Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

4-hydroxy-tetrahydrodipicolinate reductase

Gene

dapB

Organism
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.UniRule annotation

Catalytic activityi

(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H.UniRule annotation

Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 4 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 (DR63_379), Aspartokinase (BTH_I1945)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA-1), 4-hydroxy-tetrahydrodipicolinate synthase (dapA-2)
  4. 4-hydroxy-tetrahydrodipicolinate reductase (dapB), 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
Binding sitei36NADUniRule annotation1
Binding sitei37NADPUniRule annotation1
Active sitei156Proton donor/acceptorUniRule annotation1
Binding sitei157SubstrateUniRule annotation1
Active sitei160Proton donorUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 15NAD(P)UniRule annotation6
Nucleotide bindingi99 – 101NAD(P)UniRule annotation3
Nucleotide bindingi123 – 126NAD(P)UniRule annotation4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

UniPathwayiUPA00034; UER00018.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-tetrahydrodipicolinate reductaseUniRule annotation (EC:1.17.1.8UniRule annotation)
Short name:
HTPA reductaseUniRule annotation
Gene namesi
Name:dapBUniRule annotation
Ordered Locus Names:BTH_I1208
OrganismiBurkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Taxonomic identifieri271848 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000001930 Componenti: Chromosome I

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_10000085471 – 2684-hydroxy-tetrahydrodipicolinate reductaseAdd BLAST268

Structurei

Secondary structure

1268
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi14 – 25Combined sources12
Beta strandi29 – 35Combined sources7
Turni41 – 44Combined sources4
Turni47 – 52Combined sources6
Helixi63 – 69Combined sources7
Beta strandi71 – 75Combined sources5
Helixi79 – 92Combined sources14
Beta strandi95 – 98Combined sources4
Helixi105 – 114Combined sources10
Turni115 – 117Combined sources3
Beta strandi118 – 122Combined sources5
Helixi128 – 143Combined sources16
Beta strandi145 – 147Combined sources3
Beta strandi149 – 156Combined sources8
Beta strandi162 – 164Combined sources3
Helixi166 – 177Combined sources12
Turni178 – 180Combined sources3
Helixi183 – 186Combined sources4
Beta strandi187 – 189Combined sources3
Beta strandi203 – 209Combined sources7
Beta strandi215 – 222Combined sources8
Beta strandi224 – 234Combined sources11
Helixi238 – 252Combined sources15
Beta strandi255 – 259Combined sources5
Helixi261 – 264Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F3YX-ray2.10A/B1-268[»]
ProteinModelPortaliQ2SZ94.
SMRiQ2SZ94.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni166 – 167Substrate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the DapB family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000227153.
KOiK00215.
OMAiYAREGHT.
OrthoDBiPOG091H01P6.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00102. DapB. 1 hit.
InterProiIPR022663. DapB_C.
IPR000846. DapB_N.
IPR022664. DapB_N_CS.
IPR023940. DHDPR_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR20836. PTHR20836. 1 hit.
PfamiPF05173. DapB_C. 1 hit.
PF01113. DapB_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000161. DHPR. 1 hit.
SUPFAMiSSF51735. SSF51735. 2 hits.
TIGRFAMsiTIGR00036. dapB. 1 hit.
PROSITEiPS01298. DAPB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2SZ94-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSMKIAIAG ASGRMGRMLI EAVLAAPDAT LVGALDRTGS PQLGQDAGAF
60 70 80 90 100
LGKQTGVALT DDIERVCAEA DYLIDFTLPE GTLVHLDAAL RHDVKLVIGT
110 120 130 140 150
TGFSEPQKAQ LRAAGEKIAL VFSANMSVGV NVTMKLLEFA AKQFAQGYDI
160 170 180 190 200
EIIEAHHRHK VDAPSGTALM MGETIAAATG RSLDDCAVYG RHGVTGERDP
210 220 230 240 250
STIGFSAIRG GDIVGDHTVL FAGIGERIEI THKSASRVSY AQGALRAARF
260
LAGRDAGFFD MQDVLGLR
Length:268
Mass (Da):28,213
Last modified:January 24, 2006 - v1
Checksum:i77D8AB40058EE3F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000086 Genomic DNA. Translation: ABC36898.1.

Genome annotation databases

EnsemblBacteriaiABC36898; ABC36898; BTH_I1208.
KEGGibte:BTH_I1208.
PATRICi19305310. VBIBurTha36512_3964.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000086 Genomic DNA. Translation: ABC36898.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F3YX-ray2.10A/B1-268[»]
ProteinModelPortaliQ2SZ94.
SMRiQ2SZ94.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC36898; ABC36898; BTH_I1208.
KEGGibte:BTH_I1208.
PATRICi19305310. VBIBurTha36512_3964.

Phylogenomic databases

HOGENOMiHOG000227153.
KOiK00215.
OMAiYAREGHT.
OrthoDBiPOG091H01P6.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00018.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00102. DapB. 1 hit.
InterProiIPR022663. DapB_C.
IPR000846. DapB_N.
IPR022664. DapB_N_CS.
IPR023940. DHDPR_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR20836. PTHR20836. 1 hit.
PfamiPF05173. DapB_C. 1 hit.
PF01113. DapB_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000161. DHPR. 1 hit.
SUPFAMiSSF51735. SSF51735. 2 hits.
TIGRFAMsiTIGR00036. dapB. 1 hit.
PROSITEiPS01298. DAPB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDAPB_BURTA
AccessioniPrimary (citable) accession number: Q2SZ94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: November 2, 2016
This is version 82 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 reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.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.