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Q1MR87

- DAPAT_LAWIP

UniProt

Q1MR87 - DAPAT_LAWIP

Protein

LL-diaminopimelate aminotransferase

Gene

dapL

Organism
Lawsonia intracellularis (strain PHE/MN1-00)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (30 May 2006)
      Previous versions | rss
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    Functioni

    Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate, a reaction that requires three enzymes in E.coli.UniRule annotation

    Catalytic activityi

    LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O.UniRule annotation

    Cofactori

    Pyridoxal phosphate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei42 – 421Substrate; via amide nitrogenUniRule annotation
    Binding sitei72 – 721Pyridoxal phosphate; shared with dimeric partnerUniRule annotation
    Binding sitei75 – 751Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei109 – 1091SubstrateUniRule annotation
    Binding sitei132 – 1321SubstrateUniRule annotation
    Binding sitei186 – 1861Pyridoxal phosphateUniRule annotation
    Binding sitei186 – 1861SubstrateUniRule annotation
    Binding sitei214 – 2141Pyridoxal phosphateUniRule annotation
    Binding sitei217 – 2171Pyridoxal phosphateUniRule annotation
    Binding sitei245 – 2451Pyridoxal phosphateUniRule annotation
    Binding sitei247 – 2471Pyridoxal phosphateUniRule annotation
    Binding sitei256 – 2561Pyridoxal phosphateUniRule annotation
    Binding sitei291 – 2911Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei387 – 3871SubstrateUniRule annotation

    GO - Molecular functioni

    1. L,L-diaminopimelate aminotransferase activity Source: UniProtKB-HAMAP
    2. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciLINT363253:GH6E-449-MONOMER.
    UniPathwayiUPA00034; UER00466.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LL-diaminopimelate aminotransferaseUniRule annotation (EC:2.6.1.83UniRule annotation)
    Short name:
    DAP-ATUniRule annotation
    Short name:
    DAP-aminotransferaseUniRule annotation
    Short name:
    LL-DAP-aminotransferaseUniRule annotation
    Gene namesi
    Name:dapLUniRule annotation
    Ordered Locus Names:LI0435
    OrganismiLawsonia intracellularis (strain PHE/MN1-00)
    Taxonomic identifieri363253 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeLawsonia
    ProteomesiUP000002430: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 410410LL-diaminopimelate aminotransferasePRO_0000342243Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei248 – 2481N6-(pyridoxal phosphate)lysineUniRule annotation

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi363253.LI0435.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1MR87.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0436.
    HOGENOMiHOG000223061.
    KOiK10206.
    OMAiKWVDYAN.
    OrthoDBiEOG6XWV2X.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_01642. DapL_aminotrans_1.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR019942. DapL_aminotrans.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11751:SF22. PTHR11751:SF22. 1 hit.
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR03542. DAPAT_plant. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q1MR87-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHTNKHYLD LPGSYFFTEI NQRVNTYKKT HPEKSIIRLS IGDVTRPLVP    50
    AVIKALHDAT DEMGQPSSFH GYGPEHGYEF LIGEIIANDY TSRNVHIEAD 100
    EIFVSDGTKC DIANIQELFD PSDTVAIIDP VYPVYIDSNV MSGRLGKLIN 150
    GIWSKLIYLP CTIENNFIPE LPTQHPDIIY LCYPNNPTGT VLSKDQLTIW 200
    VNYAKKEGAI ILFDAAYEAY ITDPTIPHSI YEIDGAKEVA IEFRSFSKTA 250
    GFTGLRCAYT VIPKELKANT REGNEQYLNM MWNRRQTTKY NGCSYIVQKA 300
    AAAIYTPEGQ KQIQESIQYY MKNALIIQNA ITQMGITAVG GINAPYVWIK 350
    TPDNLSSWDF FDLLLQNAGV VGTPGVGFGP HGEGYFRLTG FGSYEDTNKA 400
    IERIQKALLI 410
    Length:410
    Mass (Da):45,941
    Last modified:May 30, 2006 - v1
    Checksum:iC6E829F1020272F2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM180252 Genomic DNA. Translation: CAJ54489.1.
    RefSeqiYP_594811.1. NC_008011.1.

    Genome annotation databases

    GeneIDi4059387.
    KEGGilip:LI0435.
    PATRICi22304279. VBILawInt40445_0479.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM180252 Genomic DNA. Translation: CAJ54489.1 .
    RefSeqi YP_594811.1. NC_008011.1.

    3D structure databases

    ProteinModelPortali Q1MR87.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 363253.LI0435.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4059387.
    KEGGi lip:LI0435.
    PATRICi 22304279. VBILawInt40445_0479.

    Phylogenomic databases

    eggNOGi COG0436.
    HOGENOMi HOG000223061.
    KOi K10206.
    OMAi KWVDYAN.
    OrthoDBi EOG6XWV2X.

    Enzyme and pathway databases

    UniPathwayi UPA00034 ; UER00466 .
    BioCyci LINT363253:GH6E-449-MONOMER.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPi MF_01642. DapL_aminotrans_1.
    InterProi IPR004839. Aminotransferase_I/II.
    IPR019942. DapL_aminotrans.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR11751:SF22. PTHR11751:SF22. 1 hit.
    Pfami PF00155. Aminotran_1_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR03542. DAPAT_plant. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of Lawsonia intracellularis: the causative agent of proliferative enteropathy."
      Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L., Peterson A., May B., Singh S., Gebhart C., Kapur V.
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PHE/MN1-00.

    Entry informationi

    Entry nameiDAPAT_LAWIP
    AccessioniPrimary (citable) accession number: Q1MR87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 2008
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 60 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3