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Q97H84 (MURE1_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. 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-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase 1
EC=6.3.2.13
Alternative name(s):
Meso-A2pm-adding enzyme 1
Meso-diaminopimelate-adding enzyme 1
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase 1
UDP-MurNAc-tripeptide synthetase 1
UDP-N-acetylmuramyl-tripeptide synthetase 1
Gene names
Name:murE1
Ordered Locus Names:CA_C2129
OrganismClostridium acetobutylicum
Taxonomic identifier1488 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan By similarity. HAMAP MF_00208

Catalytic activity

ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate. HAMAP MF_00208

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208

Subcellular location

Cytoplasm By similarity HAMAP MF_00208.

Post-translational modification

Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP MF_00208

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase 1 HAMAP MF_00208
PRO_0000101885

Regions

Nucleotide binding110 – 1167ATP Potential
Region152 – 1532UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region402 – 4054Meso-diaminopimelate binding By similarity
Motif402 – 4054Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1791UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1871UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3781Meso-diaminopimelate By similarity
Binding site4521Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4561Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2191N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q97H84 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 28ACC8D8CEAF7CED

FASTA48254,194
        10         20         30         40         50         60 
MKLKKIIGDV KYELICGDLN VEIDNLNYDS RKVNEKGLFF CIEGYTSDGH DFIDKAVEKG 

        70         80         90        100        110        120 
ADVIVCTKVP KKLPNCTVVK VEDGRKAMAV MGANFYDNPS HKLKLIGITG TNGKTTSTYM 

       130        140        150        160        170        180 
MKSMLESSGY KVGLIGTIAN YIGDKKIESH RTTPESLELQ KLFSDMVHDK IDYCVMEVSS 

       190        200        210        220        230        240 
HSLYLDRVYG IVFEEGIFTN LTQDHLDFHK TFENYYKAKM ILFKNSKRSI INIDDKYGER 

       250        260        270        280        290        300 
VFKDAGNDKI TYGLTEKADL KAENLKMTSR GTEFDLCYRG LREHVKINIP GKYNVYNALG 

       310        320        330        340        350        360 
SVAACLNEGI SIEKVKDGLN KLSSVPGRCE IVTHNTNLDF DVVLDYAHTP DGLEKVLKAS 

       370        380        390        400        410        420 
REFTKGRLIS VFGCGGDRDK TKRPIMGEIG SKLSDIAVIT SDNPRSENPE EIIKDIVQGI 

       430        440        450        460        470        480 
KTDNYVIVEN RKEAIKKAML MAKKDDVIVL AGKGHENYQI LGDKTIHFDE KEIVSEFIKE 


LF

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE001437 Genomic DNA. Translation: AAK80087.1.
PIRD97162.
RefSeqNP_348747.1. NC_003030.1.

3D structure databases

ProteinModelPortalQ97H84.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1118312.
GenomeReviewsGene locus CA_C2129 in contig AE001437_GR.
KEGGcac:CA_C2129.
NMPDRfig|272562.1.peg.2276.
PATRIC32038637. VBICloAce74127_2331.

Phylogenomic databases

HOGENOMHBG602753.
OMAIGTIANY.
PhylomeDBQ97H84.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycCACE272562:CAC2129-MONOMER.

Family and domain databases

HAMAPMF_00208. MurE.
[Tree]
InterProIPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
Gene3DG3DSA:3.90.190.20. Mur_ligase_C. 1 hit.
G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KOK01928.
PfamPF01225. Mur_ligase. 1 hit.
PF02875. 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.
TIGRFAMsTIGR01085. MurE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE1_CLOAB
AccessionPrimary (citable) accession number: Q97H84
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: October 1, 2001
Last modified: January 25, 2012
This is version 76 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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