ID A0A167FDW8_9ASCO Unreviewed; 1131 AA.
AC A0A167FDW8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 Name=ATG26 {ECO:0000313|EMBL:ANB15176.1};
GN ORFNames=AWJ20_2800 {ECO:0000313|EMBL:ANB15176.1};
OS Sugiyamaella lignohabitans.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB15176.1, ECO:0000313|Proteomes:UP000189580};
RN [1] {ECO:0000313|EMBL:ANB15176.1, ECO:0000313|Proteomes:UP000189580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB15176.1,
RC ECO:0000313|Proteomes:UP000189580};
RA Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA Mattanovich D.;
RT "Complete genome sequence and transcriptome regulation of the pentose
RT utilising yeast Sugiyamaella lignohabitans.";
RL Submitted (FEB-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}.
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DR EMBL; CP014503; ANB15176.1; -; Genomic_DNA.
DR RefSeq; XP_018737653.1; XM_018879770.1.
DR AlphaFoldDB; A0A167FDW8; -.
DR GeneID; 30034752; -.
DR KEGG; slb:AWJ20_2800; -.
DR OrthoDB; 76239at2759; -.
DR Proteomes; UP000189580; Chromosome b.
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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000189580};
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}.
FT DOMAIN 7..108
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 232..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1131 AA; 125842 MW; 3DE51B6593AF3C1E CRC64;
MPRNQTDSIK SGSLRKKSRK TPSFSKFWFV LRSDSFSYYT NATEMYFPAG TIDLRYAVKA
EIVHHGLEKE QLKSSTFSII TETRTYTFKA DSAKAAHEWV KALQKEIFRS RNEGDYVKII
IPLVNIIDLE DSPIMNIATT LKIRAIENDE TYAVDEYVLA FFTKGKEVVD AIKVSMKELG
VSGIAVDDSS STDLAAKAGS LNLEEIRENR PKLLKTQTSL KVKSPMVAAA ASNVASTPKS
PVDSLKKTNS SVSLSKKVRN LFNDNEGSTT PGSPHLSPRI GPLKSTSSKE VIKDWTLDSP
SGLESPPGES MPSRQKSRPG TPPDQLAVSA AMAALQSDRD RKSHEQEEVY PTGHTTGHIR
ISSSIGQIFK KEGGSGSGAS TPGEDNKSYD FLSASESNQI QYESSDKKKK KSANIVHKVT
DMWGGGRKHF RDPNQAGGFR DDRHLVSEED GAESNERFRA HFSLGETDNL VATYFCHIQK
AIPIYGKMYL SNEHLCFRSL LPGTNTKMIL PLHVVENVTK EKGFRFGYSG LVIVVHGHEE
IFFEFGSSNN RDDCEIMILR EMDRSKNRSI IRQSGSDYAL RSARLITYED ALRNELPPGI
NVPPVILEPC NDTSNDFFVG KAKDSLRFTL LTIGSRGDVQ PYISLGKGLL KEGHKVKIAT
HAEFKPWIEK HGIEFAEVAG DPGALMKIMI EHGMFSVSFL REAAAKFRDW IDELLLTAWK
ACQDTDVLIE SPSAMAGIHI AEALKIPYMR AFTMPWTRTR AYPHAFIVPE QKMGGSYNYL
TYVMFDNVFW KGISGQVNRW RKKTLHLPRT NLDLLQQTQV PFMYNVSPSV LVPPVDFPSW
IRVTGYWFLD EGGEDYVPDK SLVDFIAKAR KDDAKLVYIG FGSIVVSNPK ELTKAVVASV
QKAGVRCILS KGWSDRLGKG DASVPEVELP PEIYQIKSAP HDWLFPQVDA AVHHGGSGTT
GASLRAGLPT IIKPFFGDQF FYAGRVEDLG AGVHLRKLTV NQFSKALWEV THNERIISKA
ADIGKRIREE NGVDTAIQVI YQELEYARSL IKDGNVPVGR KIPTLMDVAG LPVKLVQRAT
APLPSLPICH DDSDQEHDEE RDKKSNSSQE DDSTHTDGSW TVVDTESKEQ E
//
