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B3PC19 (DAPA_CELJU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:
Dihydrodipicolinate synthase

Short name=DHDPS
EC=4.2.1.52
Gene names
Name:dapA
Ordered Locus Names:CJA_2830
OrganismCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) [Complete proteome] [HAMAP]
Taxonomic identifier498211 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 termComplete 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 – 290290Dihydrodipicolinate synthase HAMAP MF_00418
PRO_1000124020

Regions

Region48 – 492Pyruvate binding By similarity

Sites

Active site1611Schiff-base intermediate with substrate By similarity
Binding site1061Pyruvate By similarity
Site1331Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
B3PC19 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 3A041138AC9F2CA5

FASTA29030,994
        10         20         30         40         50         60 
MIQGSMVALV TPMHADNTLD WDSLHKLVDW HLEQGTHAIV AVGTTGESAT LDVQEHLQVI 

        70         80         90        100        110        120 
KRVVDQVNGR IPVIAGTGAN STSEAVELTQ AAKDVGADAC LLVTPYYNKP TQEGLFLHHE 

       130        140        150        160        170        180 
YIANAVAIPQ YLYNVPGRTG VDMKPETALR LAQVPNIAGI KEATGDLERA RLLIDQAPPG 

       190        200        210        220        230        240 
FAIISGDDAT AVELILLGGQ GDISVTANVV PAAIARMCEL ALAGKAEEAR TINTQLLPLH 

       250        260        270        280        290 
TAMFVESNPI PVKWAVEQLG LIQSGIRLPL TRLSAQYHQQ VKTAMQLAGL 

« Hide

References

[1]"Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
J. Bacteriol. 190:5455-5463(2008) [PubMed: 18556790] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ueda107.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000934 Genomic DNA. Translation: ACE83136.1.
RefSeqYP_001983289.1. NC_010995.1.

3D structure databases

ProteinModelPortalB3PC19.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3PC19.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6416131.
GenomeReviewsGene locus CJA_2830 in contig CP000934_GR.
KEGGcja:CJA_2830.
PATRIC21329056. VBICelJap122165_2796.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG358848.
OMAFMLCGGH.
ProtClustDBPRK03170.

Enzyme and pathway databases

BioCycCJAP155077:CJA_2830-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_CELJU
AccessionPrimary (citable) accession number: B3PC19
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: January 25, 2012
This is version 27 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

SIMILARITY comments

Index of protein domains and families