Skip Header

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

Q64ZL9 (MURD_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. 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:BF0308
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length444 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 – 444444UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639
PRO_0000108968

Regions

Nucleotide binding109 – 1157ATP Potential

Sequences

Sequence LengthMass (Da)Tools
Q64ZL9 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 2770589AA6093313

FASTA44449,577
        10         20         30         40         50         60 
MKRIVVLGAG ESGAGAAVLA KVKGFDTFVS DMSAIKDKYK TLLDGHGIAW EEGRHTEEQI 

        70         80         90        100        110        120 
LSADEVVKSP GIPNDAPLIL RLREQGTPII SEIEFAGRYT DAKMICITGS NGKTTTTSLI 

       130        140        150        160        170        180 
YHIFKSAGLN VGLAGNIGKS LALQVAEEKH DYYVIELSSF QLDNMYNFRA DIAVLMNITP 

       190        200        210        220        230        240 
DHLDRYDHCM QNYINAKFRI TQNQTSEDAF IFWNDDPIIK RELDKHGIRA HLYPFSAIKE 

       250        260        270        280        290        300 
EGSIAYVEDH EVVITEPIAF NMEQEQLALT GQHNLYNSLA AGISANLAGI TKEDIRKALS 

       310        320        330        340        350        360 
DFQGVEHRLE KVARVRGIDF INDSKATNVN SCWYALQSMT TKTVLILGGK DKGNDYTEIE 

       370        380        390        400        410        420 
ELVREKCSAL VYLGLHNEKL HEFFDRLGLP VAEVQTGMKD AVEAAYKLAK KGETVLLSPC 

       430        440 
CASFDLFKSY EDRGEQFKKY VREL 

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006841 Genomic DNA. Translation: BAD47057.1.
RefSeqYP_097591.1. NC_006347.1.

3D structure databases

ProteinModelPortalQ64ZL9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3081736.
GenomeReviewsGene locus BF0308 in contig AP006841_GR.
KEGGbfr:BF0308.
PATRIC21046394. VBIBacFra17906_0331.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG750024.
OMAACASWDM.
PhylomeDBQ64ZL9.
ProtClustDBCLSK2757457.

Enzyme and pathway databases

BioCycBFRA295405:BF0308-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_BACFR
AccessionPrimary (citable) accession number: Q64ZL9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 55 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