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A4IM04 (MURE_GEOTN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:GTNG_0980
OrganismGeobacillus thermodenitrificans (strain NG80-2) [Complete proteome] [HAMAP]
Taxonomic identifier420246 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length489 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 – 489489UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_1000012355

Regions

Nucleotide binding108 – 1147ATP Potential
Region150 – 1512UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region407 – 4104Meso-diaminopimelate binding By similarity
Motif407 – 4104Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1491UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1771UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1831UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3831Meso-diaminopimelate By similarity
Binding site4591Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4631Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2171N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4IM04 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: 59FF7596C049AEEF

FASTA48953,536
        10         20         30         40         50         60 
MKLQTLLSRL PGFWVHRGGN PDIVALEMDS RHVTPGSLFF CVKGFTVDGH DFAEQAVERG 

        70         80         90        100        110        120 
AVAIVAERPL SVNVPVVVVP DSRRAMAILA DAFYGQPTHR LHLIGVTGTN GKTTTTHIIE 

       130        140        150        160        170        180 
QVARKAGKKI GLIGTVGTKI GDRSYPAVNT TPESLVLQRT FKQMVDEGVE FVTMEVSSHA 

       190        200        210        220        230        240 
LHQGRVHGCD YDVAVFTNLT QDHLDYHGTM EEYRNAKGLL FAQLGNRYDE RRPKFAVLNH 

       250        260        270        280        290        300 
DDPVSQYYKH MTAAPIITYG IKEKSDVMAE QIEMTPGGMA FQLCTPHGTM AIETKLVGLF 

       310        320        330        340        350        360 
NVYNLLAATA ACLASGFSLA TIAEALANVS PVPGRFETVD EGQNFTVIVD YAHTPDSVEN 

       370        380        390        400        410        420 
ALKTVRQFAK RNVYVVIGCG GDRDRTKRPL MAQAAVRYAD VAVFTSDNPR SEDPRQILRD 

       430        440        450        460        470        480 
MEAGVSAGDG TYVTIPDREE AIRYAIGQAQ EGDVVLIAGK GHETYQIIGD DVIDFDDRAV 


ARAAVKERR 

« Hide

References

[1]"Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed: 17372208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NG80-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000557 Genomic DNA. Translation: ABO66358.1.
RefSeqYP_001125103.1. NC_009328.1.

3D structure databases

ProteinModelPortalA4IM04.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4IM04.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4965923.
GenomeReviewsGene locus GTNG_0980 in contig CP000557_GR.
KEGGgtn:GTNG_0980.
NMPDRfig|420246.5.peg.947.
PATRIC21978295. VBIGeoThe136879_1031.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHBG602753.
OMAGALAYVD.
PhylomeDBA4IM04.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycGTHE420246:GTNG_0980-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_GEOTN
AccessionPrimary (citable) accession number: A4IM04
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2007
Last modified: December 14, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families