UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

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Q8KGC9 (MURE_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
EC=6.3.2.13

Alternative name(s):
Meso-A2pm-adding enzyme
Meso-diaminopimelate-adding enzyme
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
UDP-MurNAc-tripeptide synthetase
UDP-N-acetylmuramyl-tripeptide synthetase

Gene names

Name:	murE
Ordered Locus Names:	CT0039

Organism

Chlorobium tepidum

Taxonomic identifier

1097 [NCBI]

Taxonomic lineage

Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum

Protein attributes

Sequence length	508 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity Inferred from electronic annotation. Source: EC tetrahydrofolylpolyglutamate synthase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 508

508

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208

PRO_0000101882

Regions

Nucleotide binding

124 – 130

ATP Potential

Region

166 – 167

UDP-MurNAc-L-Ala-D-Glu binding By similarity

Region

428 – 431

Meso-diaminopimelate binding By similarity

Motif

428 – 431

Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

193

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

201

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

404

Meso-diaminopimelate By similarity

Binding site

478

Meso-diaminopimelate; via carbonyl oxygen By similarity

Binding site

482

Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue

233

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8KGC9 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 0744F64F4B4E9490
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FASTA

508

54,302

        10         20         30         40         50         60 
MKEIREGAPG AQLDDLVAAL GALAERRGGD GARAVITGVT CDSRAVTPGA LFVAVRGLVA 

        70         80         90        100        110        120 
DGHHFIGAAI EAGAVAVACE ELPAAYSDSV TWLVVPDARK ALAELSKAFY GNASDKLMLI 

       130        140        150        160        170        180 
GVTGTNGKTT TARLVTSMLN ASGVAAGYIG TGLCRIGNHD IPLERTTPEP NRLHDLFRQM 

       190        200        210        220        230        240 
VDAGCRAAVM EVSSHSLVLD RVHGLFFRAA VFTNLTPEHL DFHETMEEYA EAKRLLFDQL 

       250        260        270        280        290        300 
NAEGFAVINA DDPRAEFMAA RLAPERVFCC STGDNTSLCD PARRFHAVIT ASTVEGSKAD 

       310        320        330        340        350        360 
VTFDGQSMAM QVPLPGAYNV MNMLEAFTVG VGLGIDPATA LRSLAAADAI AGRMERIWSR 

       370        380        390        400        410        420 
DRSRCAVVDY AHTPDALQKA LEALRAVTPA DAKLAVVFGC GGNRDRQKRP EMGRIAAELA 

       430        440        450        460        470        480 
DRVILTSDNP RDENPEAILD EVEAGMAGRV HLRIADRAEA IRRAVEQLGA GDILLVAGKG 

       490        500 
HEAYQEIRGV KHHFSDRECL EACFAQMK

« Hide

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006470 Genomic DNA. Translation: AAM71287.1.
RefSeq	NP_660945.1. NC_002932.3.
3D structure databases
ProteinModelPortal	Q8KGC9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1006457.
GenomeReviews	Gene locus CT0039 in contig AE006470_GR.
KEGG	cte:CT0039.
NMPDR	fig\|194439.1.peg.39.
PATRIC	21398179. VBIChlTep116050_0038.
TIGR	CT0039.
Phylogenomic databases
HOGENOM	HBG602753.
OMA	SCANAAG.
ProtClustDB	CLSK637122.
Enzyme and pathway databases
BioCyc	CTEP194439:CT_0039-MONOMER.
Family and domain databases
HAMAP	MF_00208. MurE. [Tree]
InterPro	IPR018109. Folylpolyglutamate_synth_CS. IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KO	K01928.
Pfam	PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
SUPFAM	SSF53244. Mur_ligase_C. 1 hit. SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMs	TIGR01085. MurE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURE_CHLTE

Accession

Primary (citable) accession number: Q8KGC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents