ID B3RST8_TRIAD Unreviewed; 400 AA.
AC B3RST8;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
GN ORFNames=TRIADDRAFT_22929 {ECO:0000313|EMBL:EDV27102.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV27102.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV27102.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV27102.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor
CC beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17;
CC Evidence={ECO:0000256|RuleBase:RU362059};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362059}; Single-
CC pass membrane protein {ECO:0000256|RuleBase:RU362059}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009995, ECO:0000256|RuleBase:RU003718}.
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DR EMBL; DS985243; EDV27102.1; -; Genomic_DNA.
DR RefSeq; XP_002111098.1; XM_002111062.1.
DR AlphaFoldDB; B3RST8; -.
DR STRING; 10228.B3RST8; -.
DR EnsemblMetazoa; TriadT22929; TriadP22929; TriadG22929.
DR GeneID; 6751793; -.
DR KEGG; tad:TRIADDRAFT_22929; -.
DR CTD; 6751793; -.
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_012949_3_1_1; -.
DR InParanoid; B3RST8; -.
DR OMA; IRMFINA; -.
DR OrthoDB; 382054at2759; -.
DR PhylomeDB; B3RST8; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR PANTHER; PTHR48043:SF161; 2-HYDROXYACYLSPHINGOSINE 1-BETA-GALACTOSYLTRANSFERASE; 1.
DR PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR Pfam; PF00201; UDPGT; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU003718}; Membrane {ECO:0000256|RuleBase:RU362059};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718};
KW Transmembrane {ECO:0000256|RuleBase:RU362059};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362059}.
FT TRANSMEM 363..380
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362059"
SQ SEQUENCE 400 AA; 45366 MW; 0B8F3329DEDACA46 CRC64;
MAAQKRYCDA TLSNKTLLQS LKDIDIVVSD GVYVCSILLP EVLQKPFINI YFNGGILGVH
TFYGRYRPAS YVPTHPSLTS RKLSFFERLI SVIGKLVMER IFQWDCEKVA EQLRSKHNIS
THLSLAQLQR KLSLHLSALD FSIEYPRPIP PYVHLVGPLS PQSPSPLPQI FENFIQNSKQ
GAILMSFGSE LQLEDYKVSE MIKALSQLPY NVIWKTKQTV DNLPENVKTF GWTPQNDILG
HKRIVALITH CGSNSLYEAA YHGVPMIAMP SMIEQQLNAQ RMKHAGIGLE VDFYSFTSED
IINAINALAA SPRYKENVQK ISKILKSSKS ARDTVVDWVE YAVDTDGAHH LKVQGEMLSF
YELYNLDVFA FIILMLYISY RLLNYVTNRI CCSTTKAKSD
//
