ID A0A165E662_9APHY Unreviewed; 1279 AA.
AC A0A165E662;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=LAESUDRAFT_653996 {ECO:0000313|EMBL:KZT06312.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT06312.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT06312.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT06312.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV427625; KZT06312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165E662; -.
DR STRING; 1314785.A0A165E662; -.
DR InParanoid; A0A165E662; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000076871; 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); 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; 2.
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:UP000076871};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZT06312.1}.
FT DOMAIN 206..298
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 18..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1279 AA; 141854 MW; C1D2C5E061DE3F2C CRC64;
MHAGTQTLIQ ALQAMPWAEE QDEDDCATQG NTPADSSSDE DDRGSNRLAS SIHTIYRPLA
RSRRNVLASL YSRARSPGLP KVPDQDETPR TEEPSMSEEE LEDDFERGGP RDSPRTLSDE
EHELDGSGSE GHRKEPSSPG SMATVKLQRR AKLAGKLREV FELSGIHEVI AEMPCWLLRS
ILLQGYMYLT DSYLCFFAHM PSREDQVLKS GSLMKKAQRT KRRIRHWFIL KNDALSWYQS
PSDPYFPHGI VDLRYAISCE PLHEKDIRLR TNQKAIRLSA DSTPSRDEWV KAIKRVMFKA
QNMGDIFKIA IPYSAILEVE KSSAMDFSET IEVKVVDKND QGSIDSYFFA YFRDLPAALA
QIRDAVRAYR AMPQAATPPA VIDTTTARPP NSPPSALRTQ SLPVLGQTSK ASSGSRLTSL
LRPLQENAPL VRPAHSPERD DNEDFTHVAK RGSTNIMAIT TSPKSSTYSD AGMSHSPESP
PAPSSSSQLV ASHHTYPPSP SPSPSMSELT ATPTRDTSLI PWGVGMPSWL RMPSMPSRRT
LSNPFGGARS GSEQPGPASG RSGGEGVSEV LSPNTGSGSR MTTSGSSDFG YFSVLDTPET
ILEQDTVDKF HTAFAFDERE KLLGVFSGYI YRMLPVYGRL YVSTNFFCFK SSGPLSSRTK
MILPIRDVLS TENSKAFHFA HQGLVIVIRG YEELFFEFAD EERRAAFVHI LERQMEDVRR
RVESGDQHCQ SLGQHDALIL EEAGPQTSPD GEMEQKVEHD ASMSGSLPAV MFNSMSSTFL
TFKPKEPLHF TFLTVGSRGD VQPYIALAKG LMKDGHRVRI ATHGEFKEWI EAHGIEFGYV
GGDPAELMRI CVDNGTFTVS FLKEGMLKFR GWIDDLLKTS WEACQGTDVL IESPSAMAGY
HIAEALKIPY FRAFTMTWSR TRAYPHAFAV PEHKMGGNYN YMSYVLFDQV FWRATAGQIN
RWRKNTLGLG STSLDRMEPH KIPFLYNFSP VVVPPPLDWP EWIHVTGYWF LDDADVSSKK
WTPPASLLEF IDSARKAKKK VVYIGFGSIV VSDPKAITHC VISAIVRSGV YAILSKGWSD
RLIKNVAEAS DPEEPLPKQI YPIASVPHDW LFKRVDAACH HGGAGTTGAS LRAGIPTIIK
PFFGDQFFWA DRVEALGIGA AVRKLTVEHL TQALINATTD QRQIDRARTV GEQIRAEDGV
GTAIEAIYRD MEYARSLIKG SPADDPQDVE VDAEHATIRD YPHAMSPTRS GGTRSGGSSA
SSAHGATSDW SVISEQERD
//
