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Protein

4-hydroxy-tetrahydrodipicolinate synthase

Gene

dapA

Organism
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1) (Rochalimaea henselae)
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 (lysC)
  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
Sitei44Part of a proton relay during catalysisUniRule annotation1
Binding sitei45PyruvateUniRule annotation1
Sitei107Part of a proton relay during catalysisUniRule annotation1
Active sitei133Proton donor/acceptorUniRule annotation1
Active sitei162Schiff-base intermediate with substrateUniRule annotation1
Binding sitei204Pyruvate; 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

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:BH05000
OrganismiBartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1) (Rochalimaea henselae)
Taxonomic identifieri283166 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella
Proteomesi
  • UP000000421 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000501661 – 2944-hydroxy-tetrahydrodipicolinate synthaseAdd BLAST294

Proteomic databases

PaxDbiQ6G468.
PRIDEiQ6G468.

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi283166.BH05000.

Structurei

Secondary structure

1294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Helixi21 – 33Combined sources13
Beta strandi37 – 40Combined sources4
Turni44 – 47Combined sources4
Helixi48 – 50Combined sources3
Helixi53 – 67Combined sources15
Beta strandi73 – 76Combined sources4
Helixi82 – 94Combined sources13
Beta strandi98 – 103Combined sources6
Helixi112 – 125Combined sources14
Beta strandi130 – 134Combined sources5
Helixi136 – 139Combined sources4
Helixi145 – 154Combined sources10
Beta strandi158 – 163Combined sources6
Helixi169 – 178Combined sources10
Beta strandi180 – 187Combined sources8
Helixi189 – 191Combined sources3
Helixi192 – 197Combined sources6
Beta strandi202 – 206Combined sources5
Helixi207 – 209Combined sources3
Helixi212 – 223Combined sources12
Helixi227 – 243Combined sources17
Beta strandi246 – 248Combined sources3
Helixi251 – 259Combined sources9
Helixi276 – 288Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SI9X-ray2.10A/B/C/D1-294[»]
ProteinModelPortaliQ6G468.
SMRiQ6G468.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6G468.

Family & Domainsi

Sequence similaritiesi

Belongs to the DapA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDP. Bacteria.
COG0329. LUCA.
HOGENOMiHOG000173604.
KOiK01714.
OMAiGMDACVP.
OrthoDBiPOG091H00C1.

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.
[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.
PROSITEiPS00666. DHDPS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6G468-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKGAVTALI TPFDDNGAID EKAFCNFVEW QITQGINGVS PVGTTGESPT
60 70 80 90 100
LTHEEHKRII ELCVEQVAKR VPVVAGAGSN STSEAVELAK HAEKAGADAV
110 120 130 140 150
LVVTPYYNRP NQRGLYTHFS SIAKAISIPI IIYNIPSRSV IDMAVETMRD
160 170 180 190 200
LCRDFKNIIG VKDATGKIER ASEQREKCGK DFVQLSGDDC TALGFNAHGG
210 220 230 240 250
VGCISVSSNV APKLCAQLHA ACLCSDYKTA LKLNDLLMPL NRAVFIEPSP
260 270 280 290
AGIKYAAAKL GLCGTIVRSP IVPLSDTTKK IIDEALYHAG LLKE
Length:294
Mass (Da):31,483
Last modified:July 19, 2004 - v1
Checksum:iCDD074F2CDE871AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX897699 Genomic DNA. Translation: CAF27308.1.
RefSeqiWP_011180431.1. NZ_LRIJ01000002.1.

Genome annotation databases

EnsemblBacteriaiCAF27308; CAF27308; BH05000.
KEGGibhe:BH05000.
PATRICi20544783. VBIBarHen29080_0544.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX897699 Genomic DNA. Translation: CAF27308.1.
RefSeqiWP_011180431.1. NZ_LRIJ01000002.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SI9X-ray2.10A/B/C/D1-294[»]
ProteinModelPortaliQ6G468.
SMRiQ6G468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi283166.BH05000.

Proteomic databases

PaxDbiQ6G468.
PRIDEiQ6G468.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAF27308; CAF27308; BH05000.
KEGGibhe:BH05000.
PATRICi20544783. VBIBarHen29080_0544.

Phylogenomic databases

eggNOGiENOG4105CDP. Bacteria.
COG0329. LUCA.
HOGENOMiHOG000173604.
KOiK01714.
OMAiGMDACVP.
OrthoDBiPOG091H00C1.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00017.

Miscellaneous databases

EvolutionaryTraceiQ6G468.

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.
[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.
PROSITEiPS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDAPA_BARHE
AccessioniPrimary (citable) accession number: Q6G468
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2004
Last modified: November 2, 2016
This is version 87 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

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.