Skip Header

Contribute Send feedback
Read comments (?) or add your own

F0SDL3 (F0SDL3_PEDSD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 18. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. SAAS SAAS005263 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 SAAS SAAS005263

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. HAMAP-Rule MF_00418 SAAS SAAS005263

Subunit structure

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00418 SAAS SAAS005263.

Sequence similarities

Belongs to the DapA family. HAMAP-Rule MF_00418

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 (PubMed:8993314 and PubMed:20503968) 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 (PubMed:20503968). HAMAP-Rule MF_00418

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential EMBL ADY50740.1
Chain20 – 292273 Potential EMBL ADY50740.1
PRO_5000720397

Sites

Active site1351Proton donor/acceptor By similarity HAMAP-Rule MF_00418
Active site1641Schiff-base intermediate with substrate By similarity HAMAP-Rule MF_00418
Binding site471Pyruvate By similarity HAMAP-Rule MF_00418
Binding site2061Pyruvate; via carbonyl oxygen By similarity HAMAP-Rule MF_00418
Site461Part of a proton relay during catalysis By similarity HAMAP-Rule MF_00418
Site1091Part of a proton relay during catalysis By similarity HAMAP-Rule MF_00418

Sequences

Sequence LengthMass (Da)Tools
F0SDL3 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 871A8139E06C7B61

FASTA29231,574
        10         20         30         40         50         60 
MSRFLGTGVA MVTPFQANGS IDFDGLAATI EHLINGKVEY IVVLGTTAES ATLSKDEKKQ 

        70         80         90        100        110        120 
VFKFVTERVN GRIPLVAGIG GNNTTEVVAE VNQFEMVGYE AILSVVPYYN KPTQEGIYQH 

       130        140        150        160        170        180 
YKSIAQAAKL PIILYNVPGR TGVSMSAETT IRLAREFKNI IATKEASGSF DQFNAIMADK 

       190        200        210        220        230        240 
PEGFELISGD DPITLPMVAL GAIGVISVVG NAFPVKFSEM VRLSLNGDFK AARPLHSSFL 

       250        260        270        280        290 
EFTRLCFVES NPCGVKAAMK ELGIIEDYVR LPLTPIGDST RAKVVAEVAK LK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002545 Genomic DNA. Translation: ADY50740.1.
RefSeqYP_004272562.1. NC_015177.1.

3D structure databases

ProteinModelPortalF0SDL3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADY50740; ADY50740; Pedsa_0154.
GeneID10229685.
KEGGpsn:Pedsa_0154.
PATRIC47000875. VBIPedSal163994_0162.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01714.
OMAGQILWFE.

Enzyme and pathway databases

BioCycPSAL762903:GHB2-155-MONOMER.
UniPathwayUPA00034; UER00017.

Family and domain databases

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

Entry information

Entry nameF0SDL3_PEDSD
AccessionPrimary (citable) accession number: F0SDL3
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: May 1, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info