ID W6QIJ6_PENRF Unreviewed; 1364 AA.
AC W6QIJ6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:CDM34029.1};
GN ORFNames=PROQFM164_S03g000753 {ECO:0000313|EMBL:CDM34029.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM34029.1};
RN [1] {ECO:0000313|EMBL:CDM34029.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM34029.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792017; CDM34029.1; -; Genomic_DNA.
DR STRING; 1365484.W6QIJ6; -.
DR OMA; WRNKTLG; -.
DR OrthoDB; 76239at2759; -.
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:CDM34029.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 283..380
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1329
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 83..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1364 AA; 152954 MW; 38E40BD6B36C9489 CRC64;
MKPFRDDAKR RADRQLSASM KPTSSNRPFS DRVPDKFKDG DDAQFDFTAP PQGMGSRDGN
VHYMQQSLFS MIAAVGSKSD FHARFEESSD SDGDMEEHPW MEQTSGNPSS RTPVPSLDSR
QPSKRPESNT LVLEERGRRH QRTRSDNKLL QRLPKLDSED EASESSNSID PMLKVPPLRR
TRSATPRAAP VLSRMVEAQS HFDLTSATPH SPPNLNKPME DQPESSASAL STRLMKMFEF
AKPEKVLVEY ACSLLQSMLL QGYMYVTEGH ICFYAYLPKK SNVAIKSGYL SKRGRKNPTY
HRYWFALKGD VLSYYADPSN LYFPSGHVDL RYGISASLAD RKDGDVKDFQ VTTDQRTYLF
RADSATSAKE WVKALQKVIF RTHNEGDSVK VSFPIANIID LEESPMADFA ETFKIRVLDS
GETYAIDEYF FSFFDSDQDA FNYIKRLVNA ASATSAMKEP QSQHDIKNQK RQSVSSVRLS
DQRQEVSPRK RSSSVGHENQ GSTDSFAEQG TESSPIVQSM TDTTESASQI LHRSDVFQSP
TMRTLQGRSL GVGENIQRNS DDTTPSASTR LDLGAATGSP SRTLGRNETT EDTRYIAGES
NTMQSSGPSS VTHLNDLVKV GAYPLQRAAG FAEYLKSRSK QMSTLLATES MGYIEKVSGM
WIGGQKHYGE REGPLLEDQN VDPEDNEGSF NYGDRFRAHF ALPSTEKLQA TYYAYLHRVL
PLYGKIYISQ KKLCFRSLIP GTRTKMILPF KDIENVEKEK GFRFGYHGLV VIIRGHEELF
FEFNASDSRD DCAVTLHQNL ESVKFLVESG LLAEEERDEV EAAKAEHRML QEARLDSPEE
DDARPTFTED SSEIHPFFDD PRASIINFKP SEPLRITCLT IGSRGDVQPY IALCKGLLAE
GHKPKIATHA EFEPWIRKHG IDFAPVDGDP AELMRICVEN GMFTYSFLRE ASMKFRGWID
DLLSSAWIGC QGSDLLIESP SAMAGIHIAE ALRIPYFRGF TMPWTRTRAY PHAFAVPENR
MGGAYNYITY VMFDNIFWKA IAGQVNRWRN NELGLKATTL DKMQQNKVPF LYNYSPSVVV
PPLDYPDWIR ITGYWFLNEG TDWTPPTELS NFIAQARADG KKLVYIGFGS IVVSDPSALT
RTVIESVQKA DVRCILSKGW SDRLGDPAST KTEIPLPPEI HQIQSAPHDW LFSQIDAAAH
HGGAGTTGAS LRAGVPTIIK PFFGDQFFFG SRVEDLGVGI CLKKLNVSVF SRALWEATHS
ERMIMRATNL GVQIRNEDGV ATAIQALYRD LEYAKTLARQ KSLASSTPFS PTPTAKTSPD
GADDDLDDIE EWTFVGDETG FDISKRMRER AASDADRLGS NMFQ
//
