ID A0A0J0XVZ3_9TREE Unreviewed; 1455 AA.
AC A0A0J0XVZ3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=CC85DRAFT_282749 {ECO:0000313|EMBL:KLT45265.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT45265.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT45265.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT45265.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-2015) 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; KQ087182; KLT45265.1; -; Genomic_DNA.
DR RefSeq; XP_018281756.1; XM_018422091.1.
DR STRING; 879819.A0A0J0XVZ3; -.
DR GeneID; 28982694; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000053611; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 382..474
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1418..1435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1455 AA; 161586 MW; 28DC747A98757C77 CRC64;
MSHRNTQEEQ DPPAERSSTA TPPEPSGDLS ATMPPVPPPP IMTPAMEAQS IPSATFASSS
VSDSEQVTQR DASPTTQPSD PDSTPIAPIP GMRFPHFPTP ERHGTARPRD YRRIATADEA
SHDQKLSEMG SIRMGASALI SALSALPRDD EESSLSSDEE VSYEVDVTTH LPVRPKMSRM
HSSLQTLRPM ASMSDPDTHN AHSQPTFLRT PPRSAHSPPH RARSPLGSGR SRPTSPESHH
KLTFPYKENV ITRRARAPSL TELRYQHAPA SPEGAHERLP WQMRVGSSST LKEIASDLVE
PSQEVEEVQG SALGKPERGH LVVEREDTPR MLQRVFGLQE QEELIEEMHC WLLRSDMLQG
YMYLTRRHIC FFAKVGQTEN DKTIKSGPLW KKASRTKLSN RYWVTLRNNV LSWYESPNDP
YFPKGNVSLQ YALSCDLVDE TRFKVRLPER NYTFQSDTAS NAQEWVRVIQ KSTVKLQHEG
QGVKLIIPWE AVYEVERSPT LEFAETIEIK VIDSEDSMSL DSYFFASFPD NDYAYELLQT
LLRERPVSEL PPPAAPSPKP AERKRDSGSR FSLTNLSAAL PIPIPKFGSD KGDSSERVPI
APPMVLDLPY SGHDSFTSHS EADSEMSEDD EATRRRKEYP PRPSGPPPPG MGPASSGWAP
ADWIRRGSAQ LFGTSPGSQP PPPRRRIHRQ GSVTEVVEGY SFDSTDESES ERRLSGARQS
FSKLASTTPE SPQPAQEDAI AIKFRKTFAL PETEVLIDHI SGSLYRVLPV SGRFFVSSNY
FCFRSSGLLN KTKMIVPIRQ LYGMTAQKAF RFGHHGLIVI IKGHEELFLE FHSASRRDEL
MALLEERMDD VREASQANKA LEAAFPNAQG PFVNDMSDAP ETAIGSMFSS TTSSFLQFKP
EPMTIVCLTI GSRGDVQPYI ALCKGLQAEG HTCRIATHAE YQAWVEGHGI GFAPVGGDPA
KLMELCVDNG MFTISFLKEG LQMFRGWLDE LLNESWSACQ GADLLIESPS AMAGIHIAEA
LRIPYYRAFT MPWTRTRAYP QAFAVPEHKR GGSYNYMTYV MFDNVFWRAI SGQVNHWRKT
VLKIESTTFD KMAQDKVPFL YNFSPTVVPP PLDWTEWIHV SGYWFLDNAD GKKDWSPPDG
IVEFIDNAHA RGKKVVYIGF GSIVVSDPHE MTRCVVQGVV DSGVCAILSK GWSDRGSRGK
NDHPELTAIT SHGADGIEFP PEIFSVDAID HSWLFPRIDA ACHHGGAGTT GASLRAGIPT
IIKPFFGDQF FWAERVESLG IGSSLRQLTY EGLATALIEA TTNERQIAKA KIVGQTIRAE
DGVQRAIEAI YRDLEYARSL IRPEEENLPS RSTLSLSMSN SMSRQGSGSH SRGHSRASSL
GDLLIHSHTR TRSTEGARSD ESWSVVSDAG ASLPSSPRRE AHESDSDDHH HRIPVLGSLV
SHISSAITRE SSSRK
//
