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B2SC36 (B2SC36_BRUA1) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 45. Feed History...

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

Names and origin

Protein namesRecommended name:
4-hydroxy-tetrahydrodipicolinate reductase HAMAP-Rule MF_00102

Short name=HTPA reductase HAMAP-Rule MF_00102
EC=1.17.1.8 HAMAP-Rule MF_00102
Gene names
Name:dapB HAMAP-Rule MF_00102
Ordered Locus Names:BAbS19_II09380 EMBL ACD74423.1
OrganismBrucella abortus (strain S19) [Complete proteome] [HAMAP] EMBL ACD74423.1
Taxonomic identifier430066 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length279 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 SAAS SAAS023940

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 SAAS SAAS023940

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. HAMAP-Rule MF_00102 SAAS SAAS023940

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00102

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00102 SAAS SAAS023940.

Sequence similarities

Belongs to the DapB family. HAMAP-Rule MF_00102

Caution

Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli (PubMed:20503968) 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. HAMAP-Rule MF_00102

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding18 – 236NAD(P) By similarity HAMAP-Rule MF_00102
Nucleotide binding108 – 1103NAD(P) By similarity HAMAP-Rule MF_00102
Nucleotide binding132 – 1354NAD(P) By similarity HAMAP-Rule MF_00102
Region176 – 1772Substrate binding By similarity HAMAP-Rule MF_00102

Sites

Active site1661Proton donor/acceptor By similarity HAMAP-Rule MF_00102
Active site1701Proton donor By similarity HAMAP-Rule MF_00102
Binding site441NAD By similarity HAMAP-Rule MF_00102
Binding site451NADP By similarity HAMAP-Rule MF_00102
Binding site1671Substrate By similarity HAMAP-Rule MF_00102

Sequences

Sequence LengthMass (Da)Tools
B2SC36 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: C5F1BCA2389DF347

FASTA27928,753
        10         20         30         40         50         60 
MSEEVQGGNS EMGLVVVGAG GRMGQTLIRT IQSIEGAKLV GAIERSGSPF LGKDAGEVTG 

        70         80         90        100        110        120 
IGTLGVAITD DPLPVFAKAH GVLDFTSPAA SVEFAGLAAQ ARIVHVIGTT GCSAEDDEKI 

       130        140        150        160        170        180 
RAAARHATIV KSGNMSLGVN LLSVLVQKAA EALGPEDFDI EILEMHHRHK VDAPSGTALL 

       190        200        210        220        230        240 
LGEAAARGRD IALADNSVRV RDGYTGPRET GAIGFATLRG GSVIGDHSVI LAGTGERVVL 

       250        260        270 
SHHAEDRSIF ARGAIKAALW AHGKKPGLYS MLDVLGLNT 

« Hide

References

[1]"Genome sequence of Brucella abortus vaccine strain S19 compared to virulent strains yields candidate virulence genes."
Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.
PLoS ONE 3:E2193-E2193(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S19.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000888 Genomic DNA. Translation: ACD74423.1.
RefSeqYP_001932869.1. NC_010740.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING430066.BAbS19_II09380.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD74423; ACD74423; BAbS19_II09380.
GeneID6325885.
KEGGbmc:BAbS19_II09380.
PATRIC17816482. VBIBruAbo38055_1036.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBABO430066:GHI6-2982-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 nameB2SC36_BRUA1
AccessionPrimary (citable) accession number: B2SC36
Entry history
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)