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Reviewed, UniProtKB/Swiss-Prot P24846 (DAPA1_WHEAT)

Last modified September 22, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Dihydrodipicolinate synthase 1, chloroplastic
      Short name=DHDPS 1
    EC=4.2.1.52
OrganismTriticum aestivum (Wheat)
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

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Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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

Plastid › chloroplast.

Sequence similarities

Belongs to the DHDPS family.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6262Chloroplast Ref.1
Chain63 – 388326Dihydrodipicolinate synthase 1, chloroplastic
PRO_0000007203

Sites

Active site2451Schiff-base intermediate with substrate By similarity
Binding site1921Pyruvate By similarity
Site2171Involved in proton transfer during cleavage By similarity

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Sequences

Sequence LengthMass (Da)Tools
P24846-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 9F054AFA75BA54D0

FASTA38842,413
        10         20         30         40         50         60 
MPYLQPPRPH PHPHPTSRLS RASPPSPFPF FPAGTSRSGR LQPVPVSGHS ASRVSKGKFA 

        70         80         90        100        110        120 
VAAVTLDDYL PMRSTEVKNR TSTDGIKSLR LITAVKTPYL PDGRFDLEAY DSLINTQING 

       130        140        150        160        170        180 
GAEGVIVGGT TGEGHLMSWD EHIMLIGHTV NCFGANIKVI GNTGSNSTRE AVHATEQGFA 

       190        200        210        220        230        240 
VGMHAALHVN PYYGKTSTEG LISHFKEVLP MGPTIIYNVP SRTSQDIPPP VIEALSSYSN 

       250        260        270        280        290        300 
MAGVKECVGH ERVKCYTDKG ISIWSGNDDE CHDSRWKYGA TGVISVASNL VPGLMHSLMF 

       310        320        330        340        350        360 
EGENAALNEK LLPLMKWLFC EPNPIGLNTA LAQLGVVRPV FRLPYTPLPL EKRVEFVRIV 

       370        380 
EAIGRENFVG QKESRVLDDD DFVLISRY

« Hide

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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 63-79.
Strain: cv. Chinese Spring.

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Cross-references

Sequence databases

M60598 mRNA. Translation: AAA34263.1.
PIRWZWTH7. A39213.
UniGeneTa.23170

3D structure databases

HSSPHSSP built from PDB template 1DHP based on UniProtKB P05640.
ModBaseSearch...

Organism-specific databases

GrameneP24846.

Enzyme and pathway databases

BRENDA4.2.1.52. 253.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR005263. DapA_synth.
IPR002220. DHDPS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR12128. DHDPS. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PRINTSPR00146. DHPICSNTHASE.
ProDomPD001859. DHDPS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00674. dapA. 1 hit.
PROSITEPS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameDAPA1_WHEAT
AccessionPrimary (citable) accession number: P24846
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: September 22, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents