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Protein

Glucosamine 6-phosphate N-acetyltransferase

Gene

GNA1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acetyltransferase involved in UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthesis. UDP-GlcNAc is an essential metabolite that serves as an initial sugar donor for N-glycan synthesis and thus plays an important role in protein and lipid glycosylation.2 Publications

Catalytic activityi

Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate.1 Publication

Kineticsi

  1. KM=33 µM for acetyl-coenzyme A1 Publication
  2. KM=231 µM for glucosamine-6-phosphate1 Publication

    pH dependencei

    Optimum pH is 7.0-8.0.1 Publication

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.1 Publication

    Pathwayi: UDP-N-acetyl-alpha-D-glucosamine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I).
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Glucosamine 6-phosphate N-acetyltransferase (GNA1)
    2. Phosphoacetylglucosamine mutase (DRT101)
    This subpathway is part of the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I), the pathway UDP-N-acetyl-alpha-D-glucosamine biosynthesis and in Nucleotide-sugar biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei27SubstrateBy similarity1

    GO - Molecular functioni

    • glucosamine 6-phosphate N-acetyltransferase activity Source: TAIR

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.3.1.4. 399.
    ReactomeiR-ATH-446210. Synthesis of UDP-N-acetyl-glucosamine.
    UniPathwayiUPA00113; UER00529.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucosamine 6-phosphate N-acetyltransferase (EC:2.3.1.41 Publication)
    Alternative name(s):
    Glucose-6-phosphate acetyltransferase 1
    Short name:
    AtGNA1
    Phosphoglucosamine acetylase
    Phosphoglucosamine transacetylase
    Protein LIGNESCENS
    Gene namesi
    Name:GNA1
    Ordered Locus Names:At5g15770
    ORF Names:F14F8.150
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G15770.

    Subcellular locationi

    GO - Cellular componenti

    • endoplasmic reticulum Source: TAIR
    • endoplasmic reticulum membrane Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Retarded vegetative growth, delayed flowering and short and thick inflorescence stems and siliques.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi68G → S in lig; reduces activity 2-fold. Retarded growth. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004210371 – 149Glucosamine 6-phosphate N-acetyltransferaseAdd BLAST149

    Proteomic databases

    PaxDbiQ9LFU9.

    Expressioni

    Tissue specificityi

    Expressed in roots, leaves, stems, cauline leaves, flowers and siliques.1 Publication

    Gene expression databases

    GenevisibleiQ9LFU9. AT.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi3702.AT5G15770.1.

    Structurei

    Secondary structure

    1149
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 9Combined sources5
    Helixi12 – 16Combined sources5
    Helixi19 – 23Combined sources5
    Turni24 – 26Combined sources3
    Helixi34 – 45Combined sources12
    Helixi46 – 50Combined sources5
    Beta strandi51 – 58Combined sources8
    Turni59 – 62Combined sources4
    Beta strandi63 – 74Combined sources12
    Helixi77 – 80Combined sources4
    Beta strandi82 – 91Combined sources10
    Helixi93 – 95Combined sources3
    Helixi100 – 114Combined sources15
    Beta strandi118 – 121Combined sources4
    Helixi126 – 128Combined sources3
    Helixi129 – 133Combined sources5
    Turni134 – 136Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3T90X-ray1.50A1-149[»]
    ProteinModelPortaliQ9LFU9.
    SMRiQ9LFU9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini5 – 149N-acetyltransferasePROSITE-ProRule annotationAdd BLAST145

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni75 – 78Substrate bindingBy similarity4
    Regioni87 – 89Substrate bindingBy similarity3
    Regioni97 – 102Acetyl-CoA bindingBy similarity6
    Regioni118 – 119Substrate bindingBy similarity2
    Regioni132 – 134Acetyl-CoA bindingBy similarity3

    Sequence similaritiesi

    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiKOG3396. Eukaryota.
    COG0454. LUCA.
    HOGENOMiHOG000106325.
    InParanoidiQ9LFU9.
    KOiK00621.
    OMAiAEKIGCY.
    OrthoDBiEOG09360S2X.
    PhylomeDBiQ9LFU9.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view]
    PfamiPF00583. Acetyltransf_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9LFU9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAETFKIRKL EISDKRKGFI ELLGQLTVTG SVTDEEFDRR FEEIRSYGDD
    60 70 80 90 100
    HVICVIEEET SGKIAATGSV MIEKKFLRNC GKAGHIEDVV VDSRFRGKQL
    110 120 130 140
    GKKVVEFLMD HCKSMGCYKV ILDCSVENKV FYEKCGMSNK SIQMSKYFD
    Length:149
    Mass (Da):17,028
    Last modified:October 1, 2000 - v1
    Checksum:i209AF6CB83DCC857
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL391144 Genomic DNA. Translation: CAC01776.1.
    CP002688 Genomic DNA. Translation: AED92203.1.
    PIRiT51406.
    RefSeqiNP_197081.1. NM_121582.2.
    UniGeneiAt.31755.

    Genome annotation databases

    EnsemblPlantsiAT5G15770.1; AT5G15770.1; AT5G15770.
    GeneIDi831433.
    GrameneiAT5G15770.1; AT5G15770.1; AT5G15770.
    KEGGiath:AT5G15770.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL391144 Genomic DNA. Translation: CAC01776.1.
    CP002688 Genomic DNA. Translation: AED92203.1.
    PIRiT51406.
    RefSeqiNP_197081.1. NM_121582.2.
    UniGeneiAt.31755.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3T90X-ray1.50A1-149[»]
    ProteinModelPortaliQ9LFU9.
    SMRiQ9LFU9.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT5G15770.1.

    Proteomic databases

    PaxDbiQ9LFU9.

    Protocols and materials databases

    DNASUi831433.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G15770.1; AT5G15770.1; AT5G15770.
    GeneIDi831433.
    GrameneiAT5G15770.1; AT5G15770.1; AT5G15770.
    KEGGiath:AT5G15770.

    Organism-specific databases

    TAIRiAT5G15770.

    Phylogenomic databases

    eggNOGiKOG3396. Eukaryota.
    COG0454. LUCA.
    HOGENOMiHOG000106325.
    InParanoidiQ9LFU9.
    KOiK00621.
    OMAiAEKIGCY.
    OrthoDBiEOG09360S2X.
    PhylomeDBiQ9LFU9.

    Enzyme and pathway databases

    UniPathwayiUPA00113; UER00529.
    BRENDAi2.3.1.4. 399.
    ReactomeiR-ATH-446210. Synthesis of UDP-N-acetyl-glucosamine.

    Miscellaneous databases

    PROiQ9LFU9.

    Gene expression databases

    GenevisibleiQ9LFU9. AT.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000182. GNAT_dom.
    [Graphical view]
    PfamiPF00583. Acetyltransf_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGNA1_ARATH
    AccessioniPrimary (citable) accession number: Q9LFU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 6, 2013
    Last sequence update: October 1, 2000
    Last modified: November 30, 2016
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The mutant lignescens (lig) was originally isolated as a temperature-sensitive mutant that exhibits ectopic lignin deposition and growth defects under high-temperature conditions.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.