Q67QM7 (MURD_SYMTH) 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:	STH1031

Organism

Symbiobacterium thermophilum [Complete proteome] [HAMAP]

Taxonomic identifier

2734 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiales Family XVIII. Incertae Sedis › Symbiobacterium

Protein attributes

Sequence length	455 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 – 455	455	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000109107
Regions
	Nucleotide binding	117 – 123	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q67QM7 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: AC9D2DC65CA0668B	FASTA	455	48,635
	10 20 30 40 50 60 MAGVKLQERA AVVGIGISNM ALIRYLVARG VRVTACDRTS AEKLGERAAE LARLGVPLVA 70 80 90 100 110 120 GEGYLEPLAD HDLIFLTPGM PKHLPEIEAA RRRGAAISGE IGLVLDLCRA PVIGVTGSAG 130 140 150 160 170 180 KTTTTTLIGE ILRAAGRETY VGGNIGKPLI EQVEAIPSEA VVVLELSSFQ LQLVHRSPHI 190 200 210 220 230 240 AVVTNVSPNH LDVHATMEEY VEAKKAIFRR QSPADWLVLN ADDPTVRAFA AEARSRVVLF 250 260 270 280 290 300 SRRADPGGRD AAFVREDRVI WRRGGRETPI LFLDEIRLPG LHNQENVLAA VAACFLAGAP 310 320 330 340 350 360 LSAVREVVTQ FTGVEHRIEP VRVLDGVKWY NDSKATSPAE AVAALTTLPA PIVLIAGGSD 370 380 390 400 410 420 KGIPFDPIAP LVAEKVKTLI LMGPTAPKIE EAVRRGGYAG PIRRAADMAE AVALAREAAA 430 440 450 PGDTVLLSPA CASFDAYRNF EERGRHFKSL VEALS

References

[1]

"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism." Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T. Nucleic Acids Res. 32:4937-4944(2004) [PubMed: 15383646] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: T / IAM 14863.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP006840 Genomic DNA. Translation: BAD40016.1.
RefSeq	YP_074860.1. NC_006177.1.
3D structure databases
ProteinModelPortal	Q67QM7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2981649.
GenomeReviews	Gene locus STH1031 in contig AP006840_GR.
KEGG	sth:STH1031.
NMPDR	fig|292459.1.peg.987.
PATRIC	23780202. VBISymThe116959_1030.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG750024.
OMA	ACASWDM.
ProtClustDB	PRK01710.
Enzyme and pathway databases
BioCyc	STHE292459:STH1031-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_SYMTH

Accession

Primary (citable) accession number: Q67QM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program