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Q9PLG5 (MURD_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. 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:TC_0139
OrganismChlamydia muridarum [Complete proteome] [HAMAP]
Taxonomic identifier83560 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length416 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 caution

The sequence AAF39017.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639
PRO_0000108992

Regions

Nucleotide binding108 – 1147ATP Potential

Sequences

Sequence LengthMass (Da)Tools
Q9PLG5 [UniParc].

Last modified April 30, 2003. Version 2.
Checksum: 0F7C4879B3EDC8D3

FASTA41646,265
        10         20         30         40         50         60 
MGLKRVVVIG LGLSGKSIAR FLARKGVYVL GVDSSIQALQ HCPYIHEKLL ETDEFPTQVD 

        70         80         90        100        110        120 
YVVRSPGISK DHPWVKAARA AQISVVTDIQ LAFQTKEFIE QKSFGITGTV GKTTTILFLE 

       130        140        150        160        170        180 
YLLRKAGIPA FAMGNVGVPI LDGMQNSGVR LVEMSSFQLA DQETSYPVLS GGMILNISDN 

       190        200        210        220        230        240 
HLDYHGSFLE YCQSKQNLSL CMRNPEDLWV GDQRFCGRSY WEEVQKYMRL LDKESALKPL 

       250        260        270        280        290        300 
YLHDKYNYCC AYLLAQAEFP IAKSLFIEAV ATFKKPSHRM EYLGEKCGVH YINDSKATTV 

       310        320        330        340        350        360 
RATEKALLSI GSRAIVILGG RNKGYSFVSL LPSLRRFAKS VVAMGECAQE IAQDLDGFPV 

       370        380        390        400        410 
TVVRNLHEAL LCAEEQAIPG DVVLLSPACA SFDQFRSYEE RGAIFKQLVG MEEVLL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39017.1. Different initiation.
PIRF81736.
RefSeqNP_296518.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PLG5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1245673.
GenomeReviewsGene locus TC_0139 in contig AE002160_GR.
KEGGcmu:TC0139.
PATRIC20371644. VBIChlMur19118_0152.
TIGRTC_0139.

Phylogenomic databases

HOGENOMHBG750024.
PhylomeDBQ9PLG5.
ProtClustDBPRK00683.

Enzyme and pathway databases

BioCycCMUR243161:TC_0139-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_CHLMU
AccessionPrimary (citable) accession number: Q9PLG5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: April 30, 2003
Last modified: January 25, 2012
This is version 73 of the entry and version 2 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