Q8K9T2 (MURD_BUCAP) 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:	BUsg_212

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	440 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 – 440	440	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000108986
Regions
	Nucleotide binding	113 – 119	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8K9T2 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: DD9C28B6B8E8974E	FASTA	440	49,855
	10 20 30 40 50 60 MSYNYFGKKI LILGLGLTGI SCINFFLKKG IQPRVIDESN KPIFLNKIPK NIEYKLGNLK 70 80 90 100 110 120 ENWILESDLI IISPGISSFK PILMKARSLG IDIISDIELF SRETKCPIIS ITGTNGKSTV 130 140 150 160 170 180 ATMVKKIAEK SGYKVLLGGN IGFPVLEMLN KKASLYVLEL SSFQLETTFN LKSKIAVVLN 190 200 210 220 230 240 ITEDHLDRYP EGFEQYKKTK LSIYNKAKIC LIKLKKGEKK PFNTKSKKYI SFGTCNNNDY 250 260 270 280 290 300 YINYEKEKAI LFHKNKKIVD TSNILLNGHH NYENILTSLA ISDQMKFDQK VSINVLKKFL 310 320 330 340 350 360 GLPHRFQTVH INNNISWIND SKSTNVDSTK AALKNLKIKG TIWLLLGGDG KSSNFNILKK 370 380 390 400 410 420 YFEKIKIKIY CFGKDGLNLS KLCKKKSIYT KTLKQAIILI SKKIQPGDVV LLSPGCSSKD 430 440 QFSNFEERGN LFIKLSKEIN

References

[1]	"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM67775.1.
RefSeq	NP_660564.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8K9T2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000000148; EBBUCP00000000148; EBBUCG00000000148.
GeneID	1005411.
GenomeReviews	Gene locus BUsg_212 in contig AE013218_GR.
KEGG	bas:BUsg212.
PATRIC	21247213. VBIBucAph100086_0220.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000007738.
HOGENOM	HBG750024.
OMA	DQFSSYK.
ProtClustDB	PRK03806.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG212-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_BUCAP

Accession

Primary (citable) accession number: Q8K9T2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program