Q0RNP3 (Q0RNP3_FRAAA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639
EC=6.3.2.9 HAMAP MF_00639

Alternative name(s):
D-glutamic acid-adding enzyme HAMAP MF_00639
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase HAMAP MF_00639

Gene names

Name:	murD HAMAP MF_00639 EMBL CAJ60843.1
Ordered Locus Names:	FRAAL2194

Organism

Frankia alni (strain ACN14a) [Complete proteome] [HAMAP] EMBL CAJ60843.1

Taxonomic identifier

326424 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Frankiaceae › Frankia

Protein attributes

Sequence length	461 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 SAAS SAAS005762
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanine + glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. HAMAP MF_00639 SAAS SAAS005762
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00639 SAAS SAAS005762
Subcellular location	Cytoplasm By similarity HAMAP MF_00639 SAAS SAAS005762.
Sequence similarities	Belongs to the MurCDEF family. HAMAP MF_00639

Ontologies

Keywords
Biological process	Cell cycle Cell division HAMAP MF_00639 SAAS SAAS005762 Cell shape Cell wall biogenesis/degradation HAMAP MF_00639 SAAS SAAS005762 Peptidoglycan synthesis HAMAP MF_00639 SAAS SAAS005762
Cellular component	Cytoplasm HAMAP MF_00639 SAAS SAAS005762
Ligand	ATP-binding HAMAP MF_00639 SAAS SAAS005762 Nucleotide-binding
Molecular function	Ligase HAMAP MF_00639 SAAS SAAS005762 EMBL CAJ60843.1
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: 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
Regions
	Nucleotide binding	125 – 131	7	ATP By similarity HAMAP MF_00639

Sequences

	Sequence		Length	Mass (Da)
	Q0RNP3 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: FA8326E501061A83	FASTA	461	46,576
	10 20 30 40 50 60 MASPAEPAGP RAWAGLSVLV VGVGVSGLAA ARALLARGAR VRVVDAGDTE RHRAAAADLR 70 80 90 100 110 120 ALGATVVLGG LPAGPGGAGL VVTSPGVPPT APLITGSAAA GVPVWGEVEL AWRWRGATRW 130 140 150 160 170 180 LAVTGTNGKT TTTEMLGAML AAGGRRAITA GNIGTPIVEA VAAEPPYDTL AVELSSFQLH 190 200 210 220 230 240 YTHTVAPLAA AVLNVAPDHL DWHGGAQAYA EAKARIWRDP ATIAIGNADD AASARLLAGA 250 260 270 280 290 300 PGRRVLFGRD PAARPAPGLT VEAGHLVDHA FGGGRLVAVR DLRVTGPHLI SNALAAAALA 310 320 330 340 350 360 RAEGVDPAAI GAALAEFRAG AHRNAEVAVI DGVRWVDDSK ATNPHAAAAS LAGYPSVVWI 370 380 390 400 410 420 AGGLNKGLAF DELVRDARGV LRGAVLIGRC ADEIAVALAR HAPDVPVERA AGMDDAVRAA 430 440 450 460 AALARAGDTV LLAPAAASMD MFRDYAARGD LFAEAVRARE G

References

[1]

"Genome characteristics of facultatively symbiotic Frankia sp. strains reflect host range and host plant biogeography." Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N., Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P., Goltsman E., Huang Y. , Kopp O.R., Labarre L., Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R. Genome Res. 17:7-15(2007) [PubMed: 17151343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CT573213 Genomic DNA. Translation: CAJ60843.1.
RefSeq	YP_712422.1. NC_008278.1.
3D structure databases
ProteinModelPortal	Q0RNP3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0RNP3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4231936.
GenomeReviews	Gene locus FRAAL2194 in contig CT573213_GR.
KEGG	fal:FRAAL2194.
PATRIC	21914100. VBIFraAln347_2007.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0771.
HOGENOM	HBG750024.
OMA	ACASWDM.
ProtClustDB	PRK01438.
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	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

Q0RNP3_FRAAA

Accession

Primary (citable) accession number: Q0RNP3

Entry history

Integrated into UniProtKB/TrEMBL:	September 5, 2006
Last sequence update:	September 5, 2006
Last modified:	December 14, 2011
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)