ID A0A016WFS3_9BILA Unreviewed; 450 AA.
AC A0A016WFS3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
GN Name=Acey_s0741.g1979 {ECO:0000313|EMBL:EYC38122.1};
GN ORFNames=Y032_0741g1979 {ECO:0000313|EMBL:EYC38122.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC38122.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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}.
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:EYC38122.1}.
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DR EMBL; JARK01000341; EYC38122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016WFS3; -.
DR Proteomes; UP000024635; 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:SF62; GLUCURONOSYLTRANSFERASE; 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:UP000024635};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..450
FT /note="UDP-glucuronosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012000214"
SQ SEQUENCE 450 AA; 51175 MW; 1E449739AAC924D7 CRC64;
MRLSLVVLLW TSSDAAKIIF NGMHSSDSHI ASMLPLATRL AQEHHSIHFL ETNTKSSHYR
YPNNISFTHI QLKKDPYFLY VVLKVMWTKI YGPIEFPRVW QTGDNAFVET LEEHPQKVNP
VIDEPWDLVF ADELFAVSSY ALAMRAQQRG RPFVTLSTCI PTNLLKYHLS LGTPFAMRPS
MYHRNAVPYL IETFANRLHA VIQETWVAIR VQYVTAYNAV QGLNRIGIVD FDFSKLAKLS
AYIFLDDVNS LVFPSSVGTE IIEVGFHCPR KEELSQEYLD FVNDPFSRGT ILIAFGSNVV
WDYASDELME TVVVALNRLS EYRVVFSYNG DRKRVTLLGR HVKITRWAPQ KGILSHNKTV
AFISHGGLKS LKDTICGGVP VVYIPLFAEQ SHNGEVARSA GFAETLSKTR LTSDLIEKTV
RRVAECLCIC FHVKLTQELK KKENRARSLL
//