O67852 (MURD_AQUAE) 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:	aq_2075

Organism

Aquifex aeolicus (strain VF5)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	415 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 – 415	415	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000108957
Regions
	Nucleotide binding	91 – 97	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	O67852 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: B2B8AAF331F3F128	FASTA	415	47,284
	10 20 30 40 50 60 MKFLVWGLGR SGKGALKLLK ERGFEVYAGD DSQNPELWRE VLGEVDTVVL SPGIPPSHPL 70 80 90 100 110 120 WKEALKKEKE VVGELELAYR FFKGKVIAIT GTDGKSTTTR LTYLILKKFF DEVFEAGNIG 130 140 150 160 170 180 KPFSEVVLEN PEGIAVLEVS SFQGKTLKTF RPNIGAFISF SVDHLDWHPS IEDYLKSKYR 190 200 210 220 230 240 IFENQTEEDF LILNDLVYEI KKTPSRARKV LFSELYINSD SVFYKDIRLF NPKNLKIRGL 250 260 270 280 290 300 HNVYNASVAS LIALTLGLKP EDFEEVIYEF RGLPHRLEFL GNFNGVEVYN DSKSTTPHAL 310 320 330 340 350 360 MHALKTFPDN SVILIVGGKD KGADFYSLRH IVQKKVKIAL AIGETKEKIK DSWKDITEVK 370 380 390 400 410 TCNTLEEAVK LAREVSKLGN VVLFSPACSS FDMFRNYEER GEKFKELVEI WFTRT

References

[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000657 Genomic DNA. Translation: AAC07814.1.
PIR	H70477.
RefSeq	NP_214421.1. NC_000918.1.
3D structure databases
ProteinModelPortal	O67852.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1193841.
GenomeReviews	Gene locus aq_2075 in contig AE000657_GR.
KEGG	aae:aq_2075.
NMPDR	fig|224324.1.peg.1436.
PATRIC	20961010. VBIAquAeo85532_1598.
Phylogenomic databases
HOGENOM	HBG750024.
OMA	ACASWDM.
PhylomeDB	O67852.
ProtClustDB	CLSK2299927.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_2075-MONOMER.
Family and domain databases
HAMAP	MF_00639. MurD. Divergent sequence. [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_AQUAE

Accession

Primary (citable) accession number: O67852

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program