ID A1Y2L2_LEIDO Unreviewed; 441 AA.
AC A1Y2L2;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase {ECO:0000256|ARBA:ARBA00017659};
DE EC=2.7.8.15 {ECO:0000256|ARBA:ARBA00013225};
DE AltName: Full=GlcNAc-1-P transferase {ECO:0000256|ARBA:ARBA00029567};
DE AltName: Full=N-acetylglucosamine-1-phosphate transferase {ECO:0000256|ARBA:ARBA00033238};
DE Flags: Fragment;
OS Leishmania donovani.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5661 {ECO:0000313|EMBL:ABI17912.1};
RN [1] {ECO:0000313|EMBL:ABI17912.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Jun1 {ECO:0000313|EMBL:ABI17912.1};
RX PubMed=17142569; DOI=10.1128/EC.00282-06;
RA Waki K., Dutta S., Ray D., Kolli B.K., Akman L., Kawazu S., Lin C.P.,
RA Chang K.P.;
RT "Transmembrane molecules for phylogenetic analyses of pathogenic protists:
RT Leishmania-specific informative sites in hydrophilic loops of
RT trans- endoplasmic reticulum N-acetylglucosamine-1-phosphate transferase.";
RL Eukaryot. Cell 6:198-210(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-
CC acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP;
CC Xref=Rhea:RHEA:13289, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9519,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:58427; EC=2.7.8.15;
CC Evidence={ECO:0000256|ARBA:ARBA00034004};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family.
CC {ECO:0000256|ARBA:ARBA00009317}.
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DR EMBL; DQ836150; ABI17912.1; -; Genomic_DNA.
DR AlphaFoldDB; A1Y2L2; -.
DR VEuPathDB; TriTrypDB:LdBPK_364390.1; -.
DR VEuPathDB; TriTrypDB:LdCL_360051000; -.
DR VEuPathDB; TriTrypDB:LDHU3_36.5950; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd06855; GT_GPT_euk; 1.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR033895; GPT.
DR PANTHER; PTHR10571; UDP-N-ACETYLGLUCOSAMINE--DOLICHYL-PHOSPHATE N-ACETYLGLUCOSAMINEPHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR10571:SF0; UDP-N-ACETYLGLUCOSAMINE--DOLICHYL-PHOSPHATE N-ACETYLGLUCOSAMINEPHOSPHOTRANSFERASE; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABI17912.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABI17912.1"
FT NON_TER 441
FT /evidence="ECO:0000313|EMBL:ABI17912.1"
SQ SEQUENCE 441 AA; 48748 MW; 6283D8595900566B CRC64;
AFAVAAHAPV LGLILLGSIV AYVGTMRYIP NVARTLLERN IFGIDINKNT EEQRQKFAAK
RRAGQTEEKE FQKQAIPESL GILVGAVYLS VVMVLTVCLR FLGAAGEGSD NPYVSLPGPL
MTITLMLLLG FVDDVLDVKW RHKIILTTLG SLPLIMTYDG SLSVLMPCVF GRFGLPTMNV
TKKWLLGLAA RQGEPTTTFR VTAPSTWFSY VVNHRSYVKV SESGTALIYL GPVYLVYLSM
LCIFCTNSIN ILAGVNGVEV GQSIVIAVAS VVYNLFQMRL ERQARPALRS VDAAAADARD
MTSDHQLRAL LLLGPFIGVS LALWRYNRYP ARVFVGDSYT YFAGTVLAVS SITGVYSKTL
LLFFAPQVFN FIISLPQLFS IVPCPRHRVP TWNPRTNLLS NSHNYTILNV VLYLFGDMHE
EKLTWAILKC QVIACVFGFV V
//
