ID A0A0A2L1M4_PENIT Unreviewed; 1387 AA.
AC A0A0A2L1M4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=PITC_015550 {ECO:0000313|EMBL:KGO70510.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO70510.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO70510.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO70510.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(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}.
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:KGO70510.1}.
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DR EMBL; JQGA01001039; KGO70510.1; -; Genomic_DNA.
DR STRING; 40296.A0A0A2L1M4; -.
DR HOGENOM; CLU_000537_6_0_1; -.
DR OMA; YYAYLHR; -.
DR OrthoDB; 76239at2759; -.
DR PhylomeDB; A0A0A2L1M4; -.
DR Proteomes; UP000030104; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGO70510.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 281..378
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1387 AA; 154876 MW; DA4D1CFB5240C11D CRC64;
MRPLRDDAKR RADRQLSASM KPTSSNRPFS DRVPDRFKDG DDAQFDFTAP PRGMGSRDGN
VHYMQQSLFS MIAAVGSKLD FHARFDESSD SDAEMEPQIE QTSGKLSSRT PAPTLDSRQP
SKRLESNTLV LEERGRRHQR TRSDNKLLQR LPRLDSEGGA NESSNQPDSL LKMPPVRRTR
SATPRAAPVL SRMVEAQSHF DLTSATPYLP PNPSKSTEDQ PQSSASALST RLMKMFGFAK
PEKVLVEYAC SLLQSMLLQG YMYVTEGHIC FYAYLPKKSN VAIKSGCLSK RGRKNPTYHR
YWFALKGDVL SYYADPSNLY FPSGHVDLRY GISASLADRK DGDAKDFQVT TDQRTYLYRA
DSATSAKEWV KALQKVIFRT HYEGDSVKVS FPIANVIDLE ESPMADFAET FKIRVLDSGE
TYAIDEVGRG TKRYHGSLLI TSQYFFSFFD SSQEAFNYIK GLVNAASAAT AMKEPQGEHD
IQYQPESSRT THKRQSVSSV RVSDQRQRDS PRKRSSSVGI ENQGSADSFA EQGTGSSPII
QSMTETTESA SQILHRSDVF QSPTMHTLQR RTLDVGETAR RRSDDMTPSA SARLDLDAAA
GSPSGTLGGN ETTEDMRRVT GQSNPMQSSG PSSVTHLNEL VKAGAYPLQR AAGFAEYLKS
RSKQMSTLLA TESMGYIEKV SGMWIGGQKH YGEREGPLLE DQNVDPEDNE GAFNYGDRFR
AHFALPSSEK LQATYYAYLH RVLPLYGKIY ISQKKLCFRS LIPGTRTKMI LPFKDIENVE
KEKGFRFGYH GLVVIIRGHE ELFFEFNASG SRDDCAVTLH QNLESVKFLV ESGLLADEER
DEVEAAKAEH RMLQEARLDG PEEHDARPSL TEDSSETHPF FDDPRASIIN FKPLESLRIT
CLTIGSRGDV QPYIALCKGL LAEGHKPKIA THAEFEPWIR KHGIDFAPVD GDPAELMRIC
VENGMFTYSF LREASLKFRG WIDDLLSSAW IGCQGSDLLI ESPSAMAGVH IAEALRIPYF
RGFTMPWTRT RAYPHAFAVP ENRMGGAYNY ITYVMFDNIF WKAIAGQVNR WRNNELGLKA
TTLNKMQQNK VPFLYNYSPS VVAPPLDYPD WIRITGYWFL NEGTDWTPPI ELSNFISQAR
ADGKKLVYIG FGSIVVSDPA ALTRTVIESV QKADVRCILS KGWSDRLGDP ASMKTEIPLP
PAIHQIQSAP HDWLFSQIDA AAHHGGAGTT GASLRAGVPT IVKPFFGDQF FFGSRVEDLG
VGICMKKLNV SVFSRALWEA THSERMIVKA RNLGIQIRNE DGVATAIQAI YRDLEYAKTL
ARQKSLASST PFSPTPTAKT SPDGGDDDLD DIEEWTFVGD ETGFDISKRM RDRAASDADR
LGSNMFQ
//