Q7VUQ1 (MURD_BORPE) 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:	BP3025

Organism

Bordetella pertussis

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	510 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 Reference 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 – 510	510	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000108978
Regions
	Nucleotide binding	138 – 144	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q7VUQ1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 0E3A7C607D875E1D	FASTA	510	54,070
	10 20 30 40 50 60 MNTTETSRAA APLVLILGLG ETGVAAARWY ARQGSPLRVT DSRAQPGGLA ALQAALADAT 70 80 90 100 110 120 VEYRLGCGEQ FPPDLLDGVA QIVLSPGLVP HESPTRELLE QARERNVEVV GEIELFARAL 130 140 150 160 170 180 AGLAESREYR PRVLAITGTN GKTTVTALTR QLIEAGGMSA RAAGNISPAA LAALMDALDQ 190 200 210 220 230 240 DDLPQVWVLE LSSFQLETTR TLAPDAAVVL NVTQDHLDWH GDMQAYAQAK ARILKPARLA 250 260 270 280 290 300 IVNRDDPLAV AMVESLQALN VRSFGRDVPA LVGDMGLELG QGVAWLTACE SNDFDEPAPA 310 320 330 340 350 360 PRRKKDAPPP TRAGGRMSRL MPVDALRIRG VHNALNALAA MQLARSLDLG WGPMLRTLRD 370 380 390 400 410 420 YAGEPHRAEL VRSIGDVDYI NDSKGTNVGA TVAALEGLGQ QVVLIAGGQG KGQDFSPLVP 430 440 450 460 470 480 VVRRHARAVV LIGVDGAAIG KVLEPTGVPC AAAADMREAV RRAAELAQPG DAVLLSPACA 490 500 510 SFDMFRNYPH RGEVFAAEVR ELALDRGEVA

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640420 Genomic DNA. Translation: CAE43296.1.
RefSeq	NP_881600.1. NC_002929.2.
3D structure databases
ProteinModelPortal	Q7VUQ1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2665873.
GenomeReviews	Gene locus BP3025 in contig BX470248_GR.
KEGG	bpe:BP3025.
NMPDR	fig|257313.1.peg.2673.
PATRIC	21159588. VBIBorPer7866_3271.
Phylogenomic databases
HOGENOM	HBG750024.
OMA	ACASWDM.
PhylomeDB	Q7VUQ1.
ProtClustDB	PRK02006.
Enzyme and pathway databases
BioCyc	BPER257313:BP3025-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_BORPE

Accession

Primary (citable) accession number: Q7VUQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program