ID A0A1E3I6U9_9TREE Unreviewed; 1693 AA.
AC A0A1E3I6U9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=sterol 3beta-glucosyltransferase {ECO:0000256|ARBA:ARBA00012650};
DE EC=2.4.1.173 {ECO:0000256|ARBA:ARBA00012650};
DE AltName: Full=Autophagy-related protein 26 {ECO:0000256|ARBA:ARBA00029843};
GN ORFNames=L202_00102 {ECO:0000313|EMBL:ODN84085.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN84085.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN84085.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN84085.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-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}.
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:ODN84085.1}.
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DR EMBL; AWGJ01000001; ODN84084.1; -; Genomic_DNA.
DR EMBL; AWGJ01000001; ODN84085.1; -; Genomic_DNA.
DR RefSeq; XP_018997887.1; XM_019133182.1.
DR RefSeq; XP_018997888.1; XM_019133183.1.
DR GeneID; 30151411; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000094065; 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:0102202; F:soladodine glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016906; F:sterol 3-beta-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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000094065};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 530..622
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1573..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1635..1662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1693 AA; 185435 MW; 5B1088009DF0ED1F CRC64;
MSSQDNQHPP LNSASQQPPF PAAGTAHDSP PSHTQQVAQS LVNTVAQHTI PTEPPTAEER
GQSPSDSQPN PGVADSEAPM GDIMKSDSPP PDDIGLPAVE PPQSQSREVE SITSPAISYA
PKDQASEGWH AKITPEPTSI SSGYEAQPDL SDMGPPIVPP GSDSQGVRFS ASSPISYAPR
EPLPEGQTLE DTASDTGPRP NYEARPGFGI SKEIGSIRMG ASALVSALNA LPWDDEDEEG
DEEENDDLAP SVPGRGSASV MQETVRRPKL AKLGSSLHTI RPLSNPATPL PTPYAHPSHS
LHFPFRQNAI ARKARRPGTT ELDYQFAASP PRSGHERQGS IASEVSSDGE VPLPKGFKQS
KRESSDSSVG SITGEEADML NARITQEQGI ADEEERVEML ETAREEGVSE IELGKAISTR
GSLQDLNAAA ALSTRGSLQD LNTAAALREE NHEGEDVIAE SLETDESEKR LMRKERLAER
LMEVFGLEER EEVLAEMKCW LLRCVMLKGY MYLTKRHICF FANMPDENNL LVKSGPLYKK
ASRTKLNTKF WVVLKNDVLS WYESTSDPYF PKGNISLQYC ISVDPVRDTK FKIRTAERSY
TFTADTEGGR DEWVKVVKKV MFKLQHEGET IKVIIPFQAV IDVEKSPTLE FAETIEVKCM
DAEDKMSIDS YFFASFPDND YAFEILSQLI RDRSPDISRT SSADIPRISS AATITVGQES
LDTSYATLKT LVDKPASPSP TESLPQPIKK LSSVLKPLVS KTGDEEAASQ EDAPSQSTSD
TTGTSFDGYP PAQVGPPPAS MLEDKSTWGP SWIRKPAAKI FGSSPSGSIS SYLGRSPTDS
LTTVVEGPRA RLGRGKQHSV TEVVEAPLRD LLHDTEDEGS DDEFTGHTSR NSSFQSAAEK
RASRSSWTSE SSTGSQMVHS RSDFSMLGSD NGHSESAEMV KKFRSFFALS EKEELLDHFP
GYLYRVLPIS GRFFVSTNYF CFRSSQLLYK TKMIIPIRDL YGLKAQKAFR FGHSGLIIVI
KGHEELFLEF SNSDRRKACI SILEERMETV RLSVSSGQTP PDQNRIKAHI MEDLDESHPI
EAGTPLGSGM SSPSPMFGSA TSTSFLEFKP ESMRITCLTI GSRGDVQPYI ALCKGLQAEG
HRTKIATHGE YKDWVEGHGI EFESVGGDPA ELMQMCVDNG MFTVSFLKEG LQKFRGWLDD
LLNSSWQACQ GSDLLIESPS AMSGFHIAEA LRIPYYRAFT MPWTRTRAYP HAFAVPESRR
GGSYNYMTYT MFDQVFWRAI SSQINRWRRH ELSLDNTTFD KMEQHKVPFL YNFSPTVVPA
PLDWTEWIHV TGYWFLDKPD EKEGDTEKKW CPPDGLVEFI DGAHANGKKV VYIGFGSIVV
SDPEEMTRCV VEAVISSGVH AILSKGWSDR GTKARGEPSG GAEGADGVKY PPEIFAIDSI
DHGWLFPKID AACHHGGAGT TGASLRAGIP TIIKPFFGDQ AFWAERVESL NVGSAIRKLD
SEQLAKALVK ATSDEKQIAK AKDVGEVVRR ENGVARAIEA IYRDLEYAKS IIKPPPASAV
DDKEDNLNRV SSLLHPLTSP DLSKNIRSRS RSHSRSHSKS HSSSFSHTAS PRRASISSLL
GAGGDEEEWS VIPEGAGMSR SGSLSPSAGV RGSPEKRGSM GLGMGAVLGR EVLRGAAGLP
LPNPFGKWRS GEE
//