Q9WY76 (MURD_THEMA) 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:	TM_0234

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	430 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 430	430	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000109113
Regions
	Nucleotide binding	109 – 115	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9WY76 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 491D71CE4201B2C8	FASTA	430	49,154
	10 20 30 40 50 60 MKIGFLGFGK SNRSLLKYLL NHQEAKFFVS EAKTLDGETK KFLEEHSVEY EEGGHTEKLL 70 80 90 100 110 120 DCDVVYVSPG IKPDTSMIEL LSSRGVKLST ELQFFLDNVD PKKVVGITGT DGKSTATALM 130 140 150 160 170 180 YHVLSGRGFK TFLGGNFGTP AVEALEGEYD YYVLEMSSFQ LFWSERPYLS NFLVLNISED 190 200 210 220 230 240 HLDWHSSFKE YVDSKLKPAF LQTEGDLFVY NKHIERLRNL EGVRSRKIPF WTDENFATEK 250 260 270 280 290 300 ELIVRGKKYT LPGNYPYQMR ENILAVSVLY MEMFNELESF LELLRDFKPL PHRMEYLGQI 310 320 330 340 350 360 DGRHFYNDSK ATSTHAVLGA LSNFDKVVLI MCGIGKKENY SLFVEKASPK LKHLIMFGEI 370 380 390 400 410 420 SKELAPFVGK IPHSIVENME EAFEKAMEVS EKGDVILLSP GGASFDMYEN YAKRGEHFRE 430 IFKRHGGDEV

References

[1]

"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000512 Genomic DNA. Translation: AAD35325.1.
PIR	D72402.
RefSeq	NP_228048.1. NC_000853.1.
3D structure databases
ProteinModelPortal	Q9WY76.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	897133.
GenomeReviews	Gene locus TM_0234 in contig AE000512_GR.
KEGG	tma:TM0234.
NMPDR	fig|243274.1.peg.232.
PATRIC	23935343. VBITheMar51294_0237.
TIGR	TM_0234.
Phylogenomic databases
HOGENOM	HBG750024.
OMA	LERHKTL.
PhylomeDB	Q9WY76.
ProtClustDB	CLSK875042.
Enzyme and pathway databases
BioCyc	TMAR243274:TM_0234-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	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_THEMA

Accession

Primary (citable) accession number: Q9WY76

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program