UGT52_DICDI
ID UGT52_DICDI Reviewed; 1697 AA.
AC Q54IL5; Q9XYD4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=UDP-sugar-dependent glycosyltransferase 52;
DE EC=2.4.1.173;
DE AltName: Full=Sterol 3-beta-glucosyltransferase;
DE AltName: Full=UDP-glycosyltransferase 52;
GN Name=ugt52; ORFNames=DDB_G0288655;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 594-1697, AND FUNCTION.
RX PubMed=10224056; DOI=10.1074/jbc.274.19.13048;
RA Warnecke D.C., Erdmann R., Fahl A., Hube B., Mueller F., Zank T.,
RA Zaehringer U., Heinz E.;
RT "Cloning and functional expression of UGT genes encoding sterol
RT glucosyltransferases from Saccharomyces cerevisiae, Candida albicans,
RT Pichia pastoris, and Dictyostelium discoideum.";
RL J. Biol. Chem. 274:13048-13059(1999).
CC -!- FUNCTION: Involved in the biosynthesis of sterol glucoside. Can use
CC different sterols such as cholesterol, sitosterol, and ergosterol as
CC sugar acceptors. {ECO:0000269|PubMed:10224056}.
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 -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD28546.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AAFI02000119; EAL63104.1; -; Genomic_DNA.
DR EMBL; AF098916; AAD28546.1; ALT_INIT; mRNA.
DR RefSeq; XP_636616.1; XM_631524.1.
DR AlphaFoldDB; Q54IL5; -.
DR SMR; Q54IL5; -.
DR STRING; 44689.DDB0191537; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PaxDb; Q54IL5; -.
DR PRIDE; Q54IL5; -.
DR EnsemblProtists; EAL63104; EAL63104; DDB_G0288655.
DR GeneID; 8626744; -.
DR KEGG; ddi:DDB_G0288655; -.
DR dictyBase; DDB_G0288655; ugt52.
DR eggNOG; KOG1032; Eukaryota.
DR eggNOG; KOG1192; Eukaryota.
DR eggNOG; KOG1819; Eukaryota.
DR HOGENOM; CLU_240996_0_0_1; -.
DR InParanoid; Q54IL5; -.
DR OMA; CFAGPHI; -.
DR BRENDA; 2.4.1.173; 1939.
DR Reactome; R-DDI-156588; Glucuronidation.
DR Reactome; R-DDI-189483; Heme degradation.
DR Reactome; R-DDI-9749641; Aspirin ADME.
DR Reactome; R-DDI-9753281; Paracetamol ADME.
DR Reactome; R-DDI-9754706; Atorvastatin ADME.
DR PRO; PR:Q54IL5; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0051507; F:beta-sitosterol UDP-glucosyltransferase activity; IDA:dictyBase.
DR GO; GO:0102203; F:brassicasterol glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102205; F:cholesterol alpha-glucosyltransferase activity; IDA:dictyBase.
DR GO; GO:0051506; F:ergosterol UDP-glucosyltransferase activity; IDA:dictyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102202; F:soladodine glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0051508; F:stigmasterol UDP-glucosyltransferase activity; IDA:dictyBase.
DR GO; GO:0051509; F:tomatidine UDP-glucosyltransferase activity; IDA:dictyBase.
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 GO; GO:0016125; P:sterol metabolic process; IDA:dictyBase.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR Gene3D; 2.30.29.30; -; 4.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR007235; Glyco_trans_28_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 InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF04101; Glyco_tran_28_C; 1.
DR Pfam; PF03033; Glyco_transf_28; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00568; GRAM; 2.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase; Lipid biosynthesis; Lipid metabolism; Metal-binding;
KW Reference proteome; Repeat; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1697
FT /note="UDP-sugar-dependent glycosyltransferase 52"
FT /id="PRO_0000367478"
FT DOMAIN 234..332
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 658..793
FT /note="GRAM 1"
FT DOMAIN 881..948
FT /note="GRAM 2"
FT ZN_FING 1622..1685
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 20..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1628
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1631
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1655
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1658
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1680
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 1697 AA; 190915 MW; 9364E429FD85A618 CRC64;
MDEFTSDSLT TSRLLRQISH SDSLSSVGSS SNRSNSNYEN KINNGIINDF DSTNANDGIS
NNSNNSNNNN NSSSILKIHQ SPQSILSTEQ QHQIQQYQQY HQQQIYESGY VPPHVYIFDP
DYKSNNDEED KEKRSLIELN KSTDLSNIKT TTTTTTTTTP PPLMIPENEE ENKQLRQEIL
NELSKSESFT KIKEPGEIYG FCECSLLYNH LTCANLVITS NYLIFLPQQQ VDSDYVLENY
LYKKGDFFWK KYWFVLTPDS ISWYKSSILK ETHYPNGTIL LSKIVTVDKL DPEETGKPFC
LQIMTNTSIH LIQLDTEPQL EHWYHEINRM QKNLNVTIPI GDIVSITMES NAALFFDSLC
LTLKKGENCL VTPSSSSNEV YSLLIKLWNR NRGVTVVEPE KQQRLLEFQK TFKLSQGVNL
LIETPCVFYQ DEEFSYEGVL YATTEGTLYF SSLDSVLIIP ESDIYAITID RKSDNRDALK
VYTTDYDVLF FDSIDDIETF FNVISTSLAR SNPKIFFSTV GQIPPIDEPK HDEKEHKSTY
QTISSGIRSW KIPIPSLPNF SIPIPKSIPI PLFRSKSSSH LDPQNSQQQQ QQQQQSSSLQ
LDDNNNNIVI PHTSNPTTII PSTSSSSAIP PPPSSTSSTS STTHEKTIII QKNSSINSTF
HDIFPLLPLD ETVIMFQNCS LYYYSYDSNV EGIVYITKSY IAFNPSPLDK QQQQQQQQQQ
QQPNSSSITS TTYDRDLDTD SDTDSESDFD YPKQSQHDNS VVMVNNNQYK VKEVLMKKAL
IPIEDIVSVT KERFLLFFNQ CVKIITLDHK WIFGSLNNIN SFYNLILETW KQIPKTLLDS
SSSSSSSSSS SLLSSSPNNN NSDLNINGNS EGSIFTPLES IKIKNKLGLP ADEVLITWFN
CTNFKGAQLK YGFLYISNNN ICFRSKFGFQ KRTIVIPLSQ VIEIKKYSAF IPNGIKITTA
SHHEFQFASF IHRNRVYQIL YETWLKANNK KSNSSNSLSS SPTITSPLAI SPSIASPSIT
PPSSTPPSST TPSSTTPTIT SPTIHSTLPS TVVYNDIQEI IDGENNSNNN NNNNNTNNTN
KSNSFIGNVE EDVDKIKRSI KSLPILKIHS AQQQQQQQPK TTTTTTSTTT TNLISPRLLT
PLTITQSPGF SSLVNSPILP VKPLRITILT IGSRGDIQPF IALSLGLKEY GHNVTLATHE
LYRDLISKEF GLNYQPLGGD PRELMDLCVR NGIFTPKFIK EALSRFRSFI DDLLLTCWKA
VQNSNTQVLI ATPGCFAGPH IGEVLQIPFF NAFTMPFTRT RTYPNPFAPF ASHQMGGVFN
LATHVMMEKV LWQPISGQIN QWRTETLKIP PWNSSVSINE TYRMPYLYCF SKYLVPKPPD
WSGEIAITGY WTLKNQANSD SPPDDLIQFL NEESSTENDD IPIYIGFGSI VIDNPTALSL
LLIEAIKLSG KRAIISQGWG GLSIDEHNNN NNNNNNNNNG ENSDSNKSSL QSNRIYLLKK
PVDHSWLFEK VSLVISHGGA GTVAASLLAA KPTIVVPFFG DQFFWGERIK QTGIGTSIPF
DILTAKSLSS HIISILNEPS VRAKVNKMSH LLKREDGVKT AIDFIHRYLP FSFIPPREIP
FSSAPNSCMG CKQPFTLLHV MKARVHCHCC GKIFCESCTS HKCPIKKYRI NTPVRVCDKC
FNDLQSNPSS NSFILND
