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A0QF47 (MURE_MYCA1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 41. 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:MAV_2331
OrganismMycobacterium avium (strain 104) [Complete proteome] [HAMAP]
Taxonomic identifier243243 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium avium complex (MAC)

Protein attributes

Sequence length520 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 – 520520UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_1000058589

Regions

Nucleotide binding134 – 1407ATP Potential
Region176 – 1772UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region429 – 4324Meso-diaminopimelate binding By similarity
Motif429 – 4324Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site481UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site2031UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site2111UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site4051Meso-diaminopimelate By similarity
Binding site4831Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4871Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2431N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QF47 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: C22B8555632D09C5

FASTA52053,765
        10         20         30         40         50         60 
MVSVPTGLRP SAVPGVRLPA LADQVGAVMA GPDRRAAVPD VTVTGVTLRA QDVLPGDLFA 

        70         80         90        100        110        120 
ALPGATTHGA RHAAEAIERG AVAVLTDAAG VAQLTGGRTT PTLLHPRPRS VLGELAAAVY 

       130        140        150        160        170        180 
AHPSERLTVI GITGTSGKTT TTYLVESGLR AAGRTAGLIG TVGIRIDGAD IPSALTTPEA 

       190        200        210        220        230        240 
PALQALLAAM AEQRVDTVVM EVSSHALALG RVDGTRFAVG GFTNLSRDHL DFHPTMADYF 

       250        260        270        280        290        300 
EAKALLFDPN SPLRAHRAVV CIDDEAGREM AARAGDAVTV SAEGQPAHWR AVEVAPLGTG 

       310        320        330        340        350        360 
GQQFTVIDPA GVQHRAGIRL PGHYNVANCL VALALLDAVG VSPEQAAPGL LQTRVPGRME 

       370        380        390        400        410        420 
EIDAGQDFLA LVDYAHKPGA LRAVLSSLKR PDRRLAVVFG AGGERDPGKR APMGATAAEL 

       430        440        450        460        470        480 
ADLVVVTDDN PRGEDPAAIR REILAGATES GCAAEVIEIG DRRAAIRHAV AWAGPGDVVL 

       490        500        510        520 
VAGKGHETGQ RTGEHTRPFD DRVELAEALR EAVGPRKAQG

« Hide

References

[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 104.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000479 Genomic DNA. Translation: ABK64811.1.
RefSeqYP_881535.1. NC_008595.1.

3D structure databases

ProteinModelPortalA0QF47.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0QF47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000009090; EBMYCP00000008976; EBMYCG00000009088.
GeneID4526429.
GenomeReviewsGene locus MAV_2331 in contig CP000479_GR.
KEGGmav:MAV_2331.
PATRIC17986364. VBIMycAvi38287_2270.
TIGRMAV_2331.

Phylogenomic databases

eggNOGCOG0769.
GeneTreeEBGT00050000015779.
HOGENOMHBG602753.
OMAHTTPEST.
PhylomeDBA0QF47.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycMAVI243243:MAV_2331-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_MYCA1
AccessionPrimary (citable) accession number: A0QF47
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 41 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

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