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B2FQ70 (DAPB_STRMK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxy-tetrahydrodipicolinate reductase

Short name=HTPA reductase
EC=1.17.1.8
Gene names
Name:dapB
Ordered Locus Names:Smlt2217
OrganismStenotrophomonas maltophilia (strain K279a) [Complete proteome] [HAMAP]
Taxonomic identifier522373 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate By similarity. HAMAP-Rule MF_00102

Catalytic activity

(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H. HAMAP-Rule MF_00102

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. HAMAP-Rule MF_00102

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00102.

Sequence similarities

Belongs to the DapB family.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2392394-hydroxy-tetrahydrodipicolinate reductase HAMAP-Rule MF_00102
PRO_1000094011

Regions

Nucleotide binding12 – 176NAD(P) By similarity
Nucleotide binding94 – 963NAD(P) By similarity
Nucleotide binding118 – 1214NAD(P) By similarity
Region160 – 1612Substrate binding By similarity

Sites

Active site1501Proton donor/acceptor By similarity
Active site1541Proton donor By similarity
Binding site1511Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2FQ70 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 4287EC0BB102D83B

FASTA23925,157
        10         20         30         40         50         60 
MNQTPLRLLI HGASGRMGQA LLRLAAEHPE TLQIAAAVTG RAPAQRVVDG VPFFAASELP 

        70         80         90        100        110        120 
GAPAFDVAID FSLPEGFDPM LALCVERGAG LVSGTTGISS TQRQALEAAA ARIPLVWASN 

       130        140        150        160        170        180 
FSLGVAVLDE LVERAAQALA GWDCDIVESH HTQKKDAPSG TALTLGAAAQ RGGAEPHYAS 

       190        200        210        220        230 
LRAGDIVGEH LVQFTGLGER IELVHRATNR DIFARGALFA ARQLQGRAPG SYRVRDLLQ 

« Hide

References

[1]"The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants."
Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A., Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E., Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S., Quail M.A. expand/collapse author list , Rajandream M.A., Harris D., Churcher C., Bentley S.D., Parkhill J., Thomson N.R., Avison M.B.
Genome Biol. 9:R74.1-R74.13(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K279a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM743169 Genomic DNA. Translation: CAQ45715.1.
RefSeqYP_001972016.1. NC_010943.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING522373.Smlt2217.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ45715; CAQ45715; Smlt2217.
GeneID6394132.
KEGGsml:Smlt2217.
PATRIC23700081. VBISteMal45202_2110.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0289.
HOGENOMHOG000227153.
KOK00215.
OMAQPRYVSL.
OrthoDBEOG6SV5DS.

Enzyme and pathway databases

BioCycSMAL522373:GJE8-2156-MONOMER.
UniPathwayUPA00034; UER00018.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00102. DapB.
InterProIPR022663. DapB_C.
IPR000846. DapB_N.
IPR022664. DapB_N_CS.
IPR011770. Dihydrodipicolinate_Rdtase.
IPR023940. Dihydrodipicolinate_Rdtase_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR20836. PTHR20836. 1 hit.
PfamPF05173. DapB_C. 1 hit.
PF01113. DapB_N. 1 hit.
[Graphical view]
PIRSFPIRSF000161. DHPR. 1 hit.
TIGRFAMsTIGR00036. dapB. 1 hit.
PROSITEPS01298. DAPB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPB_STRMK
AccessionPrimary (citable) accession number: B2FQ70
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways