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D1ED56

- D1ED56_NEIGO

UniProt

D1ED56 - D1ED56_NEIGO

Protein

Amino-acid acetyltransferase

Gene

argA

Organism
Neisseria gonorrhoeae SK-93-1035
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 25 (01 Oct 2014)
      Sequence version 1 (19 Jan 2010)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.UniRule annotationSAAS annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei46 – 461SulfateImported

    GO - Molecular functioni

    1. acetyl-CoA:L-glutamate N-acetyltransferase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. arginine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    AcyltransferaseUniRule annotationSAAS annotation, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesisUniRule annotationSAAS annotation

    Enzyme and pathway databases

    UniPathwayiUPA00068; UER00106.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Amino-acid acetyltransferaseUniRule annotation (EC:2.3.1.-UniRule annotation, EC:2.3.1.1UniRule annotation)
    Alternative name(s):
    N-acetylglutamate synthaseUniRule annotation
    Gene namesi
    Name:argAUniRule annotation
    ORF Names:NGLG_00316Imported
    OrganismiNeisseria gonorrhoeae SK-93-1035Imported
    Taxonomic identifieri528360 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotation

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4I49X-ray2.75A1-436[»]
    ProteinModelPortaliD1ED56.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini287 – 436150N-acetyltransferaseUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni265 – 2673Sulfate bindingImported

    Sequence similaritiesi

    Belongs to the acetyltransferase family. ArgA subfamily.UniRule annotation
    Contains 1 N-acetyltransferase domain.UniRule annotation
    Contains N-acetyltransferase domain.SAAS annotation

    Family and domain databases

    Gene3Di3.40.1160.10. 1 hit.
    3.40.630.30. 1 hit.
    HAMAPiMF_01105. N_acetyl_glu_synth.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR000182. GNAT_dom.
    IPR010167. NH2A_AcTrfase_ArgA.
    [Graphical view]
    PfamiPF00696. AA_kinase. 1 hit.
    PF00583. Acetyltransf_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000423. ArgA. 1 hit.
    SUPFAMiSSF53633. SSF53633. 1 hit.
    SSF55729. SSF55729. 1 hit.
    TIGRFAMsiTIGR01890. N-Ac-Glu-synth. 1 hit.
    PROSITEiPS51186. GNAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    D1ED56-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNAPDSFVAH FREAAPYIRQ MRGTTLVAGI DGRLLEGGTL NKLAADIGLL    50
    SQLGIRLVLI HGAYHFLDRL AAAQGRTPHY CRGLRVTDET SLGQAQQFAG 100
    TVRSRFEAAL CGSVSGFARA PSVPLVSGNF LTARPIGVID GTDMEYAGVI 150
    RKTDTAALRF QLDAGNIVWM PPLGHSYGGK TFNLDMVQAA ASVAVSLQAE 200
    KLVYLTLSDG ISRPDGTLAE TLSAQEAQSL AEHAASETRR LISSAVAALE 250
    GGVHRVQILN GAADGSLLQE LFTRNGIGTS IAKEAFVSIR QAHSGDIPHI 300
    AALIRPLEEQ GILLHRSREY LENHISEFSI LEHDGNLYGC AALKTFAEAD 350
    CGEIACLAVS PQAQDGGYGE RLLAHIIDKA RGIGISRLFA LSTNTGEWFA 400
    ERGFQTASED ELPETRRKDY RSNGRNSHIL VRRLHR 436
    Length:436
    Mass (Da):47,006
    Last modified:January 19, 2010 - v1
    Checksum:iE29044A0B76C7B02
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EQ973086 Genomic DNA. Translation: EEZ58476.1.

    Genome annotation databases

    EnsemblBacteriaiEEZ58476; EEZ58476; NGLG_00316.
    PATRICi28195341. VBINeiGon43547_0285.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EQ973086 Genomic DNA. Translation: EEZ58476.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4I49 X-ray 2.75 A 1-436 [» ]
    ProteinModelPortali D1ED56.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai EEZ58476 ; EEZ58476 ; NGLG_00316 .
    PATRICi 28195341. VBINeiGon43547_0285.

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00106 .

    Family and domain databases

    Gene3Di 3.40.1160.10. 1 hit.
    3.40.630.30. 1 hit.
    HAMAPi MF_01105. N_acetyl_glu_synth.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR001048. Asp/Glu/Uridylate_kinase.
    IPR000182. GNAT_dom.
    IPR010167. NH2A_AcTrfase_ArgA.
    [Graphical view ]
    Pfami PF00696. AA_kinase. 1 hit.
    PF00583. Acetyltransf_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000423. ArgA. 1 hit.
    SUPFAMi SSF53633. SSF53633. 1 hit.
    SSF55729. SSF55729. 1 hit.
    TIGRFAMsi TIGR01890. N-Ac-Glu-synth. 1 hit.
    PROSITEi PS51186. GNAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE.
      Strain: SK-93-1035Imported.
    2. "Structure of the complex of Neisseria gonorrhoeae N-acetyl-L-glutamate synthase with a bound bisubstrate analog."
      Zhao G., Allewell N.M., Tuchman M., Shi D.
      Biochem. Biophys. Res. Commun. 430:1253-1258(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).

    Entry informationi

    Entry nameiD1ED56_NEIGO
    AccessioniPrimary (citable) accession number: D1ED56
    Entry historyi
    Integrated into UniProtKB/TrEMBL: January 19, 2010
    Last sequence update: January 19, 2010
    Last modified: October 1, 2014
    This is version 25 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Miscellaneous

    In bacteria which possess the bifunctional enzyme ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA fulfills an anaplerotic role.UniRule annotation

    Keywords - Technical termi

    3D-structureImported

    External Data

    Dasty 3