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Q0I1D1 (DDL_HISS1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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
Ordered Locus Names:HS_0360
OrganismHistophilus somni (strain 129Pt) (Haemophilus somnus) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length308 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 – 308308D-alanine--D-alanine ligase HAMAP-Rule MF_00047
PRO_1000030453

Regions

Domain106 – 305200ATP-grasp
Nucleotide binding136 – 19156ATP By similarity

Sites

Metal binding2591Magnesium or manganese 1 By similarity
Metal binding2721Magnesium or manganese 1 By similarity
Metal binding2721Magnesium or manganese 2 By similarity
Metal binding2741Magnesium or manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0I1D1 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: E3949E66A501D084

FASTA30833,892
        10         20         30         40         50         60 
MAKPLKQQKI AVLLGGTSAE REVSLNSGNA VLTALRNQGF DAHPIDPKEY PVAMLKEQGF 

        70         80         90        100        110        120 
DRVFNILHGR GGEDGTIQGL LEQIGLPYTG CGVMASALTM DKMRTKMLWK AFGLPVADME 

       130        140        150        160        170        180 
VVTRTSFSQL NPQVVVEKLG LPLMVKPSLE GSSVGLTKVN AIDDLKSAVE FALQYDETVL 

       190        200        210        220        230        240 
IEEWLSGDEL TVPILGNEVL PSIKIVPQGE FYDYEAKYIA DNTQYFCPSG LTEEREQELR 

       250        260        270        280        290        300 
QLVKQAYDVV GCRGWSRIDV MLDGEGKFRL VEVNTNPGMT SHSLFPKSAA TVGYSFEQLV 


VKILELSL 

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI24638.1.
RefSeqYP_718570.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I1D1.
SMRQ0I1D1. Positions 9-307.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205914.HS_0360.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI24638; ABI24638; HS_0360.
GeneID4239836.
KEGGhso:HS_0360.
PATRIC20280657. VBIHaeSom53361_0378.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1181.
HOGENOMHOG000011592.
KOK01921.
OrthoDBEOG6ND0KB.

Enzyme and pathway databases

BioCycHSOM205914:GJ7V-377-MONOMER.
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. 2 hits.
[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_HISS1
AccessionPrimary (citable) accession number: Q0I1D1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 64 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