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Q8K9Z5 (DAPB_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BUsg_139
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length273 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

Subunit structure

Homotetramer By similarity. 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 – 2732734-hydroxy-tetrahydrodipicolinate reductase HAMAP-Rule MF_00102
PRO_0000141420

Regions

Nucleotide binding12 – 176NAD(P) By similarity
Nucleotide binding102 – 1043NAD(P) By similarity
Nucleotide binding126 – 1294NAD(P) By similarity
Region169 – 1702Substrate binding By similarity

Sites

Active site1591Proton donor/acceptor By similarity
Active site1631Proton donor By similarity
Binding site391NADP By similarity
Binding site1601Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9Z5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: E49AD0EADB67042F

FASTA27330,674
        10         20         30         40         50         60 
MKKKITRIAI TGAMGRMGQV LIKEIQKNKN TVLTAALVKN NHPLIGQNIG EKIGIGKTSV 

        70         80         90        100        110        120 
SISSDINIEK NDFDVLIDFT KPSGTFYFLE QCYEFKKNMI IGTTGFSEKE IKTINSYAKK 

       130        140        150        160        170        180 
IALIKASNFS IGINLLYQLI QKTTKILGNT SDIDIIEYHH RNKIDIPSGT ALSIGENISK 

       190        200        210        220        230        240 
VMNWELNKHS LYYTKGITKK IRETKKIGFS SIRSGNIIGK HTVLFSSSDE EIKITHSAFN 

       250        260        270 
RESFAKGAIE AAVWIHEKKH GLFNMNDILK DKF 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67707.1.
RefSeqNP_660496.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9Z5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg139.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67707; AAM67707; BUsg_139.
GeneID1005956.
KEGGbas:BUsg139.
PATRIC21247059. VBIBucAph100086_0143.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0289.
KOK00215.
OMAIVMAPNM.
OrthoDBEOG6SV5DS.
ProtClustDBPRK00048.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-149-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_BUCAP
AccessionPrimary (citable) accession number: Q8K9Z5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: February 19, 2014
This is version 85 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names