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

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Reviewed, UniProtKB/Swiss-Prot Q8CZE6 (MURE1_OCEIH)

Last modified February 9, 2010. Version 53. 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 1
    UDP-MurNAc-tripeptide synthetase 1

Gene names

Name:	murE1
Ordered Locus Names:	OB1466

Organism

Oceanobacillus iheyensis [Complete proteome] [HAMAP]

Taxonomic identifier

182710 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Oceanobacillus

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Protein attributes

Sequence length	493 AA.
Sequence status	Complete.
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. 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.

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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 cellular 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 – 493

493

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

PRO_0000101918

Regions

Nucleotide binding

111 – 117

ATP Potential

Region

153 – 154

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

Region

410 – 413

Meso-diaminopimelate binding By similarity

Motif

410 – 413

Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site

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

Binding site

152

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

Binding site

180

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

Binding site

188

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

Binding site

386

Meso-diaminopimelate By similarity

Binding site

462

Meso-diaminopimelate; via carbonyl oxygen By similarity

Binding site

466

Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue

220

N6-carboxylysine By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q8CZE6-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 90ABD31721ACC3A5
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FASTA

493

54,816

        10         20         30         40         50         60 
MELKKLLECL TFYNVNGEVE NCEITSLEMD SRKITSGSAF VCITGFTVDG HDYVDQAVKN 

        70         80         90        100        110        120 
GASAIFTSKP LMKEYGVPII QVEDTNRALA MLAVKYYDYP TKHFPLIGVT GTNGKTTVTY 

       130        140        150        160        170        180 
LLDKIFEYHQ KKAGVIGTIQ VKIGEETFPI VNTTPNALEL QKTFHVMREK DVKQGIMEVS 

       190        200        210        220        230        240 
SHALDMGRVY GCDYDIAVFT NLSQDHLDYH QDIQDYLRAK SLLFAQLGNG YDSEKEKYAI 

       250        260        270        280        290        300 
INDDDSSSHL LKRSTAQHVI TYSCKKEATI MAKDIELTAS GIRFKLHSPL GNITIQSRLM 

       310        320        330        340        350        360 
GMFNVYNMLA ASAAAIASKV PLNVIQQALE SIEGVNGRFE PIVEGQNYSV IVDFAHTPDS 

       370        380        390        400        410        420 
LENVLQTIKD FAKRNVYVVV GCGGDRDRKK RPLMAEVALN YADHAVFTSD NPRTEDPQAI 

       430        440        450        460        470        480 
LDDMTAELDA NSGSYEVVVD RKEGIAKAIQ SAQKDDIVLI AGKGHETYQI IGHTKYDFDD 

       490 
RDVARNAIKQ KGE

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References

[1]

"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments."
Takami H., Takaki Y., Uchiyama I.
Nucleic Acids Res. 30:3927-3935(2002) [PubMed: 12235376] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000028 Genomic DNA. Translation: BAC13422.1.
RefSeq	NP_692387.1.
3D structure databases
SMR	Q8CZE6. Positions 18-492.
ModBase	Search...
Genome annotation databases
GeneID	1017713.
GenomeReviews	Gene locus OB1466 in contig BA000028_GR.
KEGG	oih:OB1466.
NMPDR	fig\|221109.1.peg.1468.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG602753.
OMA	EHLDFHG.
Enzyme and pathway databases
BioCyc	OIHE221109:OB1466-MONOMER.
BRENDA	6.3.2.13. 278212.
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]
TIGRFAMs	TIGR01085. murE. 1 hit.
ProtoNet	Search...

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Entry information

Entry name

MURE1_OCEIH

Accession

Primary (citable) accession number: Q8CZE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	March 1, 2003
Last modified:	February 9, 2010
This is version 53 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