Reviewed, UniProtKB/Swiss-Prot Q2IG29 (MURD_ANADE)

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:	Adeh_3769

Organism

Anaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]

Taxonomic identifier

290397 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

Protein attributes

Sequence length	462 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 – 462	462	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000257165
Regions
	Nucleotide binding	118 – 124	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q2IG29-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 0F78BB8BB8EB59A6	FASTA	462	48,010
	10 20 30 40 50 60 MAAPELKGTR VTVVGLAKSG VAAARLCARE GARVTVTDRR GEAALGGALA ALPASVTRRL 70 80 90 100 110 120 GGHDAADFTG ADLVVASPGV PLANPEIQAA RRRGVPVWGE VELAARFLGG LPIVGITGTN 130 140 150 160 170 180 GKSTTTALTG ALLARHRRTF VGGNLGTPLS ELVLSGEPAA AAVVELSSFQ LEGIERFRAR 190 200 210 220 230 240 VAAVLNVTPD HLDRYPDVDA YAAAKARLFA TQEPDDVAVA NARDPRALAM AGASRGDLHT 250 260 270 280 290 300 FGFGAPVPAS ARDEGGEPGP GGTAIWYTPR GRAPERYQLH NRALRGRHNR ENAMAAVLCA 310 320 330 340 350 360 RLMGVPGEAV QAGLDAFPGL HHRLELVAEG RGVEWVNDSK ATNVDSTFVG LAAFPAGAPR 370 380 390 400 410 420 VVLIMGGRGK KAPYAPLRPL FGGRVKALLT IGEDAPAIER ELGDLAPTEP CGDLPGAVRR 430 440 450 460 AAVLSGPGDV VLLSPACASY DQFASYEERG EAFRRLATEQ AR

References

[1]

"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000251 Genomic DNA. Translation: ABC83535.1.
RefSeq	YP_466972.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3886505.
GenomeReviews	Gene locus Adeh_3769 in contig CP000251_GR.
KEGG	ade:Adeh_3769.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2IG29.
OMA	Q2IG29. SEDHLDR.
Enzyme and pathway databases
BioCyc	ADEH290397:ADEH_3769-MON.
Family and domain databases
HAMAP	MF_00639. [Tree]
InterPro	IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. 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	PF01225. Mur_ligase. 1 hit. 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_ANADE

Accession

Primary (citable) accession number: Q2IG29

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	March 7, 2006
Last modified:	June 16, 2009
This is version 28 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)