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Reviewed, UniProtKB/Swiss-Prot O67631 (MURE_AQUAE)

Last modified November 3, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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):
    UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
    Meso-diaminopimelate-adding enzyme
    Meso-A2pm-adding enzyme
    UDP-N-acetylmuramyl-tripeptide synthetase
    UDP-MurNAc-tripeptide synthetase
Gene names
Name: murE
Ordered Locus Names: aq_1747
OrganismAquifex aeolicus [Complete proteome] [HAMAP]
Taxonomic identifier63363 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

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Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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.

Post-translational modification

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

Sequence similarities

Belongs to the murCDEF family. MurE subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101862

Regions

Nucleotide binding108 – 1147ATP Potential
Region150 – 1512UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region396 – 3994Meso-diaminopimelate binding By similarity
Motif396 – 3994Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site281UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site301UDP-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 site3721Meso-diaminopimelate By similarity
Binding site4471Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4511Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2171N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
O67631-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 1CC91DA4BB76722E

FASTA48253,991
        10         20         30         40         50         60 
MGSNPTPSAS VLYMDLSFIL KRVKGITLNS KEVKKGYLFF AIKGTRFDGH NFIREAEERG 

        70         80         90        100        110        120 
AYAVVVERPV SSKVPVIIVE DTRKALGKSA HEFFGKPSER LNVIGITGTN GKTTTTHLIE 

       130        140        150        160        170        180 
KILLEAGEKT GLIGTIYYRL GEKILGSGRT TPDQITWHRT LKEFYELGAK NVVAEISSHA 

       190        200        210        220        230        240 
LDQYRVYPTR FEAVLFTNLS QDHLDYHKTM EDYFASKAKL FTEYESKVKI INADDTYGKR 

       250        260        270        280        290        300 
LLKITHGEII TYGKKGDLKI LNFRTDFRGS ALRIAFKGKE YEFSTNLIGD FQAYNLSAAI 

       310        320        330        340        350        360 
AYALWKGIEP DLIQRALKCV NVPGRFEVVH SDKFTVIIDY AHTPDAVENV LRTARKLSKG 

       370        380        390        400        410        420 
KLISVFGAGG NRDREKRPLM GKAAEKYSDL IILTSDNPRD EEPEKIIEDI LDGISEKDKV 

       430        440        450        460        470        480 
IIEADRRKAI KKAIDMAKEG DMVAILGKGH EDYQEIKGVK YPFSDAQVVK EILGGDGCIG 


KD

« Hide

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References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

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Cross-references

Sequence databases

AE000657 Genomic DNA. Translation: AAC07591.1.
PIRE70450.
RefSeqNP_214197.1.

3D structure databases

HSSPHSSP built from PDB template 1E8C based on UniProtKB P22188.
ModBaseSearch...

Genome annotation databases

GeneID1193346.
GenomeReviewsGene locus aq_1747 in contig AE000657_GR.
KEGGaae:aq_1747.
NMPDRfig|224324.1.peg.1212.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO67631.
OMAHTPDGIE.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1747-MON.
BRENDA6.3.2.13. 189781.

Family and domain databases

HAMAPMF_00208.
[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.
PfamPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameMURE_AQUAE
AccessionPrimary (citable) accession number: O67631
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents