Reviewed, UniProtKB/Swiss-Prot O51532 (MURD_BORBU)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylmuramoylalanine--D-glutamate ligase
    EC=6.3.2.9
Alternative name(s):
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
    D-glutamic acid-adding enzyme

Gene names

Name:	murD
Ordered Locus Names:	BB_0585

Organism

Borrelia burgdorferi (Lyme disease spirochete) [Complete proteome] [HAMAP]

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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 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-acetylmuramoylalanine-D-glutamate ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 451	451	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000108979
Regions
	Nucleotide binding	118 – 124	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	O51532-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: F91D50AA9FA63A90	FASTA	451	51,069
	10 20 30 40 50 60 MLLDEIKNLN FLIMGLGLNG GGVALSRFLL KRGAKLVITD LKSETELALS IDALRDFEDQ 70 80 90 100 110 120 IRYVLGKHDV NDFKNADIVV KNPGVKPNNK YLKFAKRIET DISLFLMFNK NPIVAVTGTK 130 140 150 160 170 180 GKSTLVSLLY QALKEKYPGV KLGGNIGVSP LSFFDQLDGK SPLILELSSW QLQSLENFNP 190 200 210 220 230 240 IISIITNVYN DHQNYYLNFD DYIIDKSKIF VNQTSGIVII QDQAYCKYFS KFKSKVRVIL 250 260 270 280 290 300 FSEFNPCDFD QDIFYCNEGK VYFNDSLIGS FSNSRAVFII PKVITFFVSY YLNIDLNRTG 310 320 330 340 350 360 QILSNFKGIE HRLEFVKSVQ NVMFYNDTAS TIPESTVLSV KSLKTKDNRI NLIVGGTDKE 370 380 390 400 410 420 LDFLSFSKIA DIVRTWILIR GSATVKIIKI LEKSSIQYFL FDSLRDAVNY AFKISSPGDI 430 440 450 VLFSPASASF ELFNNEFDRG LQFKNLVNNL G

References

[1]

"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000783 Genomic DNA. Translation: AAB91522.1.
PIR	H70172.
RefSeq	NP_212719.1.
3D structure databases
HSSP	HSSP built from PDB template 1E0D based on UniProtKB P14900.
ModBase	Search...
Genome annotation databases
GeneID	1195432.
GenomeReviews	Gene locus BB_0585 in contig AE000783_GR.
KEGG	bbu:BB0585.
NMPDR	fig|224326.1.peg.969.
TIGR	BB_0585.
Phylogenomic databases
HOGENOM	O51532.
OMA	VSPLSFF.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0585-MON.
BRENDA	6.3.2.9. 142596.
Family and domain databases
HAMAP	MF_00639. [Tree]
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. 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.
Pfam	PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
TIGRFAMs	TIGR01087. murD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURD_BORBU

Accession

Primary (citable) accession number: O51532

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	June 1, 1998
Last modified:	November 3, 2009
This is version 67 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)