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Q9FVC8 (DAPA2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic

Short name=HTPA synthase 2
EC=4.3.3.7
Gene names
Name:DHDPS2
Ordered Locus Names:At2g45440
ORF Names:F4L23.5
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

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

General annotation (Comments)

Function

Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) By similarity. HAMAP-Rule MF_00418

Catalytic activity

Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O. HAMAP-Rule MF_00418

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. HAMAP-Rule MF_00418

Subcellular location

Plastidchloroplast HAMAP-Rule MF_00418.

Sequence similarities

Belongs to the DapA family.

Caution

Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Chloroplast Potential
Chain40 – 3653264-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic HAMAP-Rule MF_00418
PRO_0000007198

Sites

Active site1941Proton donor/acceptor By similarity
Active site2221Schiff-base intermediate with substrate By similarity
Binding site1081Pyruvate By similarity
Binding site2611Pyruvate; via carbonyl oxygen By similarity
Site1071Part of a proton relay during catalysis By similarity
Site1701Part of a proton relay during catalysis By similarity

Experimental info

Sequence conflict261S → G in AAG28565. Ref.1

Secondary structure

.............................................................. 365
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9FVC8 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF200325 Genomic DNA. Translation: AAG28565.1.
AC002387 Genomic DNA. Translation: AAB82620.1.
CP002685 Genomic DNA. Translation: AEC10554.1.
BT004823 mRNA. Translation: AAO44089.1.
PIRE84890.
RefSeqNP_182068.1. NM_130106.2.
UniGeneAt.12311.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DPPX-ray2.00A/B39-365[»]
4DPQX-ray2.20A/B39-365[»]
ProteinModelPortalQ9FVC8.
SMRQ9FVC8. Positions 59-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid4488. 2 interactions.
STRING3702.AT2G45440.1-P.

Proteomic databases

PaxDbQ9FVC8.
PRIDEQ9FVC8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G45440.1; AT2G45440.1; AT2G45440.
GeneID819152.
KEGGath:AT2G45440.

Organism-specific databases

TAIRAT2G45440.

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHOG000173604.
InParanoidQ9FVC8.
KOK01714.
OMAMLYSGDD.
PhylomeDBQ9FVC8.

Enzyme and pathway databases

BioCycARA:AT2G45440-MONOMER.
UniPathwayUPA00034; UER00017.

Gene expression databases

ArrayExpressQ9FVC8.
GenevestigatorQ9FVC8.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00418. DapA.
InterProIPR013785. Aldolase_TIM.
IPR005263. DapA.
IPR002220. DapA-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR020624. Dihydrodipicolinate_synth_CS.
[Graphical view]
PANTHERPTHR12128. PTHR12128. 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_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: May 14, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names