Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetylornithine/succinyldiaminopimelate aminotransferase

Gene

argD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in both the arginine and lysine biosynthetic pathways.UniRule annotation1 Publication

Miscellaneous

The reaction catalyzed by ACOAT is highly reversible. This enzyme may also transaminate ornithine.

Catalytic activityi

N2-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.UniRule annotation1 Publication
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-2-L-amino-6-oxoheptanedioate + L-glutamate.UniRule annotation1 Publication

Cofactori

pyridoxal 5'-phosphateUniRule annotation1 PublicationNote: Binds 1 pyridoxal phosphate per subunit.UniRule annotation1 Publication

Kineticsi

  1. KM=0.15 mM for N-acetylornithine1 Publication
  2. KM=0.075 mM for N-succinyldiaminopimelate1 Publication

    Pathwayi: L-arginine biosynthesis

    This protein is involved in step 4 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.UniRule annotation1 Publication
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Amino-acid acetyltransferase (argA)
    2. Acetylglutamate kinase (argB)
    3. N-acetyl-gamma-glutamyl-phosphate reductase (argC)
    4. Acetylornithine/succinyldiaminopimelate aminotransferase (argD)
    This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

    Pathwayi: L-lysine biosynthesis via DAP pathway

    This protein is involved in step 2 of the subpathway that synthesizes LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route).UniRule annotation1 Publication
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (dapD)
    2. Acetylornithine/succinyldiaminopimelate aminotransferase (argD)
    3. Succinyl-diaminopimelate desuccinylase (dapE)
    This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route), the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei141Pyridoxal phosphate; via carbonyl oxygenUniRule annotationBy similarity1
    Binding sitei144N2-acetyl-L-ornithineUniRule annotationBy similarity1
    Binding sitei283N2-acetyl-L-ornithineUniRule annotationBy similarity1
    Binding sitei284Pyridoxal phosphateUniRule annotationBy similarity1

    GO - Molecular functioni

    GO - Biological processi

    • arginine biosynthetic process via ornithine Source: EcoCyc
    • lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate Source: EcoCyc

    Keywordsi

    Molecular functionAminotransferase, Transferase
    Biological processAmino-acid biosynthesis, Arginine biosynthesis, Lysine biosynthesis
    LigandPyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:ACETYLORNTRANSAM-MONOMER.
    MetaCyc:ACETYLORNTRANSAM-MONOMER.
    UniPathwayiUPA00034; UER00020.
    UPA00068; UER00109.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetylornithine/succinyldiaminopimelate aminotransferaseUniRule annotationCurated (EC:2.6.1.11UniRule annotation1 Publication, EC:2.6.1.17UniRule annotation1 Publication)
    Short name:
    ACOAT1 PublicationUniRule annotation
    Short name:
    DapATase1 PublicationUniRule annotation
    Short name:
    Succinyldiaminopimelate transferaseUniRule annotation
    Gene namesi
    Name:argDUniRule annotation
    Synonyms:dapCUniRule annotation, dtu
    Ordered Locus Names:b3359, JW3322
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10066. argD.

    Subcellular locationi

    • Cytoplasm UniRule annotationCurated

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved2 Publications
    ChainiPRO_00001127432 – 406Acetylornithine/succinyldiaminopimelate aminotransferaseAdd BLAST405

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei255N6-(pyridoxal phosphate)lysineUniRule annotationBy similarity1

    Proteomic databases

    EPDiP18335.
    PaxDbiP18335.
    PRIDEiP18335.

    2D gel databases

    SWISS-2DPAGEiP18335.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    GO - Molecular functioni

    Protein-protein interaction databases

    BioGridi4260742. 7 interactors.
    DIPiDIP-9138N.
    IntActiP18335. 6 interactors.
    STRINGi511145.b3359.

    Structurei

    3D structure databases

    ProteinModelPortaliP18335.
    SMRiP18335.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni108 – 109Pyridoxal phosphate bindingUniRule annotationBy similarity2
    Regioni226 – 229Pyridoxal phosphate bindingUniRule annotationBy similarity4

    Sequence similaritiesi

    Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiENOG4105C8Y. Bacteria.
    COG4992. LUCA.
    HOGENOMiHOG000020206.
    InParanoidiP18335.
    KOiK00821.
    PhylomeDBiP18335.

    Family and domain databases

    CDDicd00610. OAT_like. 1 hit.
    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    HAMAPiMF_01107. ArgD_aminotrans_3. 1 hit.
    InterProiView protein in InterPro
    IPR017652. Ac/SucOrn_transaminase_bac.
    IPR004636. AcOrn/SuccOrn_fam.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_sub2.
    PANTHERiPTHR11986:SF101. PTHR11986:SF101. 1 hit.
    PfamiView protein in Pfam
    PF00202. Aminotran_3. 1 hit.
    PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR03246. arg_catab_astC. 1 hit.
    TIGR00707. argD. 1 hit.
    PROSITEiView protein in PROSITE
    PS00600. AA_TRANSFER_CLASS_3. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P18335-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAIEQTAITR ATFDEVILPI YAPAEFIPVK GQGSRIWDQQ GKEYVDFAGG
    60 70 80 90 100
    IAVTALGHCH PALVNALKTQ GETLWHISNV FTNEPALRLG RKLIEATFAE
    110 120 130 140 150
    RVVFMNSGTE ANETAFKLAR HYACVRHSPF KTKIIAFHNA FHGRSLFTVS
    160 170 180 190 200
    VGGQPKYSDG FGPKPADIIH VPFNDLHAVK AVMDDHTCAV VVEPIQGEGG
    210 220 230 240 250
    VTAATPEFLQ GLRELCDQHQ ALLVFDEVQC GMGRTGDLFA YMHYGVTPDI
    260 270 280 290 300
    LTSAKALGGG FPISAMLTTA EIASAFHPGS HGSTYGGNPL ACAVAGAAFD
    310 320 330 340 350
    IINTPEVLEG IQAKRQRFVD HLQKIDQQYD VFSDIRGMGL LIGAELKPQY
    360 370 380 390 400
    KGRARDFLYA GAEAGVMVLN AGPDVMRFAP SLVVEDADID EGMQRFAHAV

    AKVVGA
    Length:406
    Mass (Da):43,767
    Last modified:January 23, 2007 - v4
    Checksum:i645AA1EBCA442214
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti245 – 247GVT → ALA in AAA23480 (PubMed:2199330).Curated3

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M32796 Genomic DNA. Translation: AAA23480.1.
    U18997 Genomic DNA. Translation: AAA58156.1.
    U00096 Genomic DNA. Translation: AAC76384.1.
    AP009048 Genomic DNA. Translation: BAE77931.1.
    PIRiB65130.
    RefSeqiNP_417818.1. NC_000913.3.
    WP_000963792.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76384; AAC76384; b3359.
    BAE77931; BAE77931; BAE77931.
    GeneIDi947864.
    KEGGiecj:JW3322.
    eco:b3359.
    PATRICifig|1411691.4.peg.3371.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M32796 Genomic DNA. Translation: AAA23480.1.
    U18997 Genomic DNA. Translation: AAA58156.1.
    U00096 Genomic DNA. Translation: AAC76384.1.
    AP009048 Genomic DNA. Translation: BAE77931.1.
    PIRiB65130.
    RefSeqiNP_417818.1. NC_000913.3.
    WP_000963792.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP18335.
    SMRiP18335.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260742. 7 interactors.
    DIPiDIP-9138N.
    IntActiP18335. 6 interactors.
    STRINGi511145.b3359.

    2D gel databases

    SWISS-2DPAGEiP18335.

    Proteomic databases

    EPDiP18335.
    PaxDbiP18335.
    PRIDEiP18335.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76384; AAC76384; b3359.
    BAE77931; BAE77931; BAE77931.
    GeneIDi947864.
    KEGGiecj:JW3322.
    eco:b3359.
    PATRICifig|1411691.4.peg.3371.

    Organism-specific databases

    EchoBASEiEB0064.
    EcoGeneiEG10066. argD.

    Phylogenomic databases

    eggNOGiENOG4105C8Y. Bacteria.
    COG4992. LUCA.
    HOGENOMiHOG000020206.
    InParanoidiP18335.
    KOiK00821.
    PhylomeDBiP18335.

    Enzyme and pathway databases

    UniPathwayiUPA00034; UER00020.
    UPA00068; UER00109.
    BioCyciEcoCyc:ACETYLORNTRANSAM-MONOMER.
    MetaCyc:ACETYLORNTRANSAM-MONOMER.

    Miscellaneous databases

    PROiPR:P18335.

    Family and domain databases

    CDDicd00610. OAT_like. 1 hit.
    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    HAMAPiMF_01107. ArgD_aminotrans_3. 1 hit.
    InterProiView protein in InterPro
    IPR017652. Ac/SucOrn_transaminase_bac.
    IPR004636. AcOrn/SuccOrn_fam.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_sub2.
    PANTHERiPTHR11986:SF101. PTHR11986:SF101. 1 hit.
    PfamiView protein in Pfam
    PF00202. Aminotran_3. 1 hit.
    PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR03246. arg_catab_astC. 1 hit.
    TIGR00707. argD. 1 hit.
    PROSITEiView protein in PROSITE
    PS00600. AA_TRANSFER_CLASS_3. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiARGD_ECOLI
    AccessioniPrimary (citable) accession number: P18335
    Secondary accession number(s): Q2M725
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: June 7, 2017
    This is version 153 of the entry and version 4 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. 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.