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Protein

4-hydroxy-tetrahydrodipicolinate reductase

Gene

dapB

Organism
Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77) (Xenorhabdus luminescens (strain 2))
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

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

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.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 annotationSAAS 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 annotationSAAS annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Bifunctional aspartokinase/homoserine dehydrogenase (thrA), Aspartokinase (lysC), Bifunctional aspartokinase/homoserine dehydrogenase (metL)
  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
Binding sitei38NADUniRule annotation1
Binding sitei39NADPUniRule annotation1
Active sitei159Proton donor/acceptorUniRule annotation1
Binding sitei160SubstrateUniRule annotation1
Active sitei163Proton donorUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi12 – 17NAD(P)UniRule annotation6
Nucleotide bindingi102 – 104NAD(P)UniRule annotation3
Nucleotide bindingi126 – 129NAD(P)UniRule annotation4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductaseUniRule annotationSAAS annotationImported
Biological processAmino-acid biosynthesis, Diaminopimelate biosynthesisUniRule annotationSAAS annotation, Lysine biosynthesisUniRule annotationSAAS annotation
LigandNADUniRule annotationSAAS annotation, NADPUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00034; UER00018

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-tetrahydrodipicolinate reductaseUniRule annotationSAAS annotation (EC:1.17.1.8UniRule annotationSAAS annotation)
Short name:
HTPA reductaseUniRule annotation
Gene namesi
Name:dapBUniRule annotationImported
Ordered Locus Names:PAU_00560Imported
OrganismiPhotorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77) (Xenorhabdus luminescens (strain 2))Imported
Taxonomic identifieri553480 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesMorganellaceaePhotorhabdus
Proteomesi
  • UP000002747 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi553480.PAU_00560

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 129DapB_NInterPro annotationAdd BLAST124
Domaini132 – 268DapB_CInterPro annotationAdd BLAST137

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni169 – 170Substrate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the DapB family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiENOG4105DUK Bacteria
COG0289 LUCA
HOGENOMiHOG000227153
KOiK00215
OMAiRESFMPG
OrthoDBiPOG091H01P6

Family and domain databases

HAMAPiMF_00102 DapB, 1 hit
InterProiView protein in InterPro
IPR022663 DapB_C
IPR000846 DapB_N
IPR022664 DapB_N_CS
IPR023940 DHDPR_bac
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR20836 PTHR20836, 1 hit
PfamiView protein in Pfam
PF05173 DapB_C, 1 hit
PF01113 DapB_N, 1 hit
PIRSFiPIRSF000161 DHPR, 1 hit
SUPFAMiSSF51735 SSF51735, 2 hits
TIGRFAMsiTIGR00036 dapB, 1 hit
PROSITEiView protein in PROSITE
PS01298 DAPB, 1 hit

Sequencei

Sequence statusi: Complete.

C7BJY6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADTDIRVAI VGAGGRMGRQ LIQAVHQLSG VVLGVALERS GSSLLGTDAG
60 70 80 90 100
ELAGIGHIGV TVCDDLKNVV DDFDVLIDFT RPEGTLAHLE ICRRHSKAIV
110 120 130 140 150
IGTTGFDDEG KQAIKDASAN IPIVFAANFS VGVNLVLKLL EKAAKVMGEY
160 170 180 190 200
TDIEIIEAHH RHKVDAPSGT ALAMGESIAH ALGRDLKECA VYAREGYTGE
210 220 230 240 250
RDPKSIGFAT IRAGDIVGEH TAMFADVGER VEITHKASSR MTFANGAVKA
260 270
ALWLNGKNSG LFTMKDVLNL DLI
Length:273
Mass (Da):28,957
Last modified:September 22, 2009 - v1
Checksum:i9C657FA42BE8EEB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM162591 Genomic DNA Translation: CAQ82652.1

Genome annotation databases

EnsemblBacteriaiCAQ82652; CAQ82652; PAU_00560
KEGGipay:PAU_00560

Similar proteinsi

Entry informationi

Entry nameiC7BJY6_PHOAA
AccessioniPrimary (citable) accession number: C7BJY6
Entry historyiIntegrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: March 28, 2018
This is version 65 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported
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Main funding by: National Institutes of Health