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P45060 (MURE_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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:HI_1133
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length488 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 – 488488UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101900

Regions

Nucleotide binding113 – 1197ATP Potential
Region41 – 433UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region155 – 1562UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region410 – 4134Meso-diaminopimelate binding By similarity
Motif410 – 4134Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site241UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site261UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1541UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1821UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1881UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1901UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3861Meso-diaminopimelate By similarity
Binding site4611Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4651Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2221N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P45060 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 46E20FF7491BC45A

FASTA48853,523
        10         20         30         40         50         60 
MKKLTALFNL PELKNDIELH NMVLDSRKVK AGDLFVAIKG HQVDGNQFID SALHSGASAV 

        70         80         90        100        110        120 
VSETELSSEH LTVAFIGNVP VVKYYQLAHH LSSLADVFYD SPSNNLTLVG VTGTNGKTTI 

       130        140        150        160        170        180 
SQLLAQWAEL LGHRAAVMGT IGNGLFGQIV EAKNTTGSAV EIQSSLSAFK HAGADFTSIE 

       190        200        210        220        230        240 
VSSHGLAQHR VEALHFKAAI FTNLTRDHLD YHQSMENYAA AKKRLFTELD TQIKVINADD 

       250        260        270        280        290        300 
EIGYQWLTEL PDAIAVSMNA DFKVGSHQWM KAINIHYHFK GADITFESSW GNGVLHSPLI 

       310        320        330        340        350        360 
GAFNVSNLLL VMTTLLSFGY PLENLLATAK SLKGVCGRME MIQYPNKPTV IVDYAHTPDA 

       370        380        390        400        410        420 
LEKALIAARE HCQGELWCIF GCGGDRDRGK RPLMAQVAEQ FAEKIIVTKD NPRTESQSQI 

       430        440        450        460        470        480 
ETDIVAGFKN MEKVGIIPDR AQAIQFAIES AVENDVILIA GKGHEHYQII GSEVVHFSDQ 


EIALDFLK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC22788.1.
PIRH64184.
RefSeqNP_439291.1. NC_000907.1.

3D structure databases

ProteinModelPortalP45060.
SMRP45060. Positions 15-487.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID949983.
GenomeReviewsGene locus HI_1133 in contig L42023_GR.
KEGGhin:HI1133.
NMPDRfig|71421.1.peg.1086.
PATRIC20190941. VBIHaeInf48452_1183.
TIGRHI_1133.

Phylogenomic databases

HOGENOMHBG602753.
OMAGALAYVD.
PhylomeDBP45060.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycHINF71421:HI_1133-MONOMER.

Family and domain databases

HAMAPMF_00208. MurE.
[Tree]
InterProIPR004101. 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 nameMURE_HAEIN
AccessionPrimary (citable) accession number: P45060
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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