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Q83F28

- MURE_COXBU

UniProt

Q83F28 - MURE_COXBU

Protein

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

Gene

murE

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.UniRule annotation

    Catalytic activityi

    ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei30 – 301UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei182 – 1821UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei188 – 1881UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei190 – 1901UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei388 – 3881Meso-diaminopimelateUniRule annotation
    Binding sitei463 – 4631Meso-diaminopimelate; via carbonyl oxygenUniRule annotation
    Binding sitei467 – 4671Meso-diaminopimelateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi113 – 1197ATPUniRule annotation

    GO - Molecular functioni

    1. acid-amino acid ligase activity Source: TIGR
    2. ATP binding Source: UniProtKB-HAMAP
    3. UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. peptidoglycan biosynthetic process Source: TIGR
    4. regulation of cell shape Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciCBUR227377:GJ7S-128-MONOMER.
    UniPathwayiUPA00219.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligaseUniRule annotation (EC:6.3.2.13UniRule annotation)
    Alternative name(s):
    Meso-A2pm-adding enzymeUniRule annotation
    Meso-diaminopimelate-adding enzymeUniRule annotation
    UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligaseUniRule annotation
    UDP-MurNAc-tripeptide synthetaseUniRule annotation
    UDP-N-acetylmuramyl-tripeptide synthetaseUniRule annotation
    Gene namesi
    Name:murEUniRule annotation
    Ordered Locus Names:CBU_0123
    OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
    Taxonomic identifieri227377 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
    ProteomesiUP000002671: 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 – 489489UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligasePRO_0000101891Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei222 – 2221N6-carboxylysineUniRule annotation

    Post-translational modificationi

    Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.UniRule annotation

    Interactioni

    Protein-protein interaction databases

    STRINGi227377.CBU_0123.

    Structurei

    3D structure databases

    ProteinModelPortaliQ83F28.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni155 – 1562UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation
    Regioni412 – 4154Meso-diaminopimelate bindingUniRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi412 – 4154Meso-diaminopimelate recognition motif

    Sequence similaritiesi

    Belongs to the MurCDEF family. MurE subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0769.
    HOGENOMiHOG000268118.
    KOiK01928.
    OMAiKIAVDYA.
    OrthoDBiEOG6PKFCR.

    Family and domain databases

    Gene3Di3.40.1190.10. 1 hit.
    3.40.1390.10. 1 hit.
    3.90.190.20. 1 hit.
    HAMAPiMF_00208. MurE.
    InterProiIPR004101. Mur_ligase_C.
    IPR013221. Mur_ligase_cen.
    IPR000713. Mur_ligase_N.
    IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
    [Graphical view]
    PfamiPF01225. Mur_ligase. 1 hit.
    PF02875. Mur_ligase_C. 1 hit.
    PF08245. Mur_ligase_M. 1 hit.
    [Graphical view]
    SUPFAMiSSF53244. SSF53244. 1 hit.
    SSF53623. SSF53623. 1 hit.
    SSF63418. SSF63418. 1 hit.
    TIGRFAMsiTIGR01085. murE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q83F28-1 [UniParc]FASTAAdd to Basket

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    MNGKYLSQLL DAKNKALTAD VLIKALQTDS RKIQPGDLFI AYPGLQVDGR    50
    DYIKEALDKK AAAVFYEANQ YNPSIQTKVP LIPFENLQHR IGEIAARFYD 100
    DPSCEMEIIG ITGTNGKTSC AQFIAQALQS QGIRCGVIGT LGYGFLGSLH 150
    KTSHTTPEPI QLQQAFAEMR KQGAKAIAME VSSHALHQRR VEGVQFDIAV 200
    FTQLSRDHLD YHGDMENYAR AKELLFQQPG LHTGVVNCDD ALGKRIIAHY 250
    RHQLTLVGYS ANGVKDDRVS SVIASAIQPL AQGFSVEVQT PWGEGTFTTP 300
    LFGRFNISNL LAVLSVLCLC EIPFDKALLE LSQLRNVPGR MQVVDSQRQP 350
    QIIVDYAHTP DALEKALTAL REHCQGRLIC VFGCGGDRDR GKRPQMAAVA 400
    EQHADQIILT NDNPRTESPL TIIQDIQAGF KNKNAVLVKL DRAEAIRYAV 450
    QMAAVNDIVL IAGKGHETTQ TIADQVLPFN DVEEAKKAL 489
    Length:489
    Mass (Da):53,828
    Last modified:June 1, 2003 - v1
    Checksum:i6AC4716157215B22
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016828 Genomic DNA. Translation: AAO89687.1.
    RefSeqiNP_819173.1. NC_002971.3.

    Genome annotation databases

    EnsemblBacteriaiAAO89687; AAO89687; CBU_0123.
    GeneIDi1207994.
    KEGGicbu:CBU_0123.
    PATRICi17928931. VBICoxBur82552_0126.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE016828 Genomic DNA. Translation: AAO89687.1 .
    RefSeqi NP_819173.1. NC_002971.3.

    3D structure databases

    ProteinModelPortali Q83F28.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 227377.CBU_0123.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO89687 ; AAO89687 ; CBU_0123 .
    GeneIDi 1207994.
    KEGGi cbu:CBU_0123.
    PATRICi 17928931. VBICoxBur82552_0126.

    Phylogenomic databases

    eggNOGi COG0769.
    HOGENOMi HOG000268118.
    KOi K01928.
    OMAi KIAVDYA.
    OrthoDBi EOG6PKFCR.

    Enzyme and pathway databases

    UniPathwayi UPA00219 .
    BioCyci CBUR227377:GJ7S-128-MONOMER.

    Family and domain databases

    Gene3Di 3.40.1190.10. 1 hit.
    3.40.1390.10. 1 hit.
    3.90.190.20. 1 hit.
    HAMAPi MF_00208. MurE.
    InterProi IPR004101. Mur_ligase_C.
    IPR013221. Mur_ligase_cen.
    IPR000713. Mur_ligase_N.
    IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
    [Graphical view ]
    Pfami PF01225. Mur_ligase. 1 hit.
    PF02875. Mur_ligase_C. 1 hit.
    PF08245. Mur_ligase_M. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53244. SSF53244. 1 hit.
    SSF53623. SSF53623. 1 hit.
    SSF63418. SSF63418. 1 hit.
    TIGRFAMsi TIGR01085. murE. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RSA 493 / Nine Mile phase I.

    Entry informationi

    Entry nameiMURE_COXBU
    AccessioniPrimary (citable) accession number: Q83F28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 79 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. Coxiella burnetii
      Coxiella burnetii (strain RSA 493): entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3