ID C6LWC7_GIAIB Unreviewed; 192 AA.
AC C6LWC7;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase {ECO:0000256|ARBA:ARBA00012614};
DE EC=2.4.1.141 {ECO:0000256|ARBA:ARBA00012614};
GN ORFNames=GL50581_3085 {ECO:0000313|EMBL:EES99682.1};
OS Giardia intestinalis (strain ATCC 50581 / GS clone H7) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=598745 {ECO:0000313|EMBL:EES99682.1, ECO:0000313|Proteomes:UP000002488};
RN [1] {ECO:0000313|EMBL:EES99682.1, ECO:0000313|Proteomes:UP000002488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50581 / GS clone H7 {ECO:0000313|Proteomes:UP000002488};
RX PubMed=19696920; DOI=10.1371/journal.ppat.1000560;
RA Franzen O., Jerlstrom-Hultqvist J., Castro E., Sherwood E., Ankarklev J.,
RA Reiner D.S., Palm D., Andersson J.O., Andersson B., Svard S.G.;
RT "Draft genome sequencing of giardia intestinalis assemblage B isolate GS:
RT is human giardiasis caused by two different species?";
RL PLoS Pathog. 5:E1000560-E1000560(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl
CC diphosphodolichol + UDP; Xref=Rhea:RHEA:23380, Rhea:RHEA-COMP:9519,
CC Rhea:RHEA-COMP:9520, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58427;
CC EC=2.4.1.141; Evidence={ECO:0000256|ARBA:ARBA00000601};
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000256|ARBA:ARBA00006962}.
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:EES99682.1}.
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DR EMBL; ACGJ01002540; EES99682.1; -; Genomic_DNA.
DR EnsemblProtists; EES99682; EES99682; GL50581_3085.
DR VEuPathDB; GiardiaDB:GL50581_3085; -.
DR OMA; HENHQAE; -.
DR OrthoDB; 167601at2759; -.
DR Proteomes; UP000002488; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004577; F:N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR039042; Alg13-like.
DR InterPro; IPR007235; Glyco_trans_28_C.
DR PANTHER; PTHR12867; GLYCOSYL TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR12867:SF6; N-ACETYLGLUCOSAMINYLDIPHOSPHODOLICHOL N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR Pfam; PF04101; Glyco_tran_28_C; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:EES99682.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 173..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..120
FT /note="Glycosyl transferase family 28 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04101"
SQ SEQUENCE 192 AA; 20653 MW; DD3D96722381D528 CRC64;
MHVFTSVGTT RFDELVSIFS DEEVLGALVR AGVTRLTVQH GSSLFKAPLL GSGVGLEVRS
FDYAPSLASY LEDADLVFSH AATGIYLEAM QLQLPHLLVV NTSLHENHQA ELAGLLADSS
RCRTFADVGA FRAYLLSGAL ARDFLLMKNS AAIIQPQAPP ALLETFTRVP RRXGLLGXAL
AVALLLVLIR IS
//
