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C8U1G0 (C8U1G0_ECO10) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | 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 HAMAP-Rule MF_00639 RuleBase RU003664
EC=6.3.2.9 HAMAP-Rule MF_00639 RuleBase RU003664
Alternative name(s):
D-glutamic acid-adding enzyme HAMAP-Rule MF_00639
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase HAMAP-Rule MF_00639
Gene names
Name:murD HAMAP-Rule MF_00639 EMBL BAI28968.1
Ordered Locus Names:ECO103_0090 EMBL BAI28968.1
OrganismEscherichia coli O103:H2 (strain 12009 / EHEC) [Complete proteome] [HAMAP] EMBL BAI28968.1
Taxonomic identifier585395 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length438 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-Rule MF_00639 SAAS SAAS005762

Catalytic activity

ATP + UDP-N-acetylmuramoyl-L-alanine + glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. HAMAP-Rule MF_00639 SAAS SAAS005762

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00639 SAAS SAAS005762

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00639 SAAS SAAS005762.

Sequence similarities

Belongs to the MurCDEF family. HAMAP-Rule MF_00639 RuleBase RU003630

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding112 – 1187ATP By similarity HAMAP-Rule MF_00639

Sequences

Sequence LengthMass (Da)Tools
C8U1G0 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: 61EF4E13805A3B46

FASTA43846,921
        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 GLPALMLLDA 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 LNGLQVDGTL HLLLGGDGKS ADFSPLARYL 

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

       430 
KNFEQRGNEF ARLAKELG

« Hide

References

[1]"Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 12009 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP010958 Genomic DNA. Translation: BAI28968.1.
RefSeqYP_003220102.1. NC_013353.1.

3D structure databases

ProteinModelPortalC8U1G0.
SMRC8U1G0. Positions 2-438.
ModBaseSearch...

Protein-protein interaction databases

STRING585395.ECO103_0090.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAI28968; BAI28968; ECO103_0090.
GeneID8476053.
KEGGeoh:ECO103_0090.
PATRIC32091711. VBIEscCol146794_0090.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0771.
HOGENOMHOG000049427.
KOK01925.
OMARCGELDV.
ProtClustDBPRK03806.

Enzyme and pathway databases

BioCycECOL585395:GJA9-91-MONOMER.
UniPathwayUPA00219.

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]
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 nameC8U1G0_ECO10
AccessionPrimary (citable) accession number: C8U1G0
Entry history
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: May 1, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info