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Q8G1R0 (DAPA_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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 synthase

Short name=HTPA synthase
EC=4.3.3.7
Gene names
Name:dapA
Ordered Locus Names:BR0646, BS1330_I0642
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length293 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) By similarity. HAMAP-Rule MF_00418

Catalytic activity

Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O. HAMAP-Rule MF_00418

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. HAMAP-Rule MF_00418

Subunit structure

Homotetramer; dimer of dimers By similarity. HAMAP-Rule MF_00418

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00418.

Sequence similarities

Belongs to the DapA family.

Caution

Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Diaminopimelate biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processdiaminopimelate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lysine biosynthetic process via diaminopimelate

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-hydroxy-tetrahydrodipicolinate synthase

Inferred from electronic annotation. Source: UniProtKB-EC

amine-lyase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2932934-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418
PRO_0000103089

Sites

Active site1331Proton donor/acceptor By similarity
Active site1621Schiff-base intermediate with substrate By similarity
Binding site451Pyruvate By similarity
Binding site2041Pyruvate; via carbonyl oxygen By similarity
Site441Part of a proton relay during catalysis By similarity
Site1071Part of a proton relay during catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8G1R0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 4687B828C4AA5C7B

FASTA29331,598
        10         20         30         40         50         60 
MLKGSITALV TPFDREGAFD EKAFRAFVNW QIEEGTKGLV PVGTTGETPT LSHDEHKRVI 

        70         80         90        100        110        120 
EVCIEVAAGR VPVIAGAGSN NTVEAIELAQ HAEKAGADAV LVVTPYYNKP NQRGLYEHFS 

       130        140        150        160        170        180 
RVVRSISIPL VIYNIPGRSI IDMTPETMGA LVRDCKNIVG VKDATGKIER VSEQRAICGK 

       190        200        210        220        230        240 
EFIQLSGEDA TALGFNAHGG VGCISVTSNI APRLCAEFQE ACQAGNFAKA LELQDRLMPL 

       250        260        270        280        290 
HKALFLEPNP SGPKYALSRL GRIENVLRSP MVTIEAATAE KIDHAMKHAG LIN 

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014291 Genomic DNA. Translation: AAN29575.1.
CP002997 Genomic DNA. Translation: AEM17992.1.
RefSeqNP_697660.1. NC_004310.3.
YP_005615484.1. NC_017251.1.

3D structure databases

ProteinModelPortalQ8G1R0.
SMRQ8G1R0. Positions 1-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204722.BR0646.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN29575; AAN29575; BR0646.
AEM17992; AEM17992; BS1330_I0642.
GeneID1166309.
12136963.
KEGGbms:BR0646.
bsi:BS1330_I0642.
PATRIC17789587. VBIBruSui107850_0660.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHOG000173604.
KOK01714.
OMAHQKLFVE.
OrthoDBEOG6W7235.
ProtClustDBPRK03170.

Enzyme and pathway databases

UniPathwayUPA00034; UER00017.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00418. DapA.
InterProIPR013785. Aldolase_TIM.
IPR005263. DapA.
IPR002220. DapA-like.
IPR020625. Dihydrodipicolinate_synth_AS.
[Graphical view]
PANTHERPTHR12128. PTHR12128. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFPIRSF001365. DHDPS. 1 hit.
PRINTSPR00146. DHPICSNTHASE.
TIGRFAMsTIGR00674. dapA. 1 hit.
PROSITEPS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPA_BRUSU
AccessionPrimary (citable) accession number: Q8G1R0
Secondary accession number(s): G0K7Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 71 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

Brucella suis

Brucella suis (strain 1330): entries and gene names