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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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei27 – 271SubstrateBy similarity

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi68 – 681G → S in lig; reduces activity 2-fold. Retarded growth. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 149149Glucosamine 6-phosphate N-acetyltransferasePRO_0000421037Add
    BLAST

    Proteomic databases

    PaxDbiQ9LFU9.
    PRIDEiQ9LFU9.

    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

    1
    149
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95Combined sources
    Helixi12 – 165Combined sources
    Helixi19 – 235Combined sources
    Turni24 – 263Combined sources
    Helixi34 – 4512Combined sources
    Helixi46 – 505Combined sources
    Beta strandi51 – 588Combined sources
    Turni59 – 624Combined sources
    Beta strandi63 – 7412Combined sources
    Helixi77 – 804Combined sources
    Beta strandi82 – 9110Combined sources
    Helixi93 – 953Combined sources
    Helixi100 – 11415Combined sources
    Beta strandi118 – 1214Combined sources
    Helixi126 – 1283Combined sources
    Helixi129 – 1335Combined sources
    Turni134 – 1363Combined sources

    3D structure databases

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 149145N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni75 – 784Substrate bindingBy similarity
    Regioni87 – 893Substrate bindingBy similarity
    Regioni97 – 1026Acetyl-CoA bindingBy similarity
    Regioni118 – 1192Substrate bindingBy similarity
    Regioni132 – 1343Acetyl-CoA bindingBy similarity

    Sequence similaritiesi

    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiKOG3396. Eukaryota.
    COG0454. LUCA.
    HOGENOMiHOG000106325.
    InParanoidiQ9LFU9.
    KOiK00621.
    OMAiNEGFYIK.
    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_121582.1.
    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_121582.1.
    UniGeneiAt.31755.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi3702.AT5G15770.1.

    Proteomic databases

    PaxDbiQ9LFU9.
    PRIDEiQ9LFU9.

    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.
    OMAiNEGFYIK.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "A missense mutation in the glucosamine-6-phosphate N-acetyltransferase-encoding gene causes temperature-dependent growth defects and ectopic lignin deposition in Arabidopsis."
      Nozaki M., Sugiyama M., Duan J., Uematsu H., Genda T., Sato Y.
      Plant Cell 24:3366-3379(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-68.
      Strain: cv. Landsberg erecta.
    4. "Crystal structure and functional characterization of a glucosamine-6-phosphate N-acetyltransferase from Arabidopsis thaliana."
      Riegler H., Herter T., Grishkovskaya I., Lude A., Ryngajllo M., Bolger M.E., Essigmann B., Usadel B.
      Biochem. J. 443:427-437(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    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: February 17, 2016
    This is version 86 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.