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Protein

4-hydroxy-tetrahydrodipicolinate synthase

Gene

dapA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).UniRule annotation

Catalytic activityi

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

Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 3 of the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Aspartokinase 3 (yclM), Aspartokinase 2 (lysC), Aspartokinase 1 (dapG)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA)
  4. 4-hydroxy-tetrahydrodipicolinate reductase (dapB)
This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate, the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei45Part of a proton relay during catalysisUniRule annotation1
Binding sitei46PyruvateUniRule annotation1
Sitei108Part of a proton relay during catalysisUniRule annotation1
Active sitei134Proton donor/acceptorUniRule annotation1
Active sitei163Schiff-base intermediate with substrateUniRule annotation1
Binding sitei205Pyruvate; via carbonyl oxygenUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciBSUB:BSU16770-MONOMER.
UniPathwayiUPA00034; UER00017.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-tetrahydrodipicolinate synthaseUniRule annotation (EC:4.3.3.7UniRule annotation)
Short name:
HTPA synthaseUniRule annotation
Gene namesi
Name:dapAUniRule annotation
Ordered Locus Names:BSU16770
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5904.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001030841 – 2904-hydroxy-tetrahydrodipicolinate synthaseAdd BLAST290

Proteomic databases

PaxDbiQ04796.
PRIDEiQ04796.

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009236.

Chemistry databases

BindingDBiQ04796.

Structurei

3D structure databases

ProteinModelPortaliQ04796.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DapA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDP. Bacteria.
COG0329. LUCA.
HOGENOMiHOG000173604.
InParanoidiQ04796.
KOiK01714.
OMAiGMDACVP.
PhylomeDBiQ04796.

Family and domain databases

CDDicd00950. DHDPS. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00418. DapA. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR005263. DapA.
IPR002220. DapA-like.
IPR020625. Schiff_base-form_aldolases_AS.
IPR020624. Schiff_base-form_aldolases_CS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
SMARTiSM01130. DHDPS. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00674. dapA. 1 hit.
PROSITEiPS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04796-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFGNVSTAM ITPFDNKGNV DFQKLSTLID YLLKNGTDSL VVAGTTGESP
60 70 80 90 100
TLSTEEKIAL FEYTVKEVNG RVPVIAGTGS NNTKDSIKLT KKAEEAGVDA
110 120 130 140 150
VMLVTPYYNK PSQEGMYQHF KAIAAETSLP VMLYNVPGRT VASLAPETTI
160 170 180 190 200
RLAADIPNVV AIKEASGDLE AITKIIAETP EDFYVYSGDD ALTLPILSVG
210 220 230 240 250
GRGVVSVASH IAGTDMQQMI KNYTNGQTAN AALIHQKLLP IMKELFKAPN
260 270 280 290
PAPVKTALQL RGLDVGSVRL PLVPLTEDER LSLSSTISEL
Length:290
Mass (Da):31,042
Last modified:October 1, 1993 - v1
Checksum:i40FA887AC644B6F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08471 Genomic DNA. Translation: AAA22385.1.
AL009126 Genomic DNA. Translation: CAB13550.1.
PIRiE46665.
RefSeqiNP_389559.1. NC_000964.3.
WP_003245816.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13550; CAB13550; BSU16770.
GeneIDi939657.
KEGGibsu:BSU16770.
PATRICi18975163. VBIBacSub10457_1773.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08471 Genomic DNA. Translation: AAA22385.1.
AL009126 Genomic DNA. Translation: CAB13550.1.
PIRiE46665.
RefSeqiNP_389559.1. NC_000964.3.
WP_003245816.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliQ04796.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009236.

Chemistry databases

BindingDBiQ04796.
ChEMBLiCHEMBL5904.

Proteomic databases

PaxDbiQ04796.
PRIDEiQ04796.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13550; CAB13550; BSU16770.
GeneIDi939657.
KEGGibsu:BSU16770.
PATRICi18975163. VBIBacSub10457_1773.

Phylogenomic databases

eggNOGiENOG4105CDP. Bacteria.
COG0329. LUCA.
HOGENOMiHOG000173604.
InParanoidiQ04796.
KOiK01714.
OMAiGMDACVP.
PhylomeDBiQ04796.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00017.
BioCyciBSUB:BSU16770-MONOMER.

Miscellaneous databases

PROiQ04796.

Family and domain databases

CDDicd00950. DHDPS. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00418. DapA. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR005263. DapA.
IPR002220. DapA-like.
IPR020625. Schiff_base-form_aldolases_AS.
IPR020624. Schiff_base-form_aldolases_CS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
SMARTiSM01130. DHDPS. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00674. dapA. 1 hit.
PROSITEiPS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDAPA_BACSU
AccessioniPrimary (citable) accession number: Q04796
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 5, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.