Q6FFC2 (MURD_ACIAD) 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:	ACIAD0270

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

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.
Sequence caution	The sequence CAG67235.1 differs from that shown. Reason: Erroneous initiation.

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_0000108953
Regions
	Nucleotide binding	112 – 118	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6FFC2 [UniParc]. Last modified March 1, 2005. Version 2. Checksum: C3BAAFA3B2C55B56	FASTA	448	48,460
	10 20 30 40 50 60 MLIQRGGLKV VAGLGISGVS AVNFLHEQGY RVAVTDSRET PPGHDQIPQD VQTSFGQLDT 70 80 90 100 110 120 ELLLQAEEII LSPGLAPQLP EIQQAIAQGI PVIGDIQVLR RATQVPIVAI TGSNAKSTVT 130 140 150 160 170 180 TLFGQMAKDA GKRVAVGGNL GRPGLDLLKD EPELLVLELS SFQLETTSHL NAEVAVILNM 190 200 210 220 230 240 SEDHLDRHGD MLGYHQAKHR IFQGVKKVVY NRDDSLTRPL VPDSTPMQSF GLNAPDIKQY 250 260 270 280 290 300 GVLREDDGTM WLARGRTRLI KSSELYIQGT HNIANALACL ALGEAIGLPV ESMLETLKQF 310 320 330 340 350 360 KGLEHRCEYV KTVNDVRYYN DSKGTNVGAT LAAIDGLGAA IEPKQGKVIV ILGGQGKGQD 370 380 390 400 410 420 FSLLRQSVEK YVKAAILIGE DAQQIEQALT ETTQLVHAST LKDAVTQAQQ YAQPEDVVLL 430 440 SPACASFDMF KGYPDRGHQF VACVDALV

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ADP1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR543861 Genomic DNA. Translation: CAG67235.1. Different initiation.
RefSeq	YP_045057.1. NC_005966.1.
3D structure databases
ProteinModelPortal	Q6FFC2.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FFC2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2879156.
GenomeReviews	Gene locus ACIAD0270 in contig CR543861_GR.
KEGG	aci:ACIAD0270.
NMPDR	fig|62977.3.peg.611.
PATRIC	20738502. VBIAciSp98416_0241.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0771.
HOGENOM	HBG750024.
PhylomeDB	Q6FFC2.
ProtClustDB	PRK03803.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD0270-MONOMER.
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_ACIAD

Accession

Primary (citable) accession number: Q6FFC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	March 1, 2005
Last modified:	January 25, 2012
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program