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Q5FAK7

- Q5FAK7_NEIG1

UniProt

Q5FAK7 - Q5FAK7_NEIG1

Protein

Amino-acid acetyltransferase

Gene

argA

Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      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 sitei134 – 1341CoenzymeA 1Imported
    Binding sitei152 – 1521CoenzymeA 2Imported
    Binding sitei357 – 3571CoenzymeA 3; via carbonyl oxygenImported
    Binding sitei394 – 3941CoenzymeA 3; via carbonyl oxygenImported
    Binding sitei398 – 3981CoenzymeA 3Imported

    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

    BioCyciNGON242231:GI2G-24-MONOMER.
    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
    Ordered Locus Names:NGO0027Imported
    OrganismiNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090)Imported
    Taxonomic identifieri242231 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
    ProteomesiUP000000535: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi242231.NGO0027.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2R8VX-ray2.50A1-436[»]
    2R98X-ray2.40A1-436[»]
    3B8GX-ray2.60A1-436[»]
    3D2MX-ray2.21A1-436[»]
    3D2PX-ray2.56A/B1-436[»]
    ProteinModelPortaliQ5FAK7.
    SMRiQ5FAK7. Positions 5-436.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5FAK7.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni151 – 1522CoenzymeA 1 bindingImported
    Regioni357 – 3593CoenzymeA 1 bindingImported
    Regioni357 – 3593CoenzymeA 2 bindingImported
    Regioni364 – 3707CoenzymeA 1 bindingImported
    Regioni364 – 3707CoenzymeA 3 bindingImported
    Regioni365 – 3706CoenzymeA 2 bindingImported
    Regioni392 – 3987CoenzymeA 1 bindingImported
    Regioni394 – 3985CoenzymeA 2 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

    Phylogenomic databases

    eggNOGiCOG0548.
    HOGENOMiHOG000262225.
    KOiK14682.
    OMAiDARKRKY.
    OrthoDBiEOG6T1WVF.

    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.

    Q5FAK7-1 [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 GVLLHRSREY LENHISEFSI LEHDGDLYGC AALKTFAEAD 350
    CGEIACLAVS PQAQDGGYGE RLLAHIIDKA RGIGISRLFA LSTNTGEWFA 400
    ERGFQTASED ELPETRRKDY RSNGRNPHIL VRRLHR 436
    Length:436
    Mass (Da):47,003
    Last modified:March 15, 2005 - v1
    Checksum:i6019B9B2B4FC8A0C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004969 Genomic DNA. Translation: AAW88796.1.
    RefSeqiYP_207208.1. NC_002946.2.

    Genome annotation databases

    EnsemblBacteriaiAAW88796; AAW88796; NGO0027.
    GeneIDi3283070.
    KEGGingo:NGO0027.
    PATRICi20332884. VBINeiGon24812_0027.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004969 Genomic DNA. Translation: AAW88796.1 .
    RefSeqi YP_207208.1. NC_002946.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2R8V X-ray 2.50 A 1-436 [» ]
    2R98 X-ray 2.40 A 1-436 [» ]
    3B8G X-ray 2.60 A 1-436 [» ]
    3D2M X-ray 2.21 A 1-436 [» ]
    3D2P X-ray 2.56 A/B 1-436 [» ]
    ProteinModelPortali Q5FAK7.
    SMRi Q5FAK7. Positions 5-436.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 242231.NGO0027.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAW88796 ; AAW88796 ; NGO0027 .
    GeneIDi 3283070.
    KEGGi ngo:NGO0027.
    PATRICi 20332884. VBINeiGon24812_0027.

    Phylogenomic databases

    eggNOGi COG0548.
    HOGENOMi HOG000262225.
    KOi K14682.
    OMAi DARKRKY.
    OrthoDBi EOG6T1WVF.

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00106 .
    BioCyci NGON242231:GI2G-24-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q5FAK7.

    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. "The complete genome sequence of Neisseria gonorrhoeae."
      Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H.
      , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700825 / FA 1090Imported.
    2. "The crystal structure of N-acetyl-L-glutamate synthase from Neisseria gonorrhoeae provides insights into mechanisms of catalysis and regulation."
      Shi D., Sagar V., Jin Z., Yu X., Caldovic L., Morizono H., Allewell N.M., Tuchman M.
      J. Biol. Chem. 283:7176-7184(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH COENZYMEA.
    3. "Mechanism of allosteric inhibition of N-acetyl-L-glutamate synthase by L-arginine."
      Min L., Jin Z., Caldovic L., Morizono H., Allewell N.M., Tuchman M., Shi D.
      J. Biol. Chem. 284:4873-4880(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) IN COMPLEX WITH COENZYMEA.

    Entry informationi

    Entry nameiQ5FAK7_NEIG1
    AccessioniPrimary (citable) accession number: Q5FAK7
    Entry historyi
    Integrated into UniProtKB/TrEMBL: March 15, 2005
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 70 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, Complete proteome, Reference proteomeImported

    External Data

    Dasty 3