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Protein

Glucosamine 6-phosphate N-acetyltransferase

Gene

GNPNAT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate.2 Publications

Kineticsi

  1. KM=26 µM for acetyl-coenzyme A1 Publication
  2. KM=97 µM for glucosamine-6-phosphate1 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 (GNPNAT1)
    2. Phosphoacetylglucosamine mutase (PGM3)
    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 sitei61 – 611SubstrateCombined sources1 Publication1 Publication
    Binding sitei175 – 1751SubstrateCombined sources1 Publication1 Publication
    Binding sitei181 – 1811SubstrateCombined sources1 Publication1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.3.1.4. 2681.
    ReactomeiR-HSA-446210. Synthesis of UDP-N-acetyl-glucosamine.
    SABIO-RKQ96EK6.
    UniPathwayiUPA00113; UER00529.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucosamine 6-phosphate N-acetyltransferase (EC:2.3.1.42 Publications)
    Alternative name(s):
    Phosphoglucosamine acetylase
    Phosphoglucosamine transacetylase
    Gene namesi
    Name:GNPNAT1
    Synonyms:GNA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:19980. GNPNAT1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi156 – 1561E → A: Reduces affinity for glucosamine-6-phosphate 6-fold. 1 Publication
    Mutagenesisi156 – 1561E → D: Slightly reduced catalytic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134901326.

    Polymorphism and mutation databases

    BioMutaiGNPNAT1.
    DMDMi47116568.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 184184Glucosamine 6-phosphate N-acetyltransferasePRO_0000074553Add
    BLAST

    Proteomic databases

    EPDiQ96EK6.
    MaxQBiQ96EK6.
    PaxDbiQ96EK6.
    PeptideAtlasiQ96EK6.
    PRIDEiQ96EK6.

    PTM databases

    iPTMnetiQ96EK6.
    PhosphoSiteiQ96EK6.

    Expressioni

    Gene expression databases

    BgeeiQ96EK6.
    CleanExiHS_GNPNAT1.
    ExpressionAtlasiQ96EK6. baseline and differential.
    GenevisibleiQ96EK6. HS.

    Organism-specific databases

    HPAiHPA044647.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-3913338,EBI-3913338

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    BioGridi122317. 18 interactions.
    IntActiQ96EK6. 2 interactions.
    MINTiMINT-2813920.
    STRINGi9606.ENSP00000216410.

    Structurei

    Secondary structure

    1
    184
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 93Combined sources
    Helixi12 – 165Combined sources
    Helixi19 – 213Combined sources
    Beta strandi32 – 343Combined sources
    Beta strandi39 – 435Combined sources
    Helixi46 – 505Combined sources
    Helixi53 – 575Combined sources
    Turni58 – 603Combined sources
    Helixi68 – 8114Combined sources
    Beta strandi84 – 918Combined sources
    Turni92 – 954Combined sources
    Beta strandi96 – 10712Combined sources
    Helixi110 – 1134Combined sources
    Beta strandi115 – 12410Combined sources
    Helixi126 – 1283Combined sources
    Helixi133 – 14715Combined sources
    Beta strandi150 – 1578Combined sources
    Helixi159 – 1613Combined sources
    Helixi162 – 1665Combined sources
    Turni167 – 1693Combined sources
    Beta strandi174 – 1829Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HUZX-ray2.67A/B1-184[»]
    2O28X-ray1.80A/B1-184[»]
    3CXPX-ray2.01A1-184[»]
    3CXQX-ray2.30A1-184[»]
    3CXSX-ray2.70A1-184[»]
    ProteinModelPortaliQ96EK6.
    SMRiQ96EK6. Positions 3-184.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96EK6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 184146N-acetyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni108 – 1114Substrate bindingCombined sources1 Publication1 Publication
    Regioni120 – 1223Substrate bindingCombined sources1 Publication1 Publication
    Regioni130 – 1356Acetyl-CoA bindingCombined sources1 Publication
    Regioni151 – 1522Substrate bindingCombined sources1 Publication1 Publication
    Regioni165 – 1673Acetyl-CoA bindingCombined sources1 Publication

    Sequence similaritiesi

    Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiKOG3396. Eukaryota.
    COG0454. LUCA.
    GeneTreeiENSGT00390000008666.
    HOGENOMiHOG000106325.
    HOVERGENiHBG048986.
    InParanoidiQ96EK6.
    KOiK00621.
    OMAiKFIHNCA.
    OrthoDBiEOG77T165.
    PhylomeDBiQ96EK6.
    TreeFamiTF313790.

    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.

    Q96EK6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKPDETPMFD PSLLKEVDWS QNTATFSPAI SPTHPGEGLV LRPLCTADLN
    60 70 80 90 100
    RGFFKVLGQL TETGVVSPEQ FMKSFEHMKK SGDYYVTVVE DVTLGQIVAT
    110 120 130 140 150
    ATLIIEHKFI HSCAKRGRVE DVVVSDECRG KQLGKLLLST LTLLSKKLNC
    160 170 180
    YKITLECLPQ NVGFYKKFGY TVSEENYMCR RFLK
    Length:184
    Mass (Da):20,749
    Last modified:December 1, 2001 - v1
    Checksum:iE9F31803CF633BBF
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK090577 mRNA. Translation: BAC03482.1.
    BC012179 mRNA. Translation: AAH12179.1.
    CCDSiCCDS9712.1.
    RefSeqiNP_932332.1. NM_198066.3.
    XP_005268069.1. XM_005268012.1.
    XP_006720301.1. XM_006720238.2.
    UniGeneiHs.478025.

    Genome annotation databases

    EnsembliENST00000216410; ENSP00000216410; ENSG00000100522.
    GeneIDi64841.
    KEGGihsa:64841.
    UCSCiuc001xab.4. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK090577 mRNA. Translation: BAC03482.1.
    BC012179 mRNA. Translation: AAH12179.1.
    CCDSiCCDS9712.1.
    RefSeqiNP_932332.1. NM_198066.3.
    XP_005268069.1. XM_005268012.1.
    XP_006720301.1. XM_006720238.2.
    UniGeneiHs.478025.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HUZX-ray2.67A/B1-184[»]
    2O28X-ray1.80A/B1-184[»]
    3CXPX-ray2.01A1-184[»]
    3CXQX-ray2.30A1-184[»]
    3CXSX-ray2.70A1-184[»]
    ProteinModelPortaliQ96EK6.
    SMRiQ96EK6. Positions 3-184.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi122317. 18 interactions.
    IntActiQ96EK6. 2 interactions.
    MINTiMINT-2813920.
    STRINGi9606.ENSP00000216410.

    PTM databases

    iPTMnetiQ96EK6.
    PhosphoSiteiQ96EK6.

    Polymorphism and mutation databases

    BioMutaiGNPNAT1.
    DMDMi47116568.

    Proteomic databases

    EPDiQ96EK6.
    MaxQBiQ96EK6.
    PaxDbiQ96EK6.
    PeptideAtlasiQ96EK6.
    PRIDEiQ96EK6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000216410; ENSP00000216410; ENSG00000100522.
    GeneIDi64841.
    KEGGihsa:64841.
    UCSCiuc001xab.4. human.

    Organism-specific databases

    CTDi64841.
    GeneCardsiGNPNAT1.
    HGNCiHGNC:19980. GNPNAT1.
    HPAiHPA044647.
    MIMi616510. gene.
    neXtProtiNX_Q96EK6.
    PharmGKBiPA134901326.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3396. Eukaryota.
    COG0454. LUCA.
    GeneTreeiENSGT00390000008666.
    HOGENOMiHOG000106325.
    HOVERGENiHBG048986.
    InParanoidiQ96EK6.
    KOiK00621.
    OMAiKFIHNCA.
    OrthoDBiEOG77T165.
    PhylomeDBiQ96EK6.
    TreeFamiTF313790.

    Enzyme and pathway databases

    UniPathwayiUPA00113; UER00529.
    BRENDAi2.3.1.4. 2681.
    ReactomeiR-HSA-446210. Synthesis of UDP-N-acetyl-glucosamine.
    SABIO-RKQ96EK6.

    Miscellaneous databases

    ChiTaRSiGNPNAT1. human.
    EvolutionaryTraceiQ96EK6.
    GenomeRNAii64841.
    PROiQ96EK6.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ96EK6.
    CleanExiHS_GNPNAT1.
    ExpressionAtlasiQ96EK6. baseline and differential.
    GenevisibleiQ96EK6. HS.

    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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon.
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1."
      Wang J., Liu X., Liang Y.-H., Li L.-F., Su X.-D.
      FEBS Lett. 582:2973-2978(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH THE SUBSTRATE GLUCOSAMINE-6-PHOSPHATE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-156, SUBUNIT.
    6. "Structural and kinetic differences between human and Aspergillus fumigatus D-glucosamine-6-phosphate N-acetyltransferase."
      Hurtado-Guerrero R., Raimi O.G., Min J., Zeng H., Vallius L., Shepherd S., Ibrahim A.F.M., Wu H., Plotnikov A.N., van Aalten D.M.F.
      Biochem. J. 415:217-223(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH THE ACETYL-COA ANALOG COENZYME A AND THE SUBSTRATE N-ACETYLGLUCOSAMINE-6-PHOSPHATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiGNA1_HUMAN
    AccessioniPrimary (citable) accession number: Q96EK6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: December 1, 2001
    Last modified: June 8, 2016
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. 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.