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Q7U0E7

- DAPD_MYCBO

UniProt

Q7U0E7 - DAPD_MYCBO

Protein

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase

Gene

dapD

Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    • Comment

    Functioni

    Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA.UniRule annotation

    Catalytic activityi

    Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H2O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi166 – 1661Magnesium 1; shared with trimeric partnersUniRule annotation
    Metal bindingi183 – 1831Magnesium 2; shared with trimeric partnersUniRule annotation
    Active sitei199 – 1991Acyl-anhydride intermediateUniRule annotation
    Binding sitei201 – 2011Succinyl-CoAUniRule annotation
    Binding sitei216 – 2161Succinyl-CoA; via amide nitrogenUniRule annotation
    Binding sitei219 – 2191Succinyl-CoAUniRule annotation
    Binding sitei242 – 2421Succinyl-CoA; via amide nitrogenUniRule annotation
    Binding sitei265 – 2651Succinyl-CoA; via carbonyl oxygenUniRule annotation
    Binding sitei277 – 2771Succinyl-CoAUniRule annotation

    GO - Molecular functioni

    1. 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase activity Source: UniProtKB-HAMAP
    2. magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. diaminopimelate biosynthetic process Source: UniProtKB-HAMAP
    2. lysine biosynthetic process via diaminopimelate Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00034; UER00019.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferaseUniRule annotation (EC:2.3.1.117UniRule annotation)
    Alternative name(s):
    Tetrahydrodipicolinate N-succinyltransferaseUniRule annotation
    Short name:
    THDP succinyltransferaseUniRule annotation
    Short name:
    THP succinyltransferaseUniRule annotation
    Tetrahydropicolinate succinylaseUniRule annotation
    Gene namesi
    Name:dapDUniRule annotation
    Ordered Locus Names:Mb1233c
    OrganismiMycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
    Taxonomic identifieri233413 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    ProteomesiUP000001419: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3173172,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferasePRO_0000412255Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi233413.Mb1233c.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7U0E7.
    SMRiQ7U0E7. Positions 3-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni257 – 2582Succinyl-CoA bindingUniRule annotation
    Regioni290 – 2934Succinyl-CoA bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the type 2 tetrahydrodipicolinate N-succinyltransferase family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000248194.
    KOiK00674.
    OMAiTVLDTWF.
    OrthoDBiEOG6HQSR3.

    Family and domain databases

    HAMAPiMF_02122. DapD_type2.
    InterProiIPR019875. DapD_actinobacteria.
    IPR011004. Trimer_LpxA-like.
    IPR026586. Type2_DapD.
    [Graphical view]
    SUPFAMiSSF51161. SSF51161. 1 hit.
    TIGRFAMsiTIGR03535. DapD_actino. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q7U0E7-1 [UniParc]FASTAAdd to Basket

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    MSTVTGAAGI GLATLAADGS VLDTWFPAPE LTESGTSATS RLAVSDVPVE    50
    LAALIGRDDD RRTETIAVRT VIGSLDDVAA DPYDAYLRLH LLSHRLVAPH 100
    GLNAGGLFGV LTNVVWTNHG PCAIDGFEAV RARLRRRGPV TVYGVDKFPR 150
    MVDYVVPTGV RIADADRVRL GAHLAPGTTV MHEGFVNYNA GTLGASMVEG 200
    RISAGVVVGD GSDVGGGASI MGTLSGGGTH VISIGKRCLL GANSGLGISL 250
    GDDCVVEAGL YVTAGTRVTM PDSNSVKARE LSGSSNLLFR RNSVSGAVEV 300
    LARDGQGIAL NEDLHAN 317
    Length:317
    Mass (Da):32,642
    Last modified:October 1, 2003 - v1
    Checksum:iEF204F46B90ADFF3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248333 Genomic DNA. Translation: CDO42480.1.
    RefSeqiNP_854887.1. NC_002945.3.

    Genome annotation databases

    EnsemblBacteriaiCAD94094; CAD94094; Mb1233c.
    GeneIDi1090520.
    KEGGimbo:Mb1233c.
    PATRICi18004399. VBIMycBov88188_1352.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX248333 Genomic DNA. Translation: CDO42480.1 .
    RefSeqi NP_854887.1. NC_002945.3.

    3D structure databases

    ProteinModelPortali Q7U0E7.
    SMRi Q7U0E7. Positions 3-310.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 233413.Mb1233c.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD94094 ; CAD94094 ; Mb1233c .
    GeneIDi 1090520.
    KEGGi mbo:Mb1233c.
    PATRICi 18004399. VBIMycBov88188_1352.

    Phylogenomic databases

    HOGENOMi HOG000248194.
    KOi K00674.
    OMAi TVLDTWF.
    OrthoDBi EOG6HQSR3.

    Enzyme and pathway databases

    UniPathwayi UPA00034 ; UER00019 .

    Family and domain databases

    HAMAPi MF_02122. DapD_type2.
    InterProi IPR019875. DapD_actinobacteria.
    IPR011004. Trimer_LpxA-like.
    IPR026586. Type2_DapD.
    [Graphical view ]
    SUPFAMi SSF51161. SSF51161. 1 hit.
    TIGRFAMsi TIGR03535. DapD_actino. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-935 / AF2122/97.

    Entry informationi

    Entry nameiDAPD_MYCBO
    AccessioniPrimary (citable) accession number: Q7U0E7
    Secondary accession number(s): X2BHN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 56 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

    Documents

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

    External Data

    Dasty 3