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Q8NQV2 (DDL_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-alanine--D-alanine ligase

EC=6.3.2.4
Alternative name(s):
D-Ala-D-Ala ligase
D-alanylalanine synthetase
Gene names
Name:ddl
Synonyms:ddlA
Ordered Locus Names:Cgl1321, cg1493
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cell wall formation By similarity. HAMAP-Rule MF_00047

Catalytic activity

ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine. HAMAP-Rule MF_00047

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00047

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00047.

Sequence similarities

Belongs to the D-alanine--D-alanine ligase family.

Contains 1 ATP-grasp domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_0000177812

Regions

Domain149 – 353205ATP-grasp
Nucleotide binding176 – 23156ATP By similarity

Sites

Metal binding3081Magnesium or manganese 1 By similarity
Metal binding3201Magnesium or manganese 1 By similarity
Metal binding3201Magnesium or manganese 2 By similarity
Metal binding3221Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8NQV2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 5ACBC3C8D4F95662

FASTA36038,560
        10         20         30         40         50         60 
MSNSNSGKVR VAVVYGGRSS EHSVSCVSAG AIMAHLDPEK YDVIPVGITV DGAWVVGETD 

        70         80         90        100        110        120 
PQKLTLIDRT MPEVEHHEEV RPSLDPAHRG EFHFSDGSLY ATADVIFPVL HGRFGEDGTV 

       130        140        150        160        170        180 
QGLFALSDIP VVGPGVLASA AGMDKEYTKK LMAAEGLPVG REVILRDRTE LTEAEKNLLG 

       190        200        210        220        230        240 
LPVFVKPARG GSSIGISRVT AWEDFNKAVG LARAHDEKVI VESEIVGSEV ECGVLQYPDG 

       250        260        270        280        290        300 
RIVASVPALL SGTESGAGGF YDFDTKYLDN VVTAEIPAPL DEKTTELIQS LAVESFQALA 

       310        320        330        340        350        360 
CEGLARVDFF VTANGPVLNE INTMPGFTPI SMYPQMFTAS GVAYEELLDV LVQQALHRDN 

« Hide

References

[1]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB98714.1.
BX927151 Genomic DNA. Translation: CAF20019.1.
RefSeqNP_600541.1. NC_003450.3.
YP_225605.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NQV2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg1493.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB98714; BAB98714; BAB98714.
CAF20019; CAF20019; cg1493.
GeneID1019297.
3344280.
KEGGcgb:cg1493.
cgl:NCgl1267.
PATRIC21494681. VBICorGlu203724_1291.

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011593.
KOK01921.
OMAMDKIAMK.
OrthoDBEOG64BQ73.
ProtClustDBPRK01966.

Enzyme and pathway databases

UniPathwayUPA00219.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
HAMAPMF_00047. Dala_Dala_lig.
InterProIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR000291. D-Ala_lig_Van_CS.
IPR005905. D_ala_D_ala.
IPR011095. Dala_Dala_lig_C.
IPR011127. Dala_Dala_lig_N.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PANTHERPTHR23132. PTHR23132. 1 hit.
PfamPF07478. Dala_Dala_lig_C. 1 hit.
PF01820. Dala_Dala_lig_N. 1 hit.
[Graphical view]
SUPFAMSSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR01205. D_ala_D_alaTIGR. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS00843. DALA_DALA_LIGASE_1. 1 hit.
PS00844. DALA_DALA_LIGASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDDL_CORGL
AccessionPrimary (citable) accession number: Q8NQV2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: October 1, 2002
Last modified: February 19, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways