Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8DJI4

- MURE_THEEB

UniProt

Q8DJI4 - MURE_THEEB

Protein

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

Gene

murE

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei32 – 321UDP-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 sitei385 – 3851Meso-diaminopimelateUniRule annotation
    Binding sitei460 – 4601Meso-diaminopimelate; via carbonyl oxygenUniRule annotation
    Binding sitei464 – 4641Meso-diaminopimelateUniRule annotation

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. tetrahydrofolylpolyglutamate synthase activity Source: InterPro
    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: UniProtKB-HAMAP
    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

    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:tlr1239
    OrganismiThermosynechococcus elongatus (strain BP-1)
    Taxonomic identifieri197221 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
    ProteomesiUP000000440: 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 – 497497UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligasePRO_0000101959Add
    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

    STRINGi197221.tlr1239.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8DJI4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni155 – 1562UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation
    Regioni409 – 4124Meso-diaminopimelate bindingUniRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi409 – 4124Meso-diaminopimelate recognition motif

    Sequence similaritiesi

    Belongs to the MurCDEF family. MurE subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0769.
    HOGENOMiHOG000268118.
    KOiK01928.
    OMAiVDYAHTG.
    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.
    InterProiIPR018109. Folylpolyglutamate_synth_CS.
    IPR004101. 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.

    Q8DJI4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNLRELLTAA AITPGFEHPA LNQEVKSLRM NSWECEPGSL FIGMPGTRVE    50
    GGNFWPSALA AGAIAAVVSP QAKPREGEAC VIVVPDIERA CGRLAAAFYN 100
    YPSQHLSLLG VTGTNGKTTT THLVEHLLNR VGYPTALLGT LYSRWPGHCE 150
    VASHTTPFAV TLQEQLAAAV DAGCRFGVME VSSHALAQDR VWGCQFEVAA 200
    FTNLTQDHLD YHRDLEDYFA AKAKLFTADY LKGRAILNGD DPFGQRLAQQ 250
    LPRDRYWTYG LSKDADFRAE NLNYRSNGVT GAVHTPLGSG TLDSPLVGQF 300
    NVANVLAAIA MGAAVGLPLE AMLNALRDFP GVPGRMEQVR LDPEQDITVV 350
    VDYAHTPDSL ENLLRAARPF IPGKLICVFG CGGDRDRSKR PQMGAIAARL 400
    ADQVVVTSDN PRTENPQRIL DDILAGIPPE TAMIVEGDRR QAILQAILTA 450
    APGDGVIIAG KGHEDYQILG TEKVHFDDRE EARNALKERL KQPLQRG 497
    Length:497
    Mass (Da):53,933
    Last modified:March 1, 2003 - v1
    Checksum:i2F21F05584ECF07B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000039 Genomic DNA. Translation: BAC08791.1.
    RefSeqiNP_682029.1. NC_004113.1.
    WP_011057081.1. NC_004113.1.

    Genome annotation databases

    EnsemblBacteriaiBAC08791; BAC08791; BAC08791.
    GeneIDi1011779.
    KEGGitel:tlr1239.
    PATRICi23927810. VBITheElo119873_1303.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000039 Genomic DNA. Translation: BAC08791.1 .
    RefSeqi NP_682029.1. NC_004113.1.
    WP_011057081.1. NC_004113.1.

    3D structure databases

    ProteinModelPortali Q8DJI4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 197221.tlr1239.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC08791 ; BAC08791 ; BAC08791 .
    GeneIDi 1011779.
    KEGGi tel:tlr1239.
    PATRICi 23927810. VBITheElo119873_1303.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00219 .

    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 IPR018109. Folylpolyglutamate_synth_CS.
    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: BP-1.

    Entry informationi

    Entry nameiMURE_THEEB
    AccessioniPrimary (citable) accession number: Q8DJI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 83 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