Skip Header

Contribute Send feedback
Read comments (?) or add your own

A0M529 (MURD_GRAFK) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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:GFO_2770
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeGramella

Protein attributes

Sequence length445 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 – 445445UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639
PRO_0000301428

Regions

Nucleotide binding110 – 1167ATP Potential

Sequences

Sequence LengthMass (Da)Tools
A0M529 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 0FC7AD7EA9F9D06D

FASTA44549,848
        10         20         30         40         50         60 
MGKKIVILGG GESGIGTAIL AKKNGYDVFL SDKGKIKDKY KEVLKHIEIE WEDEKHTESK 

        70         80         90        100        110        120 
IFDADVVMKS PGIPDKAPMI VKLKEKGISV VSEIEFASWF SEVPVIGITG SNGKTTVTNL 

       130        140        150        160        170        180 
VQHLLKEGGI NSGMGGNIGN SYAKMVAEEM HDWFVLELSS FQLDGIEKFK PHIAILTNIT 

       190        200        210        220        230        240 
PDHLDRYDYK LENYIASKFR IAENQTEEDY FIYDADDKNI TDWLEKNPVR SQKLPFSIEK 

       250        260        270        280        290        300 
KIENGAYIEN ENIVVTINNT KFTMPTSELA LQGKHNAKNA MAASMVSQLL RIRKQTIRES 

       310        320        330        340        350        360 
MASFQGVEHR LEKVLKINNV LYINDSKATN VNATFYALES MESETVWILG GVDKGNVYDD 

       370        380        390        400        410        420 
LLPLVNEKVK AIICLGVDNE KIVSAFGNIV DTMVETTSMS EAVQMAYRLS DKGDNVLLSP 

       430        440 
ACASFDLFEN YEDRGRQFKE AVRNL 

« Hide

References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT0803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU207366 Genomic DNA. Translation: CAL67724.1.
RefSeqYP_862791.1. NC_008571.1.

3D structure databases

ProteinModelPortalA0M529.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0M529.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4652456.
GenomeReviewsGene locus GFO_2770 in contig CU207366_GR.
KEGGgfo:GFO_2770.
NMPDRfig|411154.5.peg.2617.
PATRIC22074294. VBIGraFor5527_2673.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0771.
HOGENOMHBG750024.
OMAACASWDM.
PhylomeDBA0M529.
ProtClustDBCLSK823532.

Enzyme and pathway databases

BioCycGFOR411154:GFO_2770-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_GRAFK
AccessionPrimary (citable) accession number: A0M529
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 41 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