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Q9S2W9 (MURD_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. 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:SCO2086
ORF Names:SC4A10.19c
OrganismStreptomyces coelicolor
Taxonomic identifier1902 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length471 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 – 471471UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639
PRO_0000109106

Regions

Nucleotide binding122 – 1287ATP Potential

Sequences

Sequence LengthMass (Da)Tools
Q9S2W9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: EF5A042077CBD9F3

FASTA47149,143
        10         20         30         40         50         60 
MPSEFSGKHV TVAGLGVSGV PAAKVLHGLG AQVTVVNDGD DERARTQAAE LEPLGVTVRL 

        70         80         90        100        110        120 
GDGDTLPEGT ELIVTAPGWK PTKPLFTAAG QAGVPVWGDV ELAWRLRGLN GRKPAPWLAV 

       130        140        150        160        170        180 
TGTNGKTTTV QMLASILKAA GLRTAAVGNI GVSLLDAVTG EQEYDVLAVE LSSYQLHWAP 

       190        200        210        220        230        240 
SLRAHSAAVL NLAPDHLDWH GSMEAYAADK GRIYEGNHVA CVYNVADKAT EDLVRAADVE 

       250        260        270        280        290        300 
EGCRAIGFTL GTPGPSQLGV VEGLLVDRAF VEDRQKNAQE LAEVSDVNPP APHNIANALA 

       310        320        330        340        350        360 
AAGLARAFGV SAAAVRDGLR AFTPDAHRIA HVADVDGVAY VDDSKATNTH ATEASLAAYE 

       370        380        390        400        410        420 
SIVWIAGGLA KGATFDELVA GAAKRLRGAV LIGADRALIR EALARHAPEV PVVDLDRTDT 

       430        440        450        460        470 
GAMLQAVQEA RRLARPGDTV LLAPACASMD MFTNYNQRGD AFAQAVRELG A 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939111 Genomic DNA. Translation: CAB51995.1.
PIRT34956.
RefSeqNP_626345.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9S2W9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1097520.
GenomeReviewsGene locus SCO2086 in contig AL645882_GR.
KEGGsco:SCO2086.
NMPDRfig|100226.1.peg.2052.
PATRIC23733820. VBIStrCoe124346_2119.

Phylogenomic databases

HOGENOMHBG750024.
OMAACASWDM.
PhylomeDBQ9S2W9.
ProtClustDBPRK01438.

Family and domain databases

HAMAPMF_00639. MurD.
[Tree]
InterProIPR018109. Folylpolyglutamate_synth_CS.
IPR004101. 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_STRCO
AccessionPrimary (citable) accession number: Q9S2W9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 77 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