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P14900 (MURD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
UDP-N-acetylmuramoylalanine--D-glutamate ligase

EC=6.3.2.9
Alternative name(s):
D-glutamic acid-adding enzyme
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
Gene names
Name:murD
Ordered Locus Names:b0088, JW0086
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). HAMAP-Rule MF_00639

Catalytic activity

ATP + UDP-N-acetylmuramoyl-L-alanine + glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. HAMAP-Rule MF_00639

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00639

Subcellular location

Cytoplasm HAMAP-Rule MF_00639.

Sequence similarities

Belongs to the MurCDEF family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-554780,EBI-554780

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 438437UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP-Rule MF_00639
PRO_0000109013

Regions

Nucleotide binding112 – 1187ATP Potential

Experimental info

Sequence conflict281R → A in CAA35611. Ref.2
Sequence conflict1741A → T in CAA35611. Ref.2
Sequence conflict276 – 2772AL → RV in CAA35611. Ref.2

Secondary structure

............................................................................................ 438
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14900 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 11C64782C098F761

FASTA43846,974
        10         20         30         40         50         60 
MADYQGKNVV IIGLGLTGLS CVDFFLARGV TPRVMDTRMT PPGLDKLPEA VERHTGSLND 

        70         80         90        100        110        120 
EWLMAADLIV ASPGIALAHP SLSAAADAGI EIVGDIELFC REAQAPIVAI TGSNGKSTVT 

       130        140        150        160        170        180 
TLVGEMAKAA GVNVGVGGNI GLPALMLLDD ECELYVLELS SFQLETTSSL QAVAATILNV 

       190        200        210        220        230        240 
TEDHMDRYPF GLQQYRAAKL RIYENAKVCV VNADDALTMP IRGADERCVS FGVNMGDYHL 

       250        260        270        280        290        300 
NHQQGETWLR VKGEKVLNVK EMKLSGQHNY TNALAALALA DAAGLPRASS LKALTTFTGL 

       310        320        330        340        350        360 
PHRFEVVLEH NGVRWINDSK ATNVGSTEAA LNGLHVDGTL HLLLGGDGKS ADFSPLARYL 

       370        380        390        400        410        420 
NGDNVRLYCF GRDGAQLAAL RPEVAEQTET MEQAMRLLAP RVQPGDMVLL SPACASLDQF 

       430 
KNFEQRGNEF ARLAKELG 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence involving murD and an open reading frame ORF-Y spacing murF and ftsW in Escherichia coli."
Ikeda M., Wachi M., Ishino F., Matsuhashi M.
Nucleic Acids Res. 18:1058-1058(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Nucleotide sequence of the murD gene encoding the UDP-MurNAc-L-Ala-D-Glu synthetase of Escherichia coli."
Mengin-Lecreulx D., van Heijenoort J.
Nucleic Acids Res. 18:183-183(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]Flouret B.
Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively."
Ikeda M., Sato T., Wachi M., Jung H.K., Ishino F., Kobayashi Y., Matsuhashi M.
J. Bacteriol. 171:6375-6378(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-438.
Strain: K12.
[8]"Over-production, purification and properties of the uridine diphosphate N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli."
Pratviel-Sosa F., Mengin-Lecreulx D., van Heijenoort J.
Eur. J. Biochem. 202:1169-1176(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-20.
Strain: K12.
[9]"Crystal structure of UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase from Escherichia coli."
Bertrand J.A., Auger G., Fanchon E., Martin L., Blanot D., van Heijenoort J., Dideberg O.
EMBO J. 16:3416-3425(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[10]"'Open' structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase."
Bertrand J.A., Fanchon E., Martin L., Chantalat L., Auger G., Blanot D., van Heijenoort J., Dideberg O.
J. Mol. Biol. 301:1257-1266(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51584 Genomic DNA. Translation: CAA35933.1.
X17609 Genomic DNA. Translation: CAA35611.1.
X55034 Genomic DNA. Translation: CAA38865.1.
M30807 Genomic DNA. Translation: AAA83858.1.
U00096 Genomic DNA. Translation: AAC73199.1.
AP009048 Genomic DNA. Translation: BAB96656.1.
PIRCEECME. S08396.
RefSeqNP_414630.1. NC_000913.3.
YP_488393.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0DX-ray2.40A2-438[»]
1EEHX-ray1.90A2-438[»]
1UAGX-ray1.95A2-438[»]
2JFFX-ray1.89A2-438[»]
2JFGX-ray1.52A2-438[»]
2JFHX-ray1.97A2-438[»]
2UAGX-ray1.70A2-438[»]
2UUOX-ray2.50A2-438[»]
2UUPX-ray1.88A2-438[»]
2VTDX-ray1.94A1-438[»]
2VTEX-ray2.20A1-438[»]
2WJPX-ray1.60A2-438[»]
2X5OX-ray1.46A2-438[»]
2XPCX-ray1.49A2-438[»]
2Y1OX-ray1.49A1-438[»]
2Y66X-ray1.49A1-438[»]
2Y67X-ray1.85A1-438[»]
2Y68X-ray1.49A1-438[»]
3UAGX-ray1.77A2-438[»]
4UAGX-ray1.66A2-438[»]
ProteinModelPortalP14900.
SMRP14900. Positions 2-438.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10279N.
IntActP14900. 8 interactions.
MINTMINT-1269366.
STRING511145.b0088.

Chemistry

BindingDBP14900.
ChEMBLCHEMBL4732.

Proteomic databases

PaxDbP14900.
PRIDEP14900.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73199; AAC73199; b0088.
BAB96656; BAB96656; BAB96656.
GeneID12932483.
944818.
KEGGecj:Y75_p0087.
eco:b0088.
PATRIC32115281. VBIEscCol129921_0092.

Organism-specific databases

EchoBASEEB0615.
EcoGeneEG10620. murD.

Phylogenomic databases

eggNOGCOG0771.
HOGENOMHOG000049427.
KOK01925.
OMAYCFGQDG.
OrthoDBEOG6PKFCR.
PhylomeDBP14900.

Enzyme and pathway databases

BioCycEcoCyc:UDP-NACMURALA-GLU-LIG-MONOMER.
ECOL316407:JW0086-MONOMER.
MetaCyc:UDP-NACMURALA-GLU-LIG-MONOMER.
SABIO-RKP14900.
UniPathwayUPA00219.

Gene expression databases

GenevestigatorP14900.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.40.50.720. 1 hit.
3.90.190.20. 1 hit.
HAMAPMF_00639. MurD.
InterProIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR016040. NAD(P)-bd_dom.
IPR005762. UDP-N-AcMur-Glu_ligase.
[Graphical view]
PfamPF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
SUPFAMSSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
TIGRFAMsTIGR01087. murD. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP14900.
PROP14900.

Entry information

Entry nameMURD_ECOLI
AccessionPrimary (citable) accession number: P14900
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 156 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene