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P24847 (DAPA2_WHEAT) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 69. 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 2, chloroplastic

Short name=DHDPS 2
EC=4.2.1.52
OrganismTriticum aestivum (Wheat)
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

Sensitive to lysine inhibition. This inhibition increase in an allosteric manner with increasing concentration of the inhibitor.

Pathway

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

Subunit structure

Tetramer of modified subunits derived from two genes in different combinations.

Subcellular location

Plastidchloroplast.

Sequence similarities

Belongs to the DHDPS family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Diaminopimelate biosynthesis
Lysine biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandSchiff base
   Molecular functionLyase
   Technical termAllosteric enzyme
Direct protein sequencing
Gene Ontology (GO)
   Biological processdiaminopimelate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

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

Transit peptide1 – 5151Chloroplast Ref.1
Chain52 – 377326Dihydrodipicolinate synthase 2, chloroplastic
PRO_0000007204

Sites

Active site2341Schiff-base intermediate with substrate By similarity
Binding site1811Pyruvate By similarity
Site2061Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
P24847 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: B0C08FC482BA6CDC

FASTA37740,876
        10         20         30         40         50         60 
MMAAQPTANP GVRLGWKAPG ALASPPRLAL SRSAAAPLAS HRVGRGKFSA AAITTDDYLP 

        70         80         90        100        110        120 
MRSTEVKNRT SVDGIKSLRL ITAVKTPYLP DGRFDLEAYD SLINTQINGG AEGVIVGGTT 

       130        140        150        160        170        180 
GEGHLMSWDE HIMLIGHTVN CFGTNIKVIG NTGSNSTREA IHASEQGFAV GMHAALHVNP 

       190        200        210        220        230        240 
YYGKTSTAGL ISHFDEVLPM GPTIIYNVPS RTGQDIPPAV IEALSTYPNM AGVKECVGHE 

       250        260        270        280        290        300 
RVKCYTDKGI TIWSGNDDEC HDSRWKYGAT GVISVTSNLV PGLMRSLMFE GENAALNEKL 

       310        320        330        340        350        360 
LPLMKWLFSE PNPIGLNTAL AQLGVVRPVF RRPYAPLSLE KRTEFVRIVE AIGRENFVGQ 

       370 
KEVRVLDDDD FVLISRY 

« Hide

References

[1]"Molecular cloning of wheat dihydrodipicolinate synthase."
Kaneko T., Hashimoto T., Kumpaisal R., Yamada Y.
J. Biol. Chem. 265:17451-17455(1990) [PubMed: 2211639] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 52-68.
Strain: cv. Chinese Spring.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60599 mRNA. Translation: AAA34264.1.
PIRWZWTH6. B39213.
UniGeneTa.152.

3D structure databases

ProteinModelPortalP24847.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP24847.

Family and domain databases

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.
PANTHERPTHR12128. DHDPS. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PRINTSPR00146. DHPICSNTHASE.
TIGRFAMsTIGR00674. DapA. 1 hit.
PROSITEPS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPA2_WHEAT
AccessionPrimary (citable) accession number: P24847
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: September 21, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families