A8FCX9 (MURD_BACP2) 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:	BPUM_1413

Organism

Bacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]

Taxonomic identifier

315750 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	451 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 – 451	451	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_1000061451
Regions
	Nucleotide binding	120 – 126	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	A8FCX9 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: B68B57044C9269BC	FASTA	451	50,169
	10 20 30 40 50 60 MNKMQMLKNE HVLVLGLAKS GYAAASILHE HGVNVTVNDQ KPFEENEPAQ LLSEKGIDVV 70 80 90 100 110 120 CGSHPLRIFE DKDITILIKN PGIPYENVMV QEALRRQIPV WTEIELAYHL TSSPFIGITG 130 140 150 160 170 180 SNGKTTTTTL IYEMLKKDSQ KTLVAGNIGT VASEVAANAD GDEWIVTELS SFQLMGTVEF 190 200 210 220 230 240 RPKISLILNI FDAHLDYHHT REEYEKAKQK VFVHQHEDDI AVINLDDPSV VKLAEGSKAK 250 260 270 280 290 300 KVFFSVKEPV EHGAFIQHGA IYYMNEHIID VKDVVLPGEH NQENILAAIC VVKNAGCSND 310 320 330 340 350 360 AIVHVLTTFG GVKHRLQFVD TIQSRKFYND SKATNILATS KALSAFEQPT ILLAGGLDRG 370 380 390 400 410 420 NEFDELKPFM KHVKGMITFG ETAPKFVKLG EELGIHHVKH VDNVEQAVPA AFNISEEEDV 430 440 450 ILLSPACASW DQHKTFEERG DMFVNAVHML K

References

[1]

"Paradoxical DNA repair and peroxide resistance gene conservation in Bacillus pumilus SAFR-032." Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C. , Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., Weinstock G.M. PLoS ONE 2:E928-E928(2007) [PubMed: 17895969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SAFR-032.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000813 Genomic DNA. Translation: ABV62096.1.
RefSeq	YP_001486656.1. NC_009848.1.
3D structure databases
ProteinModelPortal	A8FCX9.
ModBase	Search...
Protein-protein interaction databases
STRING	A8FCX9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000064012; EBBACP00000062345; EBBACG00000064003.
GeneID	5620680.
GenomeReviews	Gene locus BPUM_1413 in contig CP000813_GR.
KEGG	bpu:BPUM_1413.
PATRIC	18966661. VBIBacPum16546_1427.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0771.
GeneTree	EBGT00070000032130.
HOGENOM	HBG750024.
OMA	ACASWDM.
ProtClustDB	PRK02472.
Enzyme and pathway databases
BioCyc	BPUM315750:BPUM_1413-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_BACP2

Accession

Primary (citable) accession number: A8FCX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 13, 2007
Last modified:	January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program