Reviewed, UniProtKB/Swiss-Prot Q8NNN0 (MURE_CORGL)

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

Gene names

Name:	murE
Ordered Locus Names:	Cgl2163, cg2374

Organism

Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
Post-translational modification	Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity.
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
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP 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: HAMAP UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 517	517	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208		PRO_0000101890
Regions
	Nucleotide binding	122 – 128	7	ATP Potential
	Region	164 – 165	2	UDP-MurNAc-L-Ala-D-Glu binding By similarity
	Region	418 – 421	4	Meso-diaminopimelate binding By similarity
	Motif	418 – 421	4	Meso-diaminopimelate recognition motif HAMAP MF_00208
Sites
	Binding site	34	1	UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
	Binding site	36	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	191	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	199	1	UDP-MurNAc-L-Ala-D-Glu By similarity
	Binding site	394	1	Meso-diaminopimelate By similarity
	Binding site	476	1	Meso-diaminopimelate; via carbonyl oxygen By similarity
	Binding site	480	1	Meso-diaminopimelate By similarity
Amino acid modifications
	Modified residue	231	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8NNN0-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: F0A266A70DD5DFE5	FASTA	517	53,862
	10 20 30 40 50 60 MLDLTKLIDG ILKGSAQGVP AHAVGEQAIA AIGLDSSSLP TSDAIFAAVP GTRTHGAQFA 70 80 90 100 110 120 GTDNAAKAVA ILTDAAGLEV LNEAGETRPV IVVDDVRAVL GAASSSIYGD PSKDFTLIGV 130 140 150 160 170 180 TGTSGKTTTS YLLEKGLMEA GHKVGLIGTT GTRIDGEEVP TKLTTPEAPT LQALFARMRD 190 200 210 220 230 240 HGVTHVVMEV SSHALSLGRV AGSHFDVAAF TNLSQDHLDF HPTMDDYFDA KALFFRADSP 250 260 270 280 290 300 LVADKQVVCV DDSWGQRMAS VAADVQTVST LGQEADFSAT DINVSDSGAQ SFKINAPSNQ 310 320 330 340 350 360 SYQVELALPG AFNVANATLA FAAAARVGVD GEAFARGMSK VAVPGRMERI DEGQDFLAVV 370 380 390 400 410 420 DYAHKPAAVA AVLDTLRTQI DGRLGVVIGA GGDRDSTKRG PMGQLSAQRA DLVIVTDDNP 430 440 450 460 470 480 RSEVPATIRA AVTAGAQQGA SESERPVEVL EIGDRAEAIR VLVEWAQPGD GIVVAGKGHE 490 500 510 VGQLVAGVTH HFDDREEVRA ALTEKLNNKL PLTTEEG

References

[1]

"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

[2]

"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000036 Genomic DNA. Translation: BAB99556.1. BX927154 Genomic DNA. Translation: CAF20503.1. Different initiation.
RefSeq	NP_601365.1. YP_226404.1.
3D structure databases
HSSP	HSSP built from PDB template 1E8C based on UniProtKB P22188.
ModBase	Search...
Genome annotation databases
GeneID	1020115. 3345142.
GenomeReviews	Gene locus Cgl2163 in contig BA000036_GR. Gene locus cg2374 in contig BX927147_GR.
KEGG	cgb:cg2374. cgl:NCgl2083.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8NNN0.
OMA	FPVIVDY.
Enzyme and pathway databases
BioCyc	CGLU196627-1:CG2374-MON.
BRENDA	6.3.2.13. 812.
Family and domain databases
HAMAP	MF_00208. [Tree]
InterPro	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.
Pfam	PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
TIGRFAMs	TIGR01085. murE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURE_CORGL

Accession

Primary (citable) accession number: Q8NNN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	October 1, 2002
Last modified:	November 3, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)