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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. no protein annotated in this organism
  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)LengthDescriptionGraphical viewFeature identifierActions
Sitei44 – 441Part of a proton relay during catalysisUniRule annotation
Binding sitei45 – 451PyruvateUniRule annotation
Sitei107 – 1071Part of a proton relay during catalysisUniRule annotation
Active sitei133 – 1331Proton donor/acceptorUniRule annotation
Active sitei162 – 1621Schiff-base intermediate with substrateUniRule annotation
Binding sitei204 – 2041Pyruvate; via carbonyl oxygenUniRule annotation

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

BioCyciBHEN283166:GIVZ-499-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: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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2942944-hydroxy-tetrahydrodipicolinate synthasePRO_1000050166Add
BLAST

Proteomic databases

PaxDbiQ6G468.

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi283166.BH05000.

Structurei

Secondary structure

1
294
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi21 – 3313Combined sources
Beta strandi37 – 404Combined sources
Turni44 – 474Combined sources
Helixi48 – 503Combined sources
Helixi53 – 6715Combined sources
Beta strandi73 – 764Combined sources
Helixi82 – 9413Combined sources
Beta strandi98 – 1036Combined sources
Helixi112 – 12514Combined sources
Beta strandi130 – 1345Combined sources
Helixi136 – 1394Combined sources
Helixi145 – 15410Combined sources
Beta strandi158 – 1636Combined sources
Helixi169 – 17810Combined sources
Beta strandi180 – 1878Combined sources
Helixi189 – 1913Combined sources
Helixi192 – 1976Combined sources
Beta strandi202 – 2065Combined sources
Helixi207 – 2093Combined sources
Helixi212 – 22312Combined sources
Helixi227 – 24317Combined sources
Beta strandi246 – 2483Combined sources
Helixi251 – 2599Combined sources
Helixi276 – 28813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SI9X-ray2.10A/B/C/D1-294[»]
ProteinModelPortaliQ6G468.
SMRiQ6G468. Positions 1-288.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
3SI9X-ray2.10A/B/C/D1-294[»]
ProteinModelPortaliQ6G468.
SMRiQ6G468. Positions 1-288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi283166.BH05000.

Proteomic databases

PaxDbiQ6G468.

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.
BioCyciBHEN283166:GIVZ-499-MONOMER.

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: September 7, 2016
This is version 85 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.