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Q1QVG5 (MURD_CHRSD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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-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:Csal_2192
OrganismChromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]
Taxonomic identifier290398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHalomonadaceaeChromohalobacter

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00639

Subcellular location

Cytoplasm By similarity HAMAP MF_00639.

Sequence similarities

Belongs to the MurCDEF family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 455455UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639
PRO_0000257179

Regions

Nucleotide binding118 – 1247ATP Potential

Sequences

Sequence LengthMass (Da)Tools
Q1QVG5 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 16D3EA8BA4530CCB

FASTA45548,490
        10         20         30         40         50         60 
MPRVPAAHTL VIGLGVSGQA IARHLSRRGE PFMVADTRES PAGLEAFRAA HPGVDVVCGP 

        70         80         90        100        110        120 
LEALDMQEAR EIVLSPGVDP RTPGLIDYVD HPGSGPEVVG EMALFVRECR SPIAAITGSN 

       130        140        150        160        170        180 
AKSTVTTLLG EMARESGWKT AVGGNLGTPA LDLLDESPDA ELFVLELSSF QLETTPWLGA 

       190        200        210        220        230        240 
DTAAFLNLSE DHLDRHGDMQ GYRAAKQRIF RGARHAVVNA EDPATWPDAP SCAVTRFTTD 

       250        260        270        280        290        300 
MPESGEWGIV DHDGERWLAQ GRAAIMPVGQ VRMPGRHNHA NALAALAMGA HLGLSREAMC 

       310        320        330        340        350        360 
RVLERFPGLP HRGEFIVERE GVRWINDSKG TNVGATLAAI AGIGSDLEGR LILLAGGDGK 

       370        380        390        400        410        420 
GADFSPLAEP LAHHAREAIV FGRDAERLEQ ALSARLPVTR VADLAAAMQR ARTIARAGDT 

       430        440        450 
VLLSPACASL DQFPNYMARG EAFRQWLATD GEAAC 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000285 Genomic DNA. Translation: ABE59543.1.
RefSeqYP_574242.1. NC_007963.1.

3D structure databases

ProteinModelPortalQ1QVG5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1QVG5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4026686.
GenomeReviewsGene locus Csal_2192 in contig CP000285_GR.
KEGGcsa:Csal_2192.
NMPDRfig|290398.4.peg.2862.
PATRIC21448236. VBIChrSal113723_2212.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0771.
HOGENOMHBG750024.
OMAACASWDM.

Enzyme and pathway databases

BioCycCSAL290398:CSAL_2192-MONOMER.

Family and domain databases

HAMAPMF_00639. MurD.
[Tree]
InterProIPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR016040. NAD(P)-bd_dom.
IPR005762. UDP-N-AcMur-Glu_ligase.
[Graphical view]
Gene3DG3DSA:3.90.190.20. Mur_ligase_C. 1 hit.
G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK01925.
PANTHERPTHR23135:SF2. PTHR23135:SF2. 1 hit.
PfamPF02875. 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.
TIGRFAMsTIGR01087. MurD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURD_CHRSD
AccessionPrimary (citable) accession number: Q1QVG5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 16, 2006
Last modified: January 25, 2012
This is version 45 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