B7I325 (MURD_ACIB5) 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:	AB57_0334

Organism

Acinetobacter baumannii (strain AB0057) [Complete proteome] [HAMAP]

Taxonomic identifier

480119 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length	448 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 448	448	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_1000130820
Regions
	Nucleotide binding	112 – 118	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	B7I325 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 9C01945CDA3E63EC	FASTA	448	47,932
	10 20 30 40 50 60 MLIQRGGLKV VAGLGISGVS AVNFLHEQGY QVAVTDSRPT PPGHDQIPAG VKTSFGQLDQ 70 80 90 100 110 120 ELLLQAEEII LSPGLAPQLP EIQAAIAKGI SVVGDIQLLR RATDVPIVAI TGSNAKSTVT 130 140 150 160 170 180 TLIGLMAKDA GKKVAVGGNL GRPALDLLKD QPELLVLELS SFQLETTSHL NAEVAVVLNM 190 200 210 220 230 240 SEDHLDRHGN MLGYHQAKHR IFQGAKKVVF NRDDALSRPL VPDTTPMQSF GLNAPDLNQY 250 260 270 280 290 300 GVLRDADGTL WLARGLQRLI KSSDLYIQGM HNVANALACL ALGEAIGLPM ESMLETLKQF 310 320 330 340 350 360 KGLEHRCEYV KTVHDVRYYN DSKGTNVGAT LAAIDGLGAA IEVKKGKVAL ILGGQGKGQD 370 380 390 400 410 420 FGPLRSSIEK YAKVVVLIGE DAPVIEQAIQ GATKILHAAT LKEAVELCQR ETQAEDVVLL 430 440 SPACASFDMF KSYNDRGQQF VACVNSLV

References

[1]

"Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii." Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., Bonomo R.A., Gill S.R. J. Bacteriol. 190:8053-8064(2008) [PubMed: 18931120] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AB0057.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001182 Genomic DNA. Translation: ACJ39760.1.
RefSeq	YP_002317743.1. NC_011586.1.
3D structure databases
ProteinModelPortal	B7I325.
ModBase	Search...
Protein-protein interaction databases
STRING	B7I325.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7045992.
GenomeReviews	Gene locus AB57_0334 in contig CP001182_GR.
KEGG	abn:AB57_0334.
PATRIC	20694477. VBIAciBau111166_0332.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG750024.
OMA	ACASWDM.
ProtClustDB	PRK03803.
Family and domain databases
HAMAP	MF_00639. MurD. [Tree]
InterPro	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_ACIB5

Accession

Primary (citable) accession number: B7I325

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	January 25, 2012
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program