Q2YM69 (MURD_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-N-acetylmuramoylalanine--D-glutamate ligase
EC=6.3.2.9

Alternative name(s):
D-glutamic acid-adding enzyme
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase

Gene names

Name:	murD
Ordered Locus Names:	BAB1_1452

Organism

Brucella abortus (strain 2308) [Complete proteome] [HAMAP]

Taxonomic identifier

359391 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	467 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) By similarity. HAMAP MF_00639
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanine + glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. HAMAP MF_00639
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00639
Subcellular location	Cytoplasm By similarity HAMAP MF_00639.
Sequence similarities	Belongs to the MurCDEF family.

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: 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-acetylmuramoylalanine-D-glutamate ligase activity Inferred from electronic annotation. Source: EC tetrahydrofolylpolyglutamate synthase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 467	467	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000257169
Regions
	Nucleotide binding	121 – 127	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q2YM69 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 460D244D6D7849CA	FASTA	467	48,694
	10 20 30 40 50 60 MIPITALKDK TVALFGLGGS GIATAKAIVA GGARIIAWDD NPDSVARAQS AGIATGDLRQ 70 80 90 100 110 120 ADWSQFAVFV LSPGVPLTHP QPHWSVDLAR AAGVEIIGDV ELFVRERNHI APDCPFIAIT 130 140 150 160 170 180 GTNGKSTTTA LIAHIIKATG RDMQLGGNIG TAILTLEPPC ADRFYVVECS SYQIDLAPSL 190 200 210 220 230 240 NPTAGILLNL TPDHLDRHGS MENYAAIKER LVAASGTAII GIDDAYCQAI ADRLHGAGIR 250 260 270 280 290 300 VVRISKEKHL DRGYFADGAK LLWAQDGEID EIASLEGIGS LRGAHNAQNA LAAIVACLSA 310 320 330 340 350 360 GLSLEEIHAG LKSFPGLAHR MEQVGRRGKV LFVNDSKATN AEATAPALSS FPQNIYWIVG 370 380 390 400 410 420 GVPKAGGINS LTAFFPRVAK AYLIGEAAAQ FAATLGGAVP FEISDTLAAA VAHAAGDAGN 430 440 450 460 DAAPEPVVLL SPACASFDQF QNFEKRGDAF RDAVLALPGV MPMRGGS

References

[1]

"Whole-genome analyses of speciation events in pathogenic Brucellae." Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E. Infect. Immun. 73:8353-8361(2005) [PubMed: 16299333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 2308.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM040264 Genomic DNA. Translation: CAJ11408.1.
RefSeq	YP_414824.1. NC_007618.1.
3D structure databases
ProteinModelPortal	Q2YM69.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2YM69.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3788810.
GenomeReviews	Gene locus BAB1_1452 in contig AM040264_GR.
KEGG	bmf:BAB1_1452.
PATRIC	17845892. VBIBruMel86222_1509.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0771.
HOGENOM	HBG750024.
OMA	ACASWDM.
ProtClustDB	PRK01390.
Enzyme and pathway databases
BioCyc	BMEL359391:BAB1_1452-MONOMER.
Family and domain databases
HAMAP	MF_00639. MurD. [Tree]
InterPro	IPR018109. Folylpolyglutamate_synth_CS. IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR016040. NAD(P)-bd_dom. IPR005762. UDP-N-AcMur-Glu_ligase. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K01925.
PANTHER	PTHR23135:SF2. PTHR23135:SF2. 1 hit.
Pfam	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	TIGR01087. MurD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURD_BRUA2

Accession

Primary (citable) accession number: Q2YM69

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	December 20, 2005
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program