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D2BPS8

- D2BPS8_LACLK

UniProt

D2BPS8 - D2BPS8_LACLK

Protein

Arginine biosynthesis bifunctional protein ArgJ

Gene

argJ

Organism
Lactococcus lactis subsp. lactis (strain KF147)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (09 Feb 2010)
      Previous versions | rss
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    Functioni

    Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.UniRule annotation

    Catalytic activityi

    Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.UniRule annotation
    N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei112 – 1121Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion holeUniRule annotation
    Sitei113 – 1131Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion holeUniRule annotation
    Binding sitei147 – 1471SubstrateUniRule annotation
    Binding sitei173 – 1731SubstrateUniRule annotation
    Sitei183 – 1842Cleavage; by autolysisUniRule annotation
    Active sitei184 – 1841NucleophileUniRule annotation
    Binding sitei184 – 1841SubstrateUniRule annotation
    Binding sitei270 – 2701SubstrateUniRule annotation
    Binding sitei391 – 3911SubstrateUniRule annotation
    Binding sitei396 – 3961SubstrateUniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. arginine biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    AcyltransferaseUniRule annotationImported, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Arginine biosynthesisUniRule annotation

    Enzyme and pathway databases

    BioCyciLLAC684738:GI3F-858-MONOMER.
    UniPathwayiUPA00068; UER00106.
    UPA00068; UER00111.

    Protein family/group databases

    MEROPSiT05.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine biosynthesis bifunctional protein ArgJUniRule annotation
    Gene namesi
    Name:argJUniRule annotationImported
    Ordered Locus Names:LLKF_0818Imported
    OrganismiLactococcus lactis subsp. lactis (strain KF147)Imported
    Taxonomic identifieri684738 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
    ProteomesiUP000001886: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    CytoplasmUniRule annotation

    PTM / Processingi

    Keywords - PTMi

    Autocatalytic cleavageUniRule annotation

    Interactioni

    Subunit structurei

    Heterotetramer of two alpha and two beta chains.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliD2BPS8.
    SMRiD2BPS8. Positions 184-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ArgJ family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000022797.
    KOiK00620.
    OMAiVTVHIAG.
    OrthoDBiEOG6P8TQQ.

    Family and domain databases

    Gene3Di3.60.70.12. 1 hit.
    HAMAPiMF_01106. ArgJ.
    InterProiIPR002813. Arg_biosynth_ArgJ.
    IPR016117. ArgJ-like_dom.
    [Graphical view]
    PANTHERiPTHR23100. PTHR23100. 1 hit.
    PfamiPF01960. ArgJ. 1 hit.
    [Graphical view]
    SUPFAMiSSF56266. SSF56266. 1 hit.
    TIGRFAMsiTIGR00120. ArgJ. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    D2BPS8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKEIKGTIAS PKGFLADAVH AQLKYKNLDL GLILSQVPAA IAGVFTTNKV    50
    CAAPVLIDRQ IVKNGQARAI ICNSAVANAV TGEQGYANAL KTQKLLAEKF 100
    ELKAEEVAVC STGVIGVQLP MEKIATGISK LSQNEGTAAY FAKAILTTDT 150
    QTKTINFEAE IGGQIVNMAG VCKGSGMIHP NMATMLAFIT TDAKIAQALL 200
    QKTLSEIIET TFNQITVDGD TSTNDTVLLM ANGQAKNNEI LEGSSDYLLF 250
    KEMLAKVCQS LAKQIAADGE GATKLIEVTV KGAPNDLAAR FIAKKIVGSS 300
    LVKTAIFGAD PNWGRIISSI GQVANFEVSD IELKLQDELV LYHSTPVDFD 350
    AAFLSEKLKE DKIEIIADLN AGSGLGQAWG CDLTYKYVEI NALYTS 396
    Length:396
    Mass (Da):42,130
    Last modified:February 9, 2010 - v1
    Checksum:i51534E125DABCBF7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001834 Genomic DNA. Translation: ADA64553.1.
    RefSeqiYP_003353274.1. NC_013656.1.

    Genome annotation databases

    EnsemblBacteriaiADA64553; ADA64553; LLKF_0818.
    GeneIDi8678239.
    KEGGillk:LLKF_0818.
    PATRICi32250113. VBILacLac141273_0830.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001834 Genomic DNA. Translation: ADA64553.1 .
    RefSeqi YP_003353274.1. NC_013656.1.

    3D structure databases

    ProteinModelPortali D2BPS8.
    SMRi D2BPS8. Positions 184-394.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi T05.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADA64553 ; ADA64553 ; LLKF_0818 .
    GeneIDi 8678239.
    KEGGi llk:LLKF_0818.
    PATRICi 32250113. VBILacLac141273_0830.

    Phylogenomic databases

    HOGENOMi HOG000022797.
    KOi K00620.
    OMAi VTVHIAG.
    OrthoDBi EOG6P8TQQ.

    Enzyme and pathway databases

    UniPathwayi UPA00068 ; UER00106 .
    UPA00068 ; UER00111 .
    BioCyci LLAC684738:GI3F-858-MONOMER.

    Family and domain databases

    Gene3Di 3.60.70.12. 1 hit.
    HAMAPi MF_01106. ArgJ.
    InterProi IPR002813. Arg_biosynth_ArgJ.
    IPR016117. ArgJ-like_dom.
    [Graphical view ]
    PANTHERi PTHR23100. PTHR23100. 1 hit.
    Pfami PF01960. ArgJ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56266. SSF56266. 1 hit.
    TIGRFAMsi TIGR00120. ArgJ. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome-scale genotype-phenotype matching of two Lactococcus lactis isolates from plants identifies mechanisms of adaptation to the plant niche."
      Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D., van Hylckama Vlieg J.E.
      Appl. Environ. Microbiol. 74:424-436(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: KF147Imported.

    Entry informationi

    Entry nameiD2BPS8_LACLK
    AccessioniPrimary (citable) accession number: D2BPS8
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 9, 2010
    Last sequence update: February 9, 2010
    Last modified: October 1, 2014
    This is version 37 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Miscellaneous

    Some bacteria possess a monofunctional ArgJ, i.e., capable of catalyzing only the fifth step of the arginine biosynthetic pathway.UniRule annotation

    Keywords - Technical termi

    Complete proteomeImported, Multifunctional enzymeUniRule annotation

    External Data

    Dasty 3