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Q3ME15

- MURE_ANAVT

UniProt

Q3ME15 - MURE_ANAVT

Protein

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

Gene

murE

Organism
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (25 Oct 2005)
      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 sitei32 – 321UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei185 – 1851UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei191 – 1911UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei193 – 1931UDP-MurNAc-L-Ala-D-GluUniRule annotation
    Binding sitei389 – 3891Meso-diaminopimelateUniRule annotation
    Binding sitei464 – 4641Meso-diaminopimelate; via carbonyl oxygenUniRule annotation
    Binding sitei468 – 4681Meso-diaminopimelateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi116 – 1227ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. 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

    BioCyciAVAR240292:GCY3-1159-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:Ava_1147
    OrganismiAnabaena variabilis (strain ATCC 29413 / PCC 7937)
    Taxonomic identifieri240292 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena
    ProteomesiUP000002533: 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 – 496496UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligasePRO_1000012335Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei225 – 2251N6-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

    STRINGi240292.Ava_1147.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3ME15.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni158 – 1592UDP-MurNAc-L-Ala-D-Glu bindingUniRule annotation
    Regioni413 – 4164Meso-diaminopimelate bindingUniRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi413 – 4164Meso-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.
    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.

    Q3ME15-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLRELLATV DSVENLPPVL ADTEVKGIKT NSHACGAGDL FIGMPGTRVD    50
    GGEFWPSAIA SGAIAAIVSP QAVEKNPPSD EAVVISSNNM TKACAAIAAA 100
    FYGYPGQKLK LVGVTGTNGK TTTTHLIEFF LTKAQLSTAL MGTLYTRWPG 150
    FEQTATHTTP FAVELQQQLA QAVNAGCEFG VMEVSSHALA QGRVLGCPFE 200
    VGVFSNLTQD HLDYHSDMED YFAAKALLFS PDYLKGRAII NADDTYGQRL 250
    IKALSPEKVW SYSVNDSSAD LWMSDLSYEP NGVTGTIHTP EGDVSFRSPL 300
    VGQYNLENLL ASVGAVLHLG LDLQLIANAI PEFPGVPGRM ERVQINPDQD 350
    ISVIVDYAHT PDSLENLLKA ARPFIPGRMI CVFGCGGDRD RTKRPKMGKI 400
    AAELADLAFV TSDNPRTEDP EKILDDILAG IPDTVQPTVI GDRAIAIRTA 450
    ILQAQPGDGV LLAGKGHEDY QILGTEKIHF DDREHARAAL TEREKL 496
    Length:496
    Mass (Da):53,416
    Last modified:October 25, 2005 - v1
    Checksum:iDCDF7907B96B79BA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000117 Genomic DNA. Translation: ABA20771.1.
    RefSeqiWP_011317994.1. NC_007413.1.
    YP_321666.1. NC_007413.1.

    Genome annotation databases

    EnsemblBacteriaiABA20771; ABA20771; Ava_1147.
    GeneIDi3683401.
    KEGGiava:Ava_1147.
    PATRICi35422808. VBIAnaVar43351_1967.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000117 Genomic DNA. Translation: ABA20771.1 .
    RefSeqi WP_011317994.1. NC_007413.1.
    YP_321666.1. NC_007413.1.

    3D structure databases

    ProteinModelPortali Q3ME15.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 240292.Ava_1147.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABA20771 ; ABA20771 ; Ava_1147 .
    GeneIDi 3683401.
    KEGGi ava:Ava_1147.
    PATRICi 35422808. VBIAnaVar43351_1967.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00219 .
    BioCyci AVAR240292:GCY3-1159-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. "Complete sequence of Anabaena variabilis ATCC 29413."
      Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 29413 / PCC 7937.

    Entry informationi

    Entry nameiMURE_ANAVT
    AccessioniPrimary (citable) accession number: Q3ME15
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: October 25, 2005
    Last modified: October 1, 2014
    This is version 66 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