Skip Header

Contribute Send feedback
Read comments (?) or add your own

O67216 (DAPA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Dihydrodipicolinate synthase

Short name=DHDPS
EC=4.2.1.52
Gene names
Name:dapA
Ordered Locus Names:aq_1143
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length294 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
Reference 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 – 294294Dihydrodipicolinate synthase HAMAP MF_00418
PRO_0000103081

Regions

Region47 – 482Pyruvate binding By similarity

Sites

Active site1611Schiff-base intermediate with substrate By similarity
Binding site1051Pyruvate By similarity
Site1321Involved in proton transfer during cleavage By similarity

Secondary structure

............................................... 294
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O67216 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 0778B824E6619E31

FASTA29432,670
        10         20         30         40         50         60 
MFQGSIVALI TPFKEGEVDY EALGNLIEFH VDNGTDAILV CGTTGESPTL TFEEHEKVIE 

        70         80         90        100        110        120 
FAVKRAAGRI KVIAGTGGNA THEAVHLTAH AKEVGADGAL VVVPYYNKPT QRGLYEHFKT 

       130        140        150        160        170        180 
VAQEVDIPII IYNIPSRTCV EISVDTMFKL ASECENIVAS KESTPNMDRI SEIVKRLGES 

       190        200        210        220        230        240 
FSVLSGDDSL TLPMMALGAK GVISVANNVM PREVKELIRA ALEGDFRRAR EIHYYLHDLF 

       250        260        270        280        290 
KVLFIETNPI PVKTACWMLG MCEKEFRLPL TEMSPENENK LREVLKKYNL PLKN 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07169.1.
PIRE70398.
RefSeqNP_213780.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EHHX-ray1.90A/C/D/E1-294[»]
ProteinModelPortalO67216.
SMRO67216. Positions 1-294.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1192562.
GenomeReviewsGene locus aq_1143 in contig AE000657_GR.
KEGGaae:aq_1143.
NMPDRfig|224324.1.peg.795.
PATRIC20959542. VBIAquAeo85532_0891.

Phylogenomic databases

HOGENOMHBG358848.
OMAFMLCGGH.
PhylomeDBO67216.
ProtClustDBPRK03170.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1143-MONOMER.

Family and domain databases

HAMAPMF_00418. DapA.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR002220. Dihydrodipicolinate_synth-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR020624. Dihydrodipicolinate_synth_CS.
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. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPA_AQUAE
AccessionPrimary (citable) accession number: O67216
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 78 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