Skip Header

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

F4CMF2 (F4CMF2_PSEUX) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 17. 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

Names and origin

Protein namesRecommended name:
4-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418
Short name=HTPA synthase HAMAP-Rule MF_00418
EC=4.3.3.7 HAMAP-Rule MF_00418
Gene names
Name:dapA HAMAP-Rule MF_00418
Ordered Locus Names:Psed_1336 EMBL AEA23579.1
OrganismPseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 / CB1190) [Complete proteome] [HAMAP]
Taxonomic identifier675635 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Pseudonocardia ›

Protein attributes

Sequence length303 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. SAAS SAAS002220 HAMAP-Rule MF_00418

Catalytic activity

Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O. SAAS SAAS002220 HAMAP-Rule MF_00418

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. SAAS SAAS002220 HAMAP-Rule MF_00418

Subunit structure

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

Subcellular location

Cytoplasm By similarity SAAS SAAS020625 HAMAP-Rule MF_00418.

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

Sites

Active site1421Proton donor/acceptor By similarity HAMAP-Rule MF_00418
Active site1711Schiff-base intermediate with substrate By similarity HAMAP-Rule MF_00418
Binding site531Pyruvate By similarity HAMAP-Rule MF_00418
Binding site2131Pyruvate; via carbonyl oxygen By similarity HAMAP-Rule MF_00418
Site521Part of a proton relay during catalysis By similarity HAMAP-Rule MF_00418
Site1151Part of a proton relay during catalysis By similarity HAMAP-Rule MF_00418

Sequences

Sequence LengthMass (Da)Tools
F4CMF2 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 461F1FB2727B6662

FASTA30332,570
        10         20         30         40         50         60 
MKFRTDPARI RGSIAPVVTP FTADGAVDTE SLRGLIRWQL DQGSHGISIG GSTGEPAAQT 

        70         80         90        100        110        120 
AAERIAAIRI TAEEVADAVP FLPGTGSAKL DETLEITAAA REAGADAALV ITPYYARPTQ 

       130        140        150        160        170        180 
DGLVHWYSTV AGEFPDLPIV VYNVPSRTAV DIAPETVARL FREHDNIVGI KETTKDFEHF 

       190        200        210        220        230        240 
SRVLQLCGRD LLVWSGIELL GIPLLALGGV GFISAVANLA PAVVARMYEA WEAGDHEQAR 

       250        260        270        280        290        300 
ELHYALHPLV DLLFVETNPA PAKWALHQQG RISSSHVREP LLPLTAAGQE RVRALLEQGS 


ALL

« Hide

References

[1]"Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans strain CB1190."
Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T., Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A., Alvarez-Cohen L.
J. Bacteriol. 193:4549-4550(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 55486 / DSM 44775 / JCM 13855 / CB1190.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002593 Genomic DNA. Translation: AEA23579.1.
RefSeqYP_004331432.1. NC_015312.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEA23579; AEA23579; Psed_1336.
GeneID10363161.
KEGGpdx:Psed_1336.
PATRIC54394072. VBIPseDio141225_1332.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01714.

Enzyme and pathway databases

BioCycPDIO675635:GHMF-1675-MONOMER.
UniPathwayUPA00034; UER00017.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00418. DapA.
InterProIPR013785. Aldolase_TIM.
IPR002220. Dihydrodipicolinate_synth-like.
IPR020625. Dihydrodipicolinate_synth_AS.
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.
PROSITEPS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF4CMF2_PSEUX
AccessionPrimary (citable) accession number: F4CMF2
Entry history
Integrated into UniProtKB/TrEMBL: June 28, 2011
Last sequence update: June 28, 2011
Last modified: May 1, 2013
This is version 17 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