ID B8NAU8_ASPFN Unreviewed; 1311 AA.
AC B8NAU8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=AFLA_043230 {ECO:0000313|EMBL:EED52621.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED52621.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED52621.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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}. Preautophagosomal structure membrane
CC {ECO:0000256|ARBA:ARBA00004623}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004623}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000256|ARBA:ARBA00006962}.
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DR EMBL; EQ963476; EED52621.1; -; Genomic_DNA.
DR RefSeq; XP_002377785.1; XM_002377744.1.
DR STRING; 332952.B8NAU8; -.
DR EnsemblFungi; EED52621; EED52621; AFLA_043230.
DR VEuPathDB; FungiDB:AFLA_007885; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_000537_6_0_1; -.
DR OMA; WRNKTLG; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0034045; C:phagophore assembly site 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:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; 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); 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 Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EED52621.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 212..311
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1311 AA; 146268 MW; 9D799CEE73C3FB1E CRC64;
MIAAVGSKSD FHARFDESSD SEGEAEGQTQ KQPGKASLSN KKKFPLSPTL KPQSTLEGRG
RRHRRSISDN KLLRSLKPSP KSSKGTETTV QTEPPTSDEM SPLASPRRAR SATPRAAPIL
SRMLEAEALL DKKQSADQPS SSTKGETDGT SEQSCASPLS LRLKEMFGFE MPEKVLMEYA
CSLLQNILLQ GYMYVTEGHI CFYAYLPRKS AVTIRSGYLH KRGRKNPKYN RYWFSLKGDV
LSYYTDPSSL YFPSGHVDLR YGISASLTEQ KDKDKEVRDF QVTTDQRTYY FRADSSASAK
EWVKALQKVI FRAHNEGDSV KISFPIESII DIEESPITDL AETFKIRVVE SDESYAIDEY
YFSFFESGRD AYNFVKGLIS EGPMKTSQLL PPPSEQTSPA TRARGPRNRW SLNSDLSQSR
GNGIFKTQRK RSASTGQTNS GPDGIGMSPR QRDLSDSFVN SFEQATDASA VLQSMIDTTE
SASQILNRSD VFQSPTIHTL RQRHPSGDRT GRRLSDGTAR STHPNAADAN RNGQEMQYAS
SDSDQGTQHP SKVNSSAPTL NELVKAGAYP LQRAAGFAEY LRSRSRQMSN LLASESMGYI
EKVSGMWAGG RRHYGETEGV LPDDQDVDPE DKEDGVKHGD RFRAHFALPS TERLQATYYA
YLHRVLPLYG KIYISQKKLC FRSLIPGTRT KLILPLKDIE NVEKEKGFRF GYQGLVIIIR
GHEELFFEFN TADARDDCAV TVHQSLESMR FLVESGLLAE QEKDEIESAQ AEHRMLQEAR
LDGAGEHDSH ASVNESSELH PIFDDPRASI INFKPSESLR ITCLTIGSRG DVQPYIALCK
GLLAEGHKPK IATHAEFEPW VRQHGIDFAP VDGDPAELMR ICVENGMFTY SFLKEASTKF
RGWIDDLLSS AWASCQDSDL LIESPSAMAG IHIAEALRIP YFRAFTMPWS RTRAYPHAFA
VPENKMGGAY NYITYVMFDT VFWKAIAGQV NRWRKKQLGL KATTLDKMQP NKVPFLYNYS
PSVVAPPLDY PDWIRITGYW FLSEGGNWTP PTDLLDFIHR ARSDGKKIVY IGFGSIVVSD
PSALTRTVVE SVLKADVRCI LSKGWSDRLG DPASAKVEIP LPPEIFQIQA APHDWLFSQI
DAAAHHGGAG TTGASLRAGV PTIVKPFFGD QFFFGTRVED LGVGICMKKL NVSVFSRALW
EATHSERMIV KARELGAQIR SENGVDTAIQ AIYRDLEYAK TLARQRSIVS STPFSPTPSA
KTTAEQEEDD VDDSEEWTFV GDDTEIDVSR RLRDRAVSDA DMLPEPVTSA S
//
