ID A1Y2M2_LEIAM Unreviewed; 441 AA.
AC A1Y2M2;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 39.
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 amazonensis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5659 {ECO:0000313|EMBL:ABI17922.1};
RN [1] {ECO:0000313|EMBL:ABI17922.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LUO {ECO:0000313|EMBL:ABI17922.1};
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; DQ836160; ABI17922.1; -; Genomic_DNA.
DR AlphaFoldDB; A1Y2M2; -.
DR VEuPathDB; TriTrypDB:LAMA_000349000; -.
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:ABI17922.1};
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:ABI17922.1"
FT NON_TER 441
FT /evidence="ECO:0000313|EMBL:ABI17922.1"
SQ SEQUENCE 441 AA; 48554 MW; A43EB5449FB56F0C CRC64;
AFAVAAHAPV LGLILLGSIV AYVGTLRYIP NVARTLLDRN IFGIDINKST EEQRQKFAAK
RRAGQTEEKE FQKQAIPESL GILVGAMYLS VVVVLTVCLR FLGAAGEGLD NPYASLPGPL
MTITVVLLLG FVDDVLDVKW RHKIILTALG SLPLIMTYDG SLSVLMPCAF GRFGLSTMNV
MKEWRLGLAA PQGEPTTTFR ATAPSTWFSF TVNHRSYVKV TESGAALIYL GPVYLVYLSM
LCIFCTNSIN ILAGVNGVEV GQSIVIVVAS VVYNLFQMRL DRQLTPDFSS LDAAAADARD
MTSDHQLRAL LLLGPFIGVS LALWRYNRYP ARVFVGDSYT YFAGTVLAVS SITGVYSKTL
LLFFAPQVFN FLISLPQLFS IVPCPRHRVP TWNPRTNLLS NSHNYTILNV VLYLFGDMHE
EKLTWAILKC QVIACVFGFV V
//
