKISNDMEVN
     NTLSRDLDYK KDLFEFVRKY FGISEEETLI GHYTGWLLQE VLIQGNLFIT NSSLVYLAHL
     PKLTDAVVLC GKLKLRSRLK GNPRYWCVLK HSTLALYNDP SDIYFPILSI DLNHVEEISL
     ENSLKDENTM TFVLEASSKN YKFIAGSSHS AKTWVKCLKK QLFSIKNQSK DTIGIKFPIS
     SIIDVECQSY MNQGQSIKVK CFDGNKNYAL KEYTFLFFDK DGDSFYNIIS NFIPRNMNPV
     EASLQNSNPT IHLNSKSHFN DKIKILSAVN IDDIICDTDS FEMTSSDILS DIDENIQPLS
     LKHVRDISNC KNYLKEDLKT SNKMTIQDCN KKVQTSEIQL ITYSKHDSRM ELNDDSKYYQ
     GNIGNDNKGI LSFKNICSIW NTSPIHNKDS DNFFMTSDPF VTSINDTTLA KIKDWFNLHD
     NEVLHALYYA YLIKGYPVYG KLYVTNRRLY FKSCIPGVNV KMVLPLEDIE GYNEILGTNY
     GNFGILLTVQ NEKELQFGFN SCTNRSDFEN VLQRCLDICK YAIKTPELVT SRVIESESEH
     SRLRFFEEKF STEGIDIPFL VEDNPYFKTK IMPTKSYNFG FLTIGSRGDV QPYIALAKGL
     IQEGHSVTII THREFKSFVE CHGIDFKEIA GDPTKLMSLM VEHEAINVGM LMEASSKFRG
     WIHDLLVTTW EACKNLKLDI LIESPSAMAG IHISEALQIP YFRAFTMPWT RTRAYPHAFI
     VPDQKRGGSF NYLTHVIFEN VFWRGICSQV NKWRVQTLGL EKTNLAQLQQ NKIPFLYNIS
     PVIFPPAIDF DEWIKVTGYW FLDESESFEP SQELETFISK ARKLGKKLVY IGFGSIVVNN
     AKEMTRAVID SVLETDIFCI LNKGWSERLG KEELRYEEEP EYPETIFLCD SIPHDWLFPK
     VDAAVHHGGS GTTGATLKAG TPVVIKPFFG DQFFFASRIE DIGAGIALKK LNVSSLSNAI
     KKVLTDKSIK RKAVSLKKRV AKENGVTTAI NCIYSELEYA RSLVVKKNHK SSNIEFIQHP
     NNVNDTTKTV IPLTSMV
//