Reviewed, UniProtKB/Swiss-Prot B0C915 (MURD_ACAM1)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylmuramoylalanine--D-glutamate ligase
    EC=6.3.2.9
Alternative name(s):
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
    D-glutamic acid-adding enzyme

Gene names

Name:	murD
Ordered Locus Names:	AM1_1525

Organism

Acaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]

Taxonomic identifier

329726 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Acaryochloris

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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 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
Molecule processing
	Chain	1 – 461	461	UDP-N-acetylmuramoylalanine--D-glutamate ligase HAMAP MF_00639		PRO_1000082675
Regions
	Nucleotide binding	118 – 124	7	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	B0C915-1 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: A7F9BD8FA96EBF8E	FASTA	461	49,514
	10 20 30 40 50 60 MPAVHIIGLG RSGIAAARLL RREGWQVSVG DAGHSEGLVA TQKTLAAEGI PVHLNLKFSL 70 80 90 100 110 120 SALAELSLDR PDRIVVSPGV PWQLPALEEA RSQGIETFGE LELAWRSLKQ YPWVGITGTN 130 140 150 160 170 180 GKTTTTAIVE AIFKAAGLRA PACGNIGYSA CELALAGDPL DWVIAEVSSY QIESSPTLAP 190 200 210 220 230 240 TIGVWTTFSP DHLERHGTVE CYREIKALLL NQSKQKILNG DDQGLIKGLP WRWADAYWTS 250 260 270 280 290 300 SHGPSLPDAC NGQRCPVPNI FIEEGWVKVE GEPIVQVSSM RMLGVHNQQN LLLAVAVAHL 310 320 330 340 350 360 AGIGKDAIAT AVSTFPGVAH RLEHICTWQG VDFINDSKAT NYEAAQTGLA AVNSPAILIA 370 380 390 400 410 420 GGEAKVGDDQ AWLQTIQAQA AKVLLIGSAA GAFSQRLKAI GYDDYEIVDT MNKAVTRAAE 430 440 450 460 LAPSLQAKSV LLSPACASFD QYQNFERRGD HFRQLCQDLS Q

References

[1]

"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina." Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W. Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000828 Genomic DNA. Translation: ABW26550.1.
RefSeq	YP_001515864.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5680345.
GenomeReviews	Gene locus AM1_1525 in contig CP000828_GR.
KEGG	amr:AM1_1525.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	B0C915. SEDHLDR.
Family and domain databases
HAMAP	MF_00639. [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.
Pfam	PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
TIGRFAMs	TIGR01087. murD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURD_ACAM1

Accession

Primary (citable) accession number: B0C915

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 26, 2008
Last modified:	June 16, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)