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Q5HG25 (DAPA_STAAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydrodipicolinate synthase
Short name=DHDPS
EC=4.2.1.52
Gene names
Name:dapA
Ordered Locus Names:SACOL1430
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2 H2O. HAMAP MF_00418

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. HAMAP MF_00418

Subunit structure

Homotetramer By similarity. HAMAP MF_00418

Subcellular location

Cytoplasm By similarity HAMAP MF_00418.

Sequence similarities

Belongs to the DHDPS family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Diaminopimelate biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processdiaminopimelate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydrodipicolinate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Dihydrodipicolinate synthase HAMAP MF_00418
PRO_0000103154

Regions

Region50 – 512Pyruvate binding By similarity

Sites

Active site1631Schiff-base intermediate with substrate By similarity
Binding site1081Pyruvate By similarity
Site1351Involved in proton transfer during cleavage By similarity

Secondary structure

1 ............................................. 295
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5HG25 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 6ED1E5887F0C2C01

FASTA29532,584
        10         20         30         40         50         60 
MTHLFEGVGV ALTTPFTNNK VNIEALKTHV NFLLENNAQA IIVNGTTAES PTLTTDEKER 

        70         80         90        100        110        120 
ILKTVIDLVD KRVPVIAGTG TNDTEKSIQA SIQAKALGAD AIMLITPYYN KTNQRGLVKH 

       130        140        150        160        170        180 
FEAIADAVKL PVVLYNVPSR TNMTIEPETV EILSQHPYIV ALKDATNDFE YLEEVKKRID 

       190        200        210        220        230        240 
TNSFALYSGN DDNVVEYYQR GGQGVISVIA NVIPKEFQAL YDAQQSGLDI QDQFKPIGTL 

       250        260        270        280        290 
LSALSVDINP IPIKALTSYL GFGNYELRLP LVSLEDTDTK VLRETYDTFK AGENE

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: COL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000046 Genomic DNA. Translation: AAW38175.1.
RefSeqYP_186282.1. NC_002951.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DI0X-ray2.38A/B1-295[»]
3DI1X-ray2.20A/B1-295[»]
ProteinModelPortalQ5HG25.
SMRQ5HG25. Positions 2-293.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HG25.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000009025; EBSTAP00000008760; EBSTAG00000009024.
GeneID3236210.
GenomeReviewsGene locus SACOL1430 in contig CP000046_GR.
KEGGsac:SACOL1430.
PATRIC19529075. VBIStaAur112458_1391.
TIGRSACOL1430.

Phylogenomic databases

eggNOGCOG0329.
GeneTreeEBGT00050000024245.
HOGENOMHBG358848.
OMACEMEDSN.
PhylomeDBQ5HG25.
ProtClustDBPRK03170.

Enzyme and pathway databases

BioCycSAUR93062:SACOL1430-MONOMER.

Family and domain databases

HAMAPMF_00418. DapA.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR002220. Dihydrodipicolinate_synth-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR005263. Dihydrodipicolinate_synth_DapA.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK01714.
PANTHERPTHR12128. DHDPS. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFPIRSF001365. DHDPS. 1 hit.
PRINTSPR00146. DHPICSNTHASE.
TIGRFAMsTIGR00674. DapA. 1 hit.
PROSITEPS00665. DHDPS_1. False negative.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPA_STAAC
AccessionPrimary (citable) accession number: Q5HG25
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 15, 2005
Last modified: January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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