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

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Q7NFN2 (MURE_GLOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. 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:	gll3492

Organism

Gloeobacter violaceus (strain PCC 7421)

Taxonomic identifier

251221 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Gloeobacteria › Gloeobacterales › Gloeobacter

Protein attributes

Sequence length	489 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 489

489

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

PRO_0000101898

Regions

Nucleotide binding

113 – 119

ATP Potential

Region

154 – 155

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

Region

405 – 408

Meso-diaminopimelate binding By similarity

Motif

405 – 408

Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site

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

Binding site

181

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

Binding site

187

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

Binding site

189

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

Binding site

381

Meso-diaminopimelate By similarity

Binding site

456

Meso-diaminopimelate; via carbonyl oxygen By similarity

Binding site

460

Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue

221

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q7NFN2 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: F97812986E7BC486
Show »

FASTA

489

52,454

        10         20         30         40         50         60 
MPAMRLHELL ARTGLDTRNL PDIDIAGLST DSRQVQPGDL FIGLPGTRVD GSEFWPQAIA 

        70         80         90        100        110        120 
GGAAGLVISE NARGVEAAVP VIRVPDVVGT CARLASAYYD FPARKLTLAG VTGTNGKTTT 

       130        140        150        160        170        180 
THLIENLLQA QAPTGLVGTL YSRWPGQSQE ARHTTPFALE IQKLLAQMVE AGCQYGVMEV 

       190        200        210        220        230        240 
SSHALAQQRV AGCRFEAAVF TNLTQDHLDF HPDMESYFQA KATLFSPEYR SGRAVINADD 

       250        260        270        280        290        300 
PWGVRLAAAY DQVWTYSFQP GADIYPEDAV FTPEGIRGTL VTPVGRAAFT SPLVGQFNLA 

       310        320        330        340        350        360 
NLLAAVGATL ALGIDLEAIA AGLSGFGGVP GRMERVSGSD DDIAVIVDYA HTPDGLRKLL 

       370        380        390        400        410        420 
EATRPFVRGR LICVFGCGGD RDRTKRPQMG RIAAELSDLP VVTSDNPRTE NPEAILDDIL 

       430        440        450        460        470        480 
AGIPVGVSPT VEVDRRRAIL QALLEAKAGD CVVIAGKGHE DYQILGTTKI HFDDREQARE 


ALSKRRSRG

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References

[1]

"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids."
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.
DNA Res. 10:137-145(2003) [PubMed: 14621292] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7421.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000045 Genomic DNA. Translation: BAC91433.1.
RefSeq	NP_926438.1. NC_005125.1.
3D structure databases
ProteinModelPortal	Q7NFN2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2601896.
GenomeReviews	Gene locus gll3492 in contig BA000045_GR.
NMPDR	fig\|251221.1.peg.3492.
PATRIC	22046475. VBIGloVio86258_3526.
Phylogenomic databases
HOGENOM	HBG602753.
OMA	GALAYVD.
PhylomeDB	Q7NFN2.
ProtClustDB	PRK00139.
Enzyme and pathway databases
BioCyc	GVIO251221:GLL3492-MONOMER.
Family and domain databases
HAMAP	MF_00208. MurE. [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]
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_GLOVI

Accession

Primary (citable) accession number: Q7NFN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	December 15, 2003
Last modified:	January 25, 2012
This is version 62 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