Q6M3S0 (Q6M3S0_CORGL) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
UDP-N-acetylmuramoylalanine--D-glutamate ligase RuleBase RU003664
EC=6.3.2.9 RuleBase RU003664

Gene names

Name:	murD EMBL CAF20500.1
Ordered Locus Names:	cg2371

Organism

Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	472 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. RuleBase RU003664 SAAS SAAS005762
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanine + glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate. RuleBase RU003664 SAAS SAAS005762
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. RuleBase RU003664 SAAS SAAS005762
Subcellular location	Cytoplasm By similarity RuleBase RU003664 SAAS SAAS005762.
Sequence similarities	Belongs to the MurCDEF family. RuleBase RU003630

Ontologies

Keywords
Biological process	Cell cycle Cell division RuleBase RU003664 SAAS SAAS005762 Cell shape Cell wall biogenesis/degradation RuleBase RU003664 SAAS SAAS005762 Peptidoglycan synthesis RuleBase RU003664 SAAS SAAS005762
Cellular component	Cytoplasm SAAS SAAS005762
Ligand	ATP-binding RuleBase RU003630 SAAS SAAS005762 Nucleotide-binding
Molecular function	Ligase RuleBase RU003630 SAAS SAAS005762 EMBL CAF20500.1
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: 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...

Sequences

	Sequence		Length	Mass (Da)
	Q6M3S0 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 8490990EABD06713	FASTA	472	49,303
	10 20 30 40 50 60 MVSLSHLPQA LQGRILVAGA GVSGLSIAKM LSELHCDVVV ADDNETARHM LIEVVDVADI 70 80 90 100 110 120 STAQAQEQLD SFSIVVTSPG WRPTSTLLVD AHRQGLEVIG DVELAWRLDQ AGVFGEPHTW 130 140 150 160 170 180 LAVTGTNGKT TTTSMLAAMM NEGGFTAKAV GNIGIPVSEA LVAKNRIDVL VAELSSFQLH 190 200 210 220 230 240 WSPTFTPDAG VVLNLAEDHI DWHGSMRDYA LAKMEVLKGK VAIIGADDPY LVQLTSEADL 250 260 270 280 290 300 SGLIGFTVNE PATGQLGVKA GELVDNAYGN NVVLASADGI NPAGPAGVLD ALAAAAVARS 310 320 330 340 350 360 QGVAPEAIAR ALDSFEVAGH RGQVVAEHDG VHFIDNSKAT NPHAADSALA GHDSVIWVVG 370 380 390 400 410 420 GQLKGADIAP LVKKHEQRIK AALVLGADRA EIVAALKEHA SQASVFVTDK TEPFEAMEEI 430 440 450 460 470 VTEAFSISEP GDTVLLAPAA ASLDMFKGMG QRGDLFAHNI IGTIKGLTEE KG

References

[1]

"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 [Kalinowski].

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX927154 Genomic DNA. Translation: CAF20500.1.
RefSeq	NP_601362.1. NC_003450.3. YP_226401.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q6M3S0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1020112. 3342625.
GenomeReviews	Gene locus cg2371 in contig BX927147_GR.
KEGG	cgb:cg2371.
PATRIC	21496324. VBICorGlu203724_2098.
Organism-specific databases
CMR	Search...
Phylogenomic databases
PhylomeDB	Q6M3S0.
ProtClustDB	PRK00141.
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

Q6M3S0_CORGL

Accession

Primary (citable) accession number: Q6M3S0

Entry history

Integrated into UniProtKB/TrEMBL:	July 5, 2004
Last sequence update:	July 5, 2004
Last modified:	December 14, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)