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A5UCB3 (DAPB_HAEIE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:CGSHiEE_05135
OrganismHaemophilus influenzae (strain PittEE) [Complete proteome] [HAMAP]
Taxonomic identifier374930 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length270 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 – 2702704-hydroxy-tetrahydrodipicolinate reductase HAMAP-Rule MF_00102
PRO_1000008567

Regions

Nucleotide binding9 – 146NAD(P) By similarity
Nucleotide binding99 – 1013NAD(P) By similarity
Nucleotide binding123 – 1264NAD(P) By similarity
Region166 – 1672Substrate binding By similarity

Sites

Active site1561Proton donor/acceptor By similarity
Active site1601Proton donor By similarity
Binding site351NAD By similarity
Binding site361NADP By similarity
Binding site1571Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A5UCB3 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 07932E5133CFDF0B

FASTA27028,923
        10         20         30         40         50         60 
MTLKIAIAGA GGRMGRQLIQ AVHSAEGVEL GAAFERKGSS LVGTDAGELA GIGHLGVAVS 

        70         80         90        100        110        120 
DDLESQKDKF DLLIDFTRPE GSLEHIAFCV ANNKKMVIGT TGFDQNGKAA IKAASDKIAI 

       130        140        150        160        170        180 
VFASNFSVGV NLVFKLLEKA AKVMGDYCDI EVIEAHHRHK VDAPSGTALS MGEHIAKTLG 

       190        200        210        220        230        240 
RDLKTHGVFC REGITGERKR DEIGFSTIRA SDVVGEHMVW FADIGERVEI SHKASSRMTF 

       250        260        270 
ANGAVRAGKW LENKANGLFD MTDVLDLNNL 

« Hide

References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PittEE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000671 Genomic DNA. Translation: ABQ98414.1.
RefSeqYP_001290797.1. NC_009566.1.

3D structure databases

ProteinModelPortalA5UCB3.
SMRA5UCB3. Positions 3-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374930.CGSHiEE_05135.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ98414; ABQ98414; CGSHiEE_05135.
GeneID5226204.
KEGGhip:CGSHiEE_05135.
PATRIC20278185. VBIHaeInf81350_1035.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0289.
HOGENOMHOG000227153.
KOK00215.
OMAIVMAPNM.
OrthoDBEOG6SV5DS.
ProtClustDBPRK00048.

Enzyme and pathway databases

BioCycHINF374930:GJDD-975-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_HAEIE
AccessionPrimary (citable) accession number: A5UCB3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: February 19, 2014
This is version 53 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