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Q9LZX6 (DAPA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxy-tetrahydrodipicolinate synthase 1, chloroplastic

Short name=HTPA synthase 1
EC=4.3.3.7
Gene names
Name:DHDPS1
Synonyms:DHDPS, DHPS1
Ordered Locus Names:At3g60880
ORF Names:T4C21_290
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 transcript 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.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Diaminopimelate biosynthesis
Lysine biosynthesis
   Cellular componentChloroplast
Plastid
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   LigandSchiff base
   Molecular functionLyase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdiaminopimelate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

lysine biosynthetic process via diaminopimelate

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-hydroxy-tetrahydrodipicolinate synthase

Inferred from direct assay PubMed 10758475. Source: TAIR

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9LZX6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: May be due to a competing acceptor splice site.
Isoform 2 (identifier: Q9LZX6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     30-30: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Chloroplast Potential
Chain40 – 3653264-hydroxy-tetrahydrodipicolinate synthase 1, chloroplastic HAMAP-Rule MF_00418
PRO_0000007197

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

Natural variations

Alternative sequence301Missing in isoform 2.
VSP_009000

Experimental info

Sequence conflict2861A → E in CAB45642. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 21, 2003. Version 2.
Checksum: F07BBAE68F004484

FASTA36540,620
        10         20         30         40         50         60 
MSALKNYGLI SIDSALHFPR SNQLQSYKRR NAKWVSPIAA VVPNFHLPMR SLEDKNRTNT 

        70         80         90        100        110        120 
DDIRSLRVIT AIKTPYLPDG RFDLQAYDDL VNTQIENGAE GVIVGGTTGE GQLMSWDEHI 

       130        140        150        160        170        180 
MLIGHTVNCF GGRIKVIGNT GSNSTREAIH ATEQGFAMGM HGALHINPYY GKTSIEGMNA 

       190        200        210        220        230        240 
HFQTVLHMGP TIIYNVPGRT CQDIPPQVIF KLSQNPNMAG VKECVGNNRV EEYTEKGIVV 

       250        260        270        280        290        300 
WSGNDDQCHD SRWDHGATGV ISVTSNLVPG LMRKLMFEGR NSALNAKLLP LMDWLFQEPN 

       310        320        330        340        350        360 
PIGVNTALAQ LGVARPVFRL PYVPLPLSKR IEFVKLVKEI GREHFVGDRD VQVLDDDDFI 


LIGRY 

« Hide

Isoform 2 [UniParc].

Checksum: 73895B17AA79E6EE
Show »

FASTA36440,464

References

« Hide 'large scale' references
[1]"Isolation of a poplar and an Arabidopsis thaliana dihydrodipicolinate synthase cDNA clone."
Vauterin M., Jacobs M.
Plant Mol. Biol. 25:545-550(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [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] (ISOFORM 1).
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]Vauterin M.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 1-159 (ISOFORM 2).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X72971 mRNA. Translation: CAB45642.1.
AL162295 Genomic DNA. Translation: CAB82692.1.
CP002686 Genomic DNA. Translation: AEE80120.1.
CP002686 Genomic DNA. Translation: AEE80121.1.
AY063943 mRNA. Translation: AAL36299.1.
AY096442 mRNA. Translation: AAM20082.1.
AY087718 mRNA. Translation: AAM65255.1.
X98080 Genomic DNA. Translation: CAA66703.1.
PIRS46304.
T47899.
RefSeqNP_191647.1. NM_115952.2. [Q9LZX6-2]
NP_850730.1. NM_180399.2. [Q9LZX6-1]
UniGeneAt.437.

3D structure databases

ProteinModelPortalQ9LZX6.
SMRQ9LZX6. Positions 69-321.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid10573. 1 interaction.

Proteomic databases

PaxDbQ9LZX6.
PRIDEQ9LZX6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G60880.2; AT3G60880.2; AT3G60880. [Q9LZX6-1]
GeneID825259.
KEGGath:AT3G60880.

Organism-specific databases

TAIRAT3G60880.

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHOG000173604.
InParanoidQ9LZX6.
KOK01714.
OMAQQRASCG.
PhylomeDBQ9LZX6.

Enzyme and pathway databases

BioCycARA:AT3G60880-MONOMER.
UniPathwayUPA00034; UER00017.

Gene expression databases

GenevestigatorQ9LZX6.

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 nameDAPA1_ARATH
AccessionPrimary (citable) accession number: Q9LZX6
Secondary accession number(s): O49355, Q8VZQ1, Q9SW58
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 21, 2003
Last modified: June 11, 2014
This is version 112 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names