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A0PZM3 (DAPA_CLONN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. 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:
Dihydrodipicolinate synthase

Short name=DHDPS
EC=4.2.1.52
Gene names
Name:dapA
Ordered Locus Names:NT01CX_1746
OrganismClostridium novyi (strain NT) [Complete proteome] [HAMAP]
Taxonomic identifier386415 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2 H2O. HAMAP MF_00418

Pathway

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

Subunit structure

Homotetramer By similarity. HAMAP MF_00418

Subcellular location

Cytoplasm By similarity HAMAP MF_00418.

Sequence similarities

Belongs to the DHDPS family.

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-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydrodipicolinate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 296296Dihydrodipicolinate synthase HAMAP MF_00418
PRO_1000050178

Regions

Region49 – 502Pyruvate binding By similarity

Sites

Active site1621Schiff-base intermediate with substrate By similarity
Binding site1071Pyruvate By similarity
Site1341Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PZM3 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: B3A608F8D39F3540

FASTA29632,585
        10         20         30         40         50         60 
MTLFKGSGVA LVTPFKDGKV NFKKLEEILN WHVECGTDAI IVCGTTGEAS TMTEEERKET 

        70         80         90        100        110        120 
IKFTVDTINK RIPVIAGTGS NNTEAAIKMS KWAESIGVDG VLVITPYYNK TTQKGIFEHF 

       130        140        150        160        170        180 
KAINDSINIP IVLYNVPSRT GLNITPKTLL KLCDLNNVVA IKEASGNFSQ LVEMKALCRD 

       190        200        210        220        230        240 
KIDLYSGNDD QVVPLLSLGG IGVISVAANI YPKEMHDICD LYMNGKTHEA LKIQLDMLDV 

       250        260        270        280        290 
INSLFIETNP IPIKTAMNLK GMDVGALRLP LCDMEENNLE VLKNALENYN KTSREA 

« Hide

References

[1]"The genome and transcriptomes of the anti-tumor agent Clostridium novyi-NT."
Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B., Zhou S.
Nat. Biotechnol. 24:1573-1580(2006) [PubMed: 17115055] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000382 Genomic DNA. Translation: ABK61511.1.
RefSeqYP_877825.1. NC_008593.1.

3D structure databases

ProteinModelPortalA0PZM3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0PZM3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4540644.
GenomeReviewsGene locus NT01CX_1746 in contig CP000382_GR.
KEGGcno:NT01CX_1746.
PATRIC19479156. VBICloNov112828_0854.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHBG358848.
OMACEMEDSN.
ProtClustDBPRK03170.

Enzyme and pathway databases

BioCycCNOV386415:NT01CX_1746-MONOMER.

Family and domain databases

HAMAPMF_00418. DapA.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR002220. Dihydrodipicolinate_synth-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR020624. Dihydrodipicolinate_synth_CS.
IPR005263. Dihydrodipicolinate_synth_DapA.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK01714.
PANTHERPTHR12128. DHDPS. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFPIRSF001365. DHDPS. 1 hit.
PRINTSPR00146. DHPICSNTHASE.
TIGRFAMsTIGR00674. DapA. 1 hit.
PROSITEPS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPA_CLONN
AccessionPrimary (citable) accession number: A0PZM3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families