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Database: UniProt
Entry: A0A0B1RTG4_OESDE
LinkDB: A0A0B1RTG4_OESDE
Original site: A0A0B1RTG4_OESDE 
ID   A0A0B1RTG4_OESDE        Unreviewed;       407 AA.
AC   A0A0B1RTG4;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE            EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
DE   Flags: Fragment;
GN   ORFNames=OESDEN_24422 {ECO:0000313|EMBL:KHJ75959.1};
OS   Oesophagostomum dentatum (Nodular worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX   NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ75959.1, ECO:0000313|Proteomes:UP000053660};
RN   [1] {ECO:0000313|EMBL:KHJ75959.1, ECO:0000313|Proteomes:UP000053660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ75959.1,
RC   ECO:0000313|Proteomes:UP000053660};
RA   Mitreva M.;
RT   "Draft genome of the hookworm Oesophagostomum dentatum.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000301,
CC         ECO:0000256|RuleBase:RU362059};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167,
CC       ECO:0000256|RuleBase:RU362059}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167, 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; KN612232; KHJ75959.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B1RTG4; -.
DR   Proteomes; UP000053660; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
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; EG:EG0003.4 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR48043:SF162; UDP-GLYCOSYLTRANSFERASE FAMILY 305 MEMBER A1, ISOFORM A-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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053660};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KHJ75959.1"
SQ   SEQUENCE   407 AA;  46652 MW;  EFF9EDBC4A5F3510 CRC64;
     LYQTLFIVEL DPDFKYSTGT QFVNHIIRYS SPYHNSADWR SLTFKRNEVF NSILGFNFID
     LIKVQMYAYR VCKGILEDSG LIRLMHDSKF DLGVFEMFHH CPAGVMELAG IPKTMLVSAI
     GIGYHHYRLL GMERQSSFVP ASFTMCGGRM TFLERLYNVF INGCGFVFSN IFEHFEQSLF
     ERRFPGFKVL HDLVKDKTDF MLMNSNEFTE STRPTLRSIQ YVGGATIPEP EPLDEDFDWI
     LSRGSKGAIL FSLGSLVKPS NMPLAFREGA FIFIDTFVDA FRAFPDYSVL WKDDIEMNFT
     YPNIHFREWV PQVDLLADGR VKLFITHCGM NSMQESLLFG VPMVTIPLFA DQDSNAAVAA
     ERGYSVNLNK LSITTEKIID AISAVLGKPG EERYRITSYF LRLIQYV
//
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