Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9FVC8 (DAPA2_ARATH)

Last modified November 3, 2009. Version 67. Feed History...

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

Names and origin

Protein namesRecommended name:
    Dihydrodipicolinate synthase 2, chloroplastic
      Short name=DHDPS 2
    EC=4.2.1.52
Gene names
Name: DHDPS2
Ordered Locus Names: At2g45440
ORF Names: F4L23.5
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

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

Pathway

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

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
Complete proteome
Gene Ontology (GO)
   Biological processdiaminopimelate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

Inferred from direct assay. Source: TAIR

   Molecular functiondihydrodipicolinate synthase activity Ref.1

Inferred from mutant phenotype. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Chloroplast Potential
Chain40 – 365326Dihydrodipicolinate synthase 2, chloroplastic
PRO_0000007198

Sites

Active site2221Schiff-base intermediate with substrate By similarity
Binding site1691Pyruvate By similarity
Site1941Involved in proton transfer during cleavage By similarity

Experimental info

Sequence conflict261S → G in AAG28565. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9FVC8-1 [UniParc].

Last modified June 20, 2001. Version 2.
Checksum: 43BECEF1FC3E557A

FASTA36540,292
        10         20         30         40         50         60 
MAALKGYGLC SMDSALQFPC PKLFNSYKRR SSKWVSPKAA VVPNFHLPMR SLEVKNRTNT 

        70         80         90        100        110        120 
DDIKALRVIT AIKTPYLPDG RFDLEAYDDL VNIQIQNGAE GVIVGGTTGE GQLMSWDEHI 

       130        140        150        160        170        180 
MLIGHTVNCF GGSIKVIGNT GSNSTREAIH ATEQGFAVGM HAALHINPYY GKTSIEGLIA 

       190        200        210        220        230        240 
HFQSVLHMGP TIIYNVPGRT GQDIPPRAIF KLSQNPNLAG VKECVGNKRV EEYTENGVVV 

       250        260        270        280        290        300 
WSGNDDECHD SRWDYGATGV ISVTSNLVPG LMRKLMFEGR NSSLNSKLLP LMAWLFHEPN 

       310        320        330        340        350        360 
PIGINTALAQ LGVSRPVFRL PYVPLPLSKR LEFVKLVKEI GREHFVGEKD VQALDDDDFI 


LIGRY 

« Hide

References

« Hide 'large scale' references
[1]"Identification of an Arabidopsis thaliana mutant accumulating threonine resulting from mutation in a new dihydrodipicolinate synthase gene."
Sarrobert C., Thibaud M.-C., Contard-David P., Gineste S., Bechtold N., Robaglia C., Nussaume L.
Plant J. 24:357-367(2000) [PubMed: 11069709] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Wassilewskija.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF200325 Genomic DNA. Translation: AAG28565.1.
AC002387 Genomic DNA. Translation: AAB82620.1.
BT004823 mRNA. Translation: AAO44089.1.
IPIIPI00541031.
PIRE84890.
RefSeqNP_182068.1.
UniGeneAt.12311

3D structure databases

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

Protein-protein interaction databases

STRINGQ9FVC8.

Proteomic databases

PRIDEQ9FVC8.

Genome annotation databases

GeneID819152.
GenomeReviewsGene locus AT2G45440 in contig CT485783_GR.
KEGGath:AT2G45440.
NMPDRfig|3702.1.peg.11720.

Organism-specific databases

TAIRAt2g45440.

Phylogenomic databases

OMAQGWQVGS.

Enzyme and pathway databases

BRENDA4.2.1.52. 302.

Gene expression databases

ArrayExpressQ9FVC8.
GenevestigatorQ9FVC8.
GermOnlineAT2G45440. Arabidopsis thaliana.

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...

Entry information

Entry nameDAPA2_ARATH
AccessionPrimary (citable) accession number: Q9FVC8
Secondary accession number(s): O22129
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 20, 2001
Last modified: November 3, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

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