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P42864

- GPT_LEIAM

UniProt

P42864 - GPT_LEIAM

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Protein

UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase

Gene

NAGT

Organism
Leishmania amazonensis
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the initial step in the synthesis of dolichol-P-P-oligosaccharides.

Catalytic activityi

UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-D-glucosaminyl-diphosphodolichol.

Enzyme regulationi

Inhibited by tunicamycin.

Pathwayi

GO - Molecular functioni

  1. phospho-N-acetylmuramoyl-pentapeptide-transferase activity Source: InterPro
  2. transferase activity, transferring glycosyl groups Source: UniProtKB-KW
  3. UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase (EC:2.7.8.15)
Alternative name(s):
GlcNAc-1-P transferase
Short name:
G1PT
Short name:
GPT
N-acetylglucosamine-1-phosphate transferase
Gene namesi
Name:NAGT
OrganismiLeishmania amazonensis
Taxonomic identifieri5659 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3221HelicalSequence AnalysisAdd
BLAST
Transmembranei91 – 11121HelicalSequence AnalysisAdd
BLAST
Transmembranei124 – 14421HelicalSequence AnalysisAdd
BLAST
Transmembranei156 – 17621HelicalSequence AnalysisAdd
BLAST
Transmembranei236 – 25621HelicalSequence AnalysisAdd
BLAST
Transmembranei263 – 28321HelicalSequence AnalysisAdd
BLAST
Transmembranei316 – 33621HelicalSequence AnalysisAdd
BLAST
Transmembranei345 – 36521HelicalSequence AnalysisAdd
BLAST
Transmembranei374 – 39421HelicalSequence AnalysisAdd
BLAST
Transmembranei442 – 46221HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 466466UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferasePRO_0000108763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 4 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR000715. Glycosyl_transferase_4.
[Graphical view]
PfamiPF00953. Glycos_transf_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42864-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLGLVESSR NAAFAVAAHA PVLGLILLGS IVAYVGTLRY IPNVARTLLD
60 70 80 90 100
RNIFGIDINK STEEQRQKFA AKRRAGQTEE KEFQKQAIPE SLGILVGAMY
110 120 130 140 150
LSVVVVLTVC LRFLGAAGEG LDNPYASLPG PLMTITVMLL LGFVDDVLDV
160 170 180 190 200
KWRHKIILTA LGSLPLIMTY DGSLSVLMPC AFGRFGLSTM NVMKEWRLGL
210 220 230 240 250
AAPQGEPTTT FRATAPSTWF SFTVNHRSYV KVTESGAALI YLGPVYLVYL
260 270 280 290 300
SMLCIFCTNS INILAGVNGV EVGQSIVIAV ASVVYNLFQM RLDRQLTPDF
310 320 330 340 350
SSLDAAAADA RDMTSDHQLR ALLLLGPFIG VSLALWRYNR YPARVFVGDS
360 370 380 390 400
YTYFAGTVLA VSSITGVYSK TLLLFFAPQV FNFLISLPQL FSIVPCPRHR
410 420 430 440 450
VPTWNPRTNL LSNSHNYTIL NVILYLFGDM HEAKLTWAIL KCQVIACVLG
460
FVVRYVLSAF LYDEVR
Length:466
Mass (Da):51,352
Last modified:November 1, 1995 - v1
Checksum:i4C423662BA4072AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96635 Genomic DNA. Translation: AAA29258.1.
PIRiA44495.
S27823.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96635 Genomic DNA. Translation: AAA29258.1 .
PIRi A44495.
S27823.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00378 .

Family and domain databases

InterProi IPR000715. Glycosyl_transferase_4.
[Graphical view ]
Pfami PF00953. Glycos_transf_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The 63-kilobase circular amplicon of tunicamycin-resistant Leishmania amazonensis contains a functional N-acetylglucosamine-1-phosphate transferase gene that can be used as a dominant selectable marker in transfection."
    Liu X., Chang K.-P.
    Mol. Cell. Biol. 12:4112-4122(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MHOM/BR/73/LV78.

Entry informationi

Entry nameiGPT_LEIAM
AccessioniPrimary (citable) accession number: P42864
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

In Leishmania sp., tunicamycin-resistant variants are associated with increased levels of NAGT gene transcription due to gene amplification.

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3