Reviewed, UniProtKB/Swiss-Prot Q0VS04 (MURD_ALCBS)

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:	ABO_0596

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	441 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 – 441	441	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000257163
Regions
	Nucleotide binding	113 – 119	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q0VS04-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: C5CDE451C470EE39	FASTA	441	46,537
	10 20 30 40 50 60 MAKDGFDLVI GLGVTGRSVI RYLTDQGMPV RAIDTRAEPV GLDALCADFP DLKVHTGGFK 70 80 90 100 110 120 KGWMGKARRL IVSPGVAVST PAIAEQVVDG KEVIGDIELF ARAASEPLVA ITGSNAKSTV 130 140 150 160 170 180 TTLLGQVADA CGMNPGIGGN LGVPALELLD DQARLYVLEL SSFQLETTYS LSAEVATVLN 190 200 210 220 230 240 VSQDHLDRYA SFADYLAAKQ RVYDGCQVAV WNRDDLATRP PATVARQISF GAHPEADYRL 250 260 270 280 290 300 DSENGQLLCR GEPLLSLSEL ALTGHHNAMN ILSVLAISDA LSLNRDKALA TVKTFTGLPH 310 320 330 340 350 360 RCQLVAESGG VRWFNDSKAT NVGATLAALT GIGESIEGKV ILVAGGLGKG QDFSPLAEPA 370 380 390 400 410 420 RQYLRAALLM GEDRTTVAQG MSAAPCELVA DMAVAVRRAH ALAQPGDAVL LSPACASFDQ 430 440 YSGFAARGDD FTTRAQELCH D

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM286690 Genomic DNA. Translation: CAL16044.1.
RefSeq	YP_692316.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4211242.
GenomeReviews	Gene locus ABO_0596 in contig AM286690_GR.
KEGG	abo:ABO_0596.
NMPDR	fig|393595.12.peg.594.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0VS04.
OMA	Q0VS04. SEDHLDR.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_0596-MON.
Family and domain databases
HAMAP	MF_00639. [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.
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_ALCBS

Accession

Primary (citable) accession number: Q0VS04

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 26 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)