Q1LSW4 (MURD_BAUCH) 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:	BCI_0520

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	446 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 – 446	446	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000257166
Regions
	Nucleotide binding	112 – 118	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q1LSW4 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: 165EEC1D7FFE2590	FASTA	446	49,108
	10 20 30 40 50 60 MTNYYGHNIV IIGLGITGIT CVNFFRSRGI TPRVMDTRYN PPQLNQLPKD IQYWLGELKI 70 80 90 100 110 120 EWLLAATLIV ISPGISLSHP AINTAMKCGI EIIGDVELFL REVTVPVVAI TGTNGKSTVA 130 140 150 160 170 180 KLVGTMANCA GLKVGVGGNI GYPVLSLLQQ SHQLYVLELS SFQLETTKNL KVAVATILNI 190 200 210 220 230 240 SEDHMDRYPL GLQQYREAKL KIYKQAKIYI INDDDKLTLP ANSTNKEYCS IIKFGIKSGH 250 260 270 280 290 300 YCLGDYQGKQ WLMAYGKPLL DCNEIKIIGR HNLLNALAAL ALAEAIAIPR QACLIALRQF 310 320 330 340 350 360 SGLMHRFELV LERKGIRWIN DSKATNVGST KAALNELTVD GTLHLLLGGD GKLADFSSLQ 370 380 390 400 410 420 PFVQGNNIHL YCFGKDSKKL AALNQHSATI TQTLSQAMHI INNQVKAGDV VLLSPACSSL 430 440 DQFENFKVRG KTFTNLVFEF NDGNNN

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000238 Genomic DNA. Translation: ABF14267.1.
RefSeq	YP_588950.1. NC_007984.1.
3D structure databases
ProteinModelPortal	Q1LSW4.
SMR	Q1LSW4. Positions 3-440.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LSW4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4056451.
GenomeReviews	Gene locus BCI_0520 in contig CP000238_GR.
KEGG	bci:BCI_0520.
PATRIC	21074549. VBIBauCic75062_0492.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0771.
HOGENOM	HBG750024.
OMA	ACASWDM.
PhylomeDB	Q1LSW4.
Enzyme and pathway databases
BioCyc	BCIC186490:BCI_0520-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_BAUCH

Accession

Primary (citable) accession number: Q1LSW4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	May 30, 2006
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program