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P63948 (DAPA_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:
4-hydroxy-tetrahydrodipicolinate synthase

Short name=HTPA synthase
EC=4.3.3.7
Gene names
Name:dapA
Ordered Locus Names:SA1227
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) By similarity. HAMAP-Rule MF_00418

Catalytic activity

Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O. HAMAP-Rule MF_00418

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00418

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00418.

Sequence similarities

Belongs to the DapA family.

Caution

Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Diaminopimelate biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processdiaminopimelate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lysine biosynthetic process via diaminopimelate

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-hydroxy-tetrahydrodipicolinate synthase

Inferred from electronic annotation. Source: UniProtKB-EC

amine-lyase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2952954-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418
PRO_0000103156

Sites

Active site1351Proton donor/acceptor By similarity
Active site1631Schiff-base intermediate with substrate By similarity
Binding site471Pyruvate By similarity
Binding site2061Pyruvate; via carbonyl oxygen By similarity
Site461Part of a proton relay during catalysis By similarity
Site1091Part of a proton relay during catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
P63948 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: EAD1E6DD4CE05A17

FASTA29532,660
        10         20         30         40         50         60 
MTHLFEGVGV ALTTPFTNNK VNLEALKAHV NFLLENNAQA IIVNGTTAES PTLTTDEKER 

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

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

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

       250        260        270        280        290 
LSALSVDINP IPIKALTSYL EFGNYELRLP LVSLEDTDTK VLREAYDTFK AGENE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000018 Genomic DNA. Translation: BAB42487.1.
PIRC89916.
RefSeqNP_374508.1. NC_002745.2.

3D structure databases

ProteinModelPortalP63948.
SMRP63948. Positions 2-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING158879.SA1227.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB42487; BAB42487; BAB42487.
GeneID1124066.
KEGGsau:SA1227.
PATRIC19574704. VBIStaAur116463_1321.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHOG000173604.
KOK01714.
OMATHKEHMR.
OrthoDBEOG6W7235.
ProtClustDBPRK03170.

Enzyme and pathway databases

BioCycSAUR158879:GJCB-1294-MONOMER.
UniPathwayUPA00034; UER00017.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00418. DapA.
InterProIPR013785. Aldolase_TIM.
IPR005263. DapA.
IPR002220. DapA-like.
IPR020625. Dihydrodipicolinate_synth_AS.
[Graphical view]
PANTHERPTHR12128. PTHR12128. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFPIRSF001365. DHDPS. 1 hit.
PRINTSPR00146. DHPICSNTHASE.
TIGRFAMsTIGR00674. dapA. 1 hit.
PROSITEPS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPA_STAAN
AccessionPrimary (citable) accession number: P63948
Secondary accession number(s): Q99U89
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: February 19, 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