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A4XI02 (MURD_CALS8) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 35. 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:Csac_0923
OrganismCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]
Taxonomic identifier351627 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor

Protein attributes

Sequence length453 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 – 453453UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639
PRO_1000056878

Regions

Nucleotide binding117 – 1237ATP Potential

Sequences

Sequence LengthMass (Da)Tools
A4XI02 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: DD92A0A801D96303

FASTA45351,359
        10         20         30         40         50         60 
MDLFGKKVLV IGMGKSGISS ARFLKKHGAY VVAFDEKRED EMKTQQKETI RKFADELYFN 

        70         80         90        100        110        120 
DLPDAVVDTS DMVVISPGVP LTKRYITLAH KRGIEVIGEI ELAYRFCRSK NIVAITGTNG 

       130        140        150        160        170        180 
KTTTTTLVGE ILKKVFDNVI VCGNIGFPFI DYVESSTDDT IFVIEISSFQ LETIKYFKPM 

       190        200        210        220        230        240 
VGCILNITPD HLNRHMNMDN YIRAKMRIFE NIDQEGYSVL NMDNSITRDL IGCAKGTVIT 

       250        260        270        280        290        300 
FSKNESDTQN SVFVDGDFIY RNFLGKVEKV MRKDDIFMPG EHNLENTLAA IGCVLPFEIQ 

       310        320        330        340        350        360 
PSIIEKTLKE FKGVEHRIEF VREINGVRFY NDSKGTNTDA SSKALNSFEV PIILIAGGYD 

       370        380        390        400        410        420 
KGESFEKFAK LISQKVKKVF LLGQTKQKIA DQLQKIGYLN FEFVEDLKEA VKKSFEIAKE 

       430        440        450 
GDVVLLSPAC ASWDMFESYE QRGRLFKQYV NEL

« Hide

References

[1]"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000679 Genomic DNA. Translation: ABP66537.1.
RefSeqYP_001179728.1. NC_009437.1.

3D structure databases

ProteinModelPortalA4XI02.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4XI02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5087512.
GenomeReviewsGene locus Csac_0923 in contig CP000679_GR.
KEGGcsc:Csac_0923.
PATRIC21251456. VBICalSac56748_1044.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0771.
HOGENOMHBG750024.
OMAACASWDM.
ProtClustDBPRK14106.

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_CALS8
AccessionPrimary (citable) accession number: A4XI02
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: December 14, 2011
This is version 35 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

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