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

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Reviewed, UniProtKB/Swiss-Prot Q8R635 (MURE_FUSNN)

Last modified November 3, 2009. Version 56. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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:	FN1225

Organism

Fusobacterium nucleatum subsp. nucleatum [Complete proteome] [HAMAP]

Taxonomic identifier

76856 [NCBI]

Taxonomic lineage

Bacteria › Fusobacteria › Fusobacterales › Fusobacteriaceae › Fusobacterium

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Protein attributes

Sequence length	485 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 485

485

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

PRO_0000101897

Regions

Nucleotide binding

108 – 114

ATP Potential

Region

148 – 149

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

Region

398 – 401

Meso-diaminopimelate binding By similarity

Motif

398 – 401

Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site

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

Binding site

147

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

Binding site

175

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

Binding site

183

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

Binding site

374

Meso-diaminopimelate By similarity

Binding site

449

Meso-diaminopimelate; via carbonyl oxygen By similarity

Binding site

453

Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue

215

N6-carboxylysine By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q8R635-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: E6299E43F2B7FF19
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FASTA

485

55,485

        10         20         30         40         50         60 
MNIFSGIEYK VLKDVNLDRK YDGIEYDSRK IKENYIFVAF EGANVDGHNY IDSAVKNGAT 

        70         80         90        100        110        120 
CIIVSKKVEM KHNVSYILID DIRHKLGYIA SNFYEWPQRK LKIIGVTGTN GKTSSTYMIE 

       130        140        150        160        170        180 
KLMGDIPITR IGTIEYKIGD KVFEAVNTTP ESLDLIKIFD KTLKKKIEYV IMEVSSHSLE 

       190        200        210        220        230        240 
IGRVEVLDFD YALFTNLTQD HLDYHLTMEN YFQAKRKLFL KLKDINNSVI NVDDEYGKRL 

       250        260        270        280        290        300 
YDEFIVDNPE IISYGIENGD LEGDYSDDGY IDVKYKNQIE KVKFSLLGDF NLYNTLGAIG 

       310        320        330        340        350        360 
IALKIGISME EILKRVSNIK AAPGRFEALD CGQDYKVIVD YAHTPDALVN VIVAARNIKN 

       370        380        390        400        410        420 
GSRIITIFGC GGDRDRTKRP IMAKVAEDLS DVVILTSDNP RTESPEQIFD DVKKGFIKSD 

       430        440        450        460        470        480 
DYFFEPDREK AIKLAINMAE KNDIILITGK GHETYHIIGT KKWHFDDKEI ARREIVRRKM 


VENVN

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References

[1]

"Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum strain ATCC 25586."
Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A., Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O., Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N.

Overbeek R.
J. Bacteriol. 184:2005-2018(2002) [PubMed: 11889109] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131.

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Cross-references

Sequence databases
	AE009951 Genomic DNA. Translation: AAL95421.1.
RefSeq	NP_604122.1.
3D structure databases
HSSP	HSSP built from PDB template 1E8C based on UniProtKB P22188.
ModBase	Search...
Genome annotation databases
GeneID	992024.
GenomeReviews	Gene locus FN1225 in contig AE009951_GR.
KEGG	fnu:FN1225.
NMPDR	fig\|190304.1.peg.1801.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8R635.
OMA	HTPDGIE.
Enzyme and pathway databases
BioCyc	FNUC190304:FN1225-MON.
BRENDA	6.3.2.13. 289963.
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...

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Entry information

Entry name

MURE_FUSNN

Accession

Primary (citable) accession number: Q8R635

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	June 1, 2002
Last modified:	November 3, 2009
This is version 56 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)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents