ID A1Y2M1_LEIAM Unreviewed; 441 AA.
AC A1Y2M1;
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:ABI17921.1};
RN [1] {ECO:0000313|EMBL:ABI17921.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BTO13 {ECO:0000313|EMBL:ABI17921.1};
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; DQ836159; ABI17921.1; -; Genomic_DNA.
DR AlphaFoldDB; A1Y2M1; -.
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:ABI17921.1};
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:ABI17921.1"
FT NON_TER 441
FT /evidence="ECO:0000313|EMBL:ABI17921.1"
SQ SEQUENCE 441 AA; 48463 MW; 0405D5A9EF735FCE CRC64;
AFAVAAHAPV LGLIPLGSIV AYVGTLRYIP NVARTLLDRN IFGIDINKST EEQRQKFAAK
RRAGQTEEKE FQKQAIPESL GILVGAMYLS VVVVLTVCLR FLGAAGEGLG NPYASLPGPL
MTITVMLLLG FVDDVLDVKW RHKIILTALG SLPLIMTYDG SLSVLMPCAF GRFGLSTMNV
MKEWRLGLAA PQSEPTTTFR ATAPSTWFSF TVNHRSYVKV TESGAALIYL GPVYLVYLSM
LCIFCTNSIN ILAGVNGVEV GQSIVIAVAS VVYNLFQMRL DRQLTPDFSS LDAAAADARD
MTSDHQLRAL LLLGPFIGVS LALWRYNRYP ARVFVGDSYT YFAGTVLAVS SITGVYSKTL
LLFFAPQVFN FLISLPQLFS IVPCPRHRVP TWNPRTNLLS NNHNYTILNV ILYLFGDMHE
AKLTWAILKC QVIACVLGFV V
//
