ID B3RH80_YEAS1 Unreviewed; 1198 AA.
AC B3RH80;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
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};
GN ORFNames=SCRG_04148 {ECO:0000313|EMBL:EDV08524.1};
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006 {ECO:0000313|EMBL:EDV08524.1, ECO:0000313|Proteomes:UP000008335};
RN [1] {ECO:0000313|Proteomes:UP000008335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a {ECO:0000313|Proteomes:UP000008335};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) 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; DS981519; EDV08524.1; -; Genomic_DNA.
DR AlphaFoldDB; B3RH80; -.
DR HOGENOM; CLU_000537_6_0_1; -.
DR Proteomes; UP000008335; 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); 2.
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; 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 {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
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:EDV08524.1}.
FT DOMAIN 238..336
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 136054 MW; 31D75148DA5DC223 CRC64;
MPITQIISAS DSEAGPKPSI SLVPDKPSEP ETSPRHHRLS RSLSKFKRWR GRSNSSLSMG
SSEQQELQDS PNEARSDDDE NGYNNDNADD LAKSKYMMKS IAGLLTTASV YAGMNNAQEM
NVLSQVDSEE SDSSDSFQEN IGRNEVKSKK ENLKTKSHPE VPRLDKRKPT LFDFSITREK
LSKDNVAKLR QRFCLDEREP FLNDFPAWLL KDVLVQGHIF ITTKHFLFFA YLPKNPRSVK
MSGNLNIRTK LIRSTRYWCV LKNHLFSMYT SSTELYFPVL TIDLREVQKI ETQKHTLNGS
ATKTFKLYTD ESTFKFNADS EFSAKSWVNA LKKEQFAAQN SENNSISLKI PLPNIIEIDD
QPIVNKALTL RLRALESSQT YAIDDFMFVF MDGSGSQVKE SLGEQLAILQ KSGVNTLYYD
IPAKKSKSSF GKETPATAEQ KNNGEDSKYL NVPTSAVPSS ENGKKSRFRF RERSNSWFRR
AKPLEDSQVE DVEEIYKDAA NDIDSSVHST IHIHEQEDSQ EQTVAWKPSH LKNFAEMWAA
KPIHYRNKFI PFQKDDTYLI KETEEVSANE RFRYHFKFNK EKSLISTYYT YLNRNVPVYG
KIYVSNDTVC FRSLLPGSNT YMVLPLVDVE TCYKEKGFRF GYFVLVIVIH GHEELFFEFS
TEVARDDIER ILLKLLDNIY ASSAEGSNIS SASLGDVQHN PDSAKLKLFE DKINAEGFEV
PLMIDENPHY KTSIKPNKSY KFGLLTIGSR GDVQPYIALG KGLIKEGHQV VIITHSEFRD
FVESHGIQFE EIAGNPVELM SLMVENESMN VKMLREASSK FRGWIDALLQ TSWEVCNRRK
FDILIESPSA MVGIHITEAL QIPYFRAFTM PWTRTRAYPH AFIVPDQKRG GNYNYLTHVL
FENVFWKGIS GQVNKWRVET LGLGKTNLFL LQQNNVPFLY NVSPTIFPPS IDFSEWVRVT
GYWFLDDKST FKPPAELQEF ISEARSKGKK LVYIGFGSIV VSNAKEMTEA LVEAVMEADV
YCILNKGWSE RLGDKAAKKT EVDLPRNILN IGNVPHDWLF PQVDAAVHHG GSGTTGASLR
AGLPTVIKPF FGDQFFYAGR VEDIGVGIAL KKLNAQTLAD ALKVATTNKI MKDRAGLIKK
KISKEDGIKT AISAIYNELE YARSVTLSRV KTPRKKEENV DATKLTPAET TDEGWTMI
//
