Q1IKG8 (MURD_KORVE) 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:	Acid345_3631

Organism

Koribacter versatilis (strain Ellin345)

Taxonomic identifier

204669 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Candidatus Koribacter

Protein attributes

Sequence length	453 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 – 453	453	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_0000257162
Regions
	Nucleotide binding	115 – 121	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q1IKG8 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: A04BB7B046C81FFD	FASTA	453	49,582
	10 20 30 40 50 60 MDVRGKRVLV VGLGKSGIAS ATFLQAQGAK VTVSDSKSEA QLRQEIPLLL DKGITVETGH 70 80 90 100 110 120 HGERTFRDQD LIVISPGVPF DQPQLEQARK QGIPVIGEIE LAAQFVPGHV IAITGSNGKT 130 140 150 160 170 180 TTTSLCGDIL QSGGKKTLVG GNIGTPAISF AQLANDDTWS VLEISSFQLE TIERFRPEIA 190 200 210 220 230 240 AILNITPDHL DRHGTFEKYA AAKERIFENQ REHDFAILNA DNEPCVEIAK RVKSQVLWFS 250 260 270 280 290 300 RQHEVKHGTF VREDKIYFRD PKGEREIMPV ADMLLKGAHN VENVLAAVCV GVAASVAPEQ 310 320 330 340 350 360 IRKAVSQFKA VEHRLEYTAT VKGVDYYNDS KATNVDATIK ALESFSKGVH LILGGKDKGS 370 380 390 400 410 420 PYTVLNDLLH ERAKTVYTIG AAAAKIEAEV KGVEVVHAET LENAVKLASQ KAVKGDVVLL 430 440 450 APACASFDQF QSYEHRGRIF KELVRKMAEQ EKK

References

[1]

"Three genomes from the phylum Acidobacteria provide insight into the lifestyles of these microorganisms in soils." Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., Davidsen T.M. , DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R. Appl. Environ. Microbiol. 75:2046-2056(2009) [PubMed: 19201974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ellin345.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000360 Genomic DNA. Translation: ABF42632.1.
RefSeq	YP_592706.1. NC_008009.1.
3D structure databases
ProteinModelPortal	Q1IKG8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1IKG8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4070151.
GenomeReviews	Gene locus Acid345_3631 in contig CP000360_GR.
KEGG	aba:Acid345_3631.
NMPDR	fig|204669.6.peg.3636.
PATRIC	31984492. VBICanKor57425_3876.
Phylogenomic databases
eggNOG	COG0771.
HOGENOM	HBG750024.
OMA	ACASWDM.
PhylomeDB	Q1IKG8.
ProtClustDB	CLSK775010.
Enzyme and pathway databases
BioCyc	ABAC204669:ACID345_3631-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_KORVE

Accession

Primary (citable) accession number: Q1IKG8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	June 13, 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