Skip Header

Contribute Send feedback
Read comments (?) or add your own

P57316 (MURE_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

EC=6.3.2.13
Alternative name(s):
Meso-A2pm-adding enzyme
Meso-diaminopimelate-adding enzyme
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
UDP-MurNAc-tripeptide synthetase
UDP-N-acetylmuramyl-tripeptide synthetase
Gene names
Name:murE
Ordered Locus Names:BU221
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP MF_00208

Catalytic activity

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. HAMAP MF_00208

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208

Subcellular location

Cytoplasm By similarity HAMAP MF_00208.

Post-translational modification

Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP MF_00208

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 497497UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101873

Regions

Nucleotide binding116 – 1227ATP Potential
Region158 – 1592UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region416 – 4194Meso-diaminopimelate binding By similarity
Motif416 – 4194Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site291UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1571UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1911UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1931UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3921Meso-diaminopimelate By similarity
Binding site4671Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4711Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2251N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P57316 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 2BE0CC808B370FBF

FASTA49756,983
        10         20         30         40         50         60 
MNKICLKYLL LPWIKNIPKK YISNLKMDSR TLTPGDLFIA VPGIKKDGRH FIVQAINKKA 

        70         80         90        100        110        120 
AAILCETKKK DKHGIFKYIK NVILIYFFKL SENVSLLANR FYKEPGKRLK IIGITGTNGK 

       130        140        150        160        170        180 
TTVTQLINQW STILGTKTAT MGTLGNGFYN SLQPTNNTTS SPIFIQLFLS KVLEKQAELV 

       190        200        210        220        230        240 
TMEVSSHGLI QHRVKEVPFY IAIFTNLTQD HLDYHENLEK YESAKWLLFS THKVKKIILN 

       250        260        270        280        290        300 
ADDQYGKIWL KKLLNFYTVA VTIQNRKQKK YSTKWINATN IEQNNNSIYI TFESSWGTGR 

       310        320        330        340        350        360 
ISSCLIGRFN VTNLLLSLAC LLELGYSLSD LIHTSEKIIP VQGRMELFSY VKKPTFIIDY 

       370        380        390        400        410        420 
AHTPDALKKT LNAIHSHYQR YIWCIFGCGG ERDQKKRPIM GAIAEKMSDK VIITNDNPRN 

       430        440        450        460        470        480 
EKEKKIIQDI LNGCKNKEKI LIIPDRKKAI SYAYFGAKYH HIILIAGKGH EEKQIIQNRS 

       490 
INYSDKKIVL NLLGKNI 

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed: 10993077] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000003 Genomic DNA. Translation: BAB12937.1.
RefSeqNP_240051.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57316.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000002951; EBBUCP00000002727; EBBUCG00000002951.
GeneID1109664.
GenomeReviewsGene locus BU221 in contig BA000003_GR.
KEGGbuc:BU221.
PATRIC21243964. VBIBucAph127364_0234.

Phylogenomic databases

GeneTreeEBGT00050000007737.
HOGENOMHBG602753.
OMAGADPYQK.
PhylomeDBP57316.
ProtClustDBCLSK2459965.

Enzyme and pathway databases

BioCycBSP107806:BU221-MONOMER.

Family and domain databases

HAMAPMF_00208. MurE.
[Tree]
InterProIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
Gene3DG3DSA:3.90.190.20. Mur_ligase_C. 1 hit.
G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KOK01928.
PfamPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
SUPFAMSSF53244. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMsTIGR01085. MurE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_BUCAI
AccessionPrimary (citable) accession number: P57316
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families