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P19808 (DAPA_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:Cgl1971, cg2161
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length301 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 term3D-structure
Complete proteome
Reference 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 – 301301Dihydrodipicolinate synthase HAMAP MF_00418
PRO_0000103109

Regions

Region60 – 612Pyruvate binding By similarity

Sites

Active site1731Schiff-base intermediate with substrate By similarity
Binding site1181Pyruvate By similarity
Site1451Involved in proton transfer during cleavage By similarity

Experimental info

Sequence conflict2661L → S in CAA37940. Ref.1

Secondary structure

1 .......................................... 301
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19808 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: 6B803A4E829393B3

FASTA30131,262
        10         20         30         40         50         60 
MSTGLTAKTG VEHFGTVGVA MVTPFTESGD IDIAAGREVA AYLVDKGLDS LVLAGTTGES 

        70         80         90        100        110        120 
PTTTAAEKLE LLKAVREEVG DRAKLIAGVG TNNTRTSVEL AEAAASAGAD GLLVVTPYYS 

       130        140        150        160        170        180 
KPSQEGLLAH FGAIAAATEV PICLYDIPGR SGIPIESDTM RRLSELPTIL AVKDAKGDLV 

       190        200        210        220        230        240 
AATSLIKETG LAWYSGDDPL NLVWLALGGS GFISVIGHAA PTALRELYTS FEEGDLVRAR 

       250        260        270        280        290        300 
EINAKLSPLV AAQGRLGGVS LAKAALRLQG INVGDPRLPI MAPNEQELEA LREDMKKAGV 


L

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the dapA gene from Corynebacterium glutamicum."
Bonnassie S., Oreglia J., Sicard A.M.
Nucleic Acids Res. 18:6421-6421(1990) [PubMed: 2129555] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[2]"A cluster of three genes (dapA, orf2, and dapB) of Brevibacterium lactofermentum encodes dihydrodipicolinate synthase, dihydrodipicolinate reductase, and a third polypeptide of unknown function."
Pisabarro A., Malumbres M., Mateos L.M., Oguiza J.A., Martin J.F.
J. Bacteriol. 175:2743-2749(1993) [PubMed: 8478336] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13869 / DSMZ 1412 / NCIMB 9567.
[3]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[4]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X53993 Genomic DNA. Translation: CAA37940.1.
Z21502 Genomic DNA. Translation: CAA79714.1.
BA000036 Genomic DNA. Translation: BAB99364.1.
BX927153 Genomic DNA. Translation: CAF20312.1.
PIRC40626.
RefSeqNP_601177.1. NC_003450.3.
YP_226213.1. NC_006958.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CPRX-ray2.20A/B2-301[»]
ProteinModelPortalP19808.
SMRP19808. Positions 12-301.
ModBaseSearch...

2D gel databases

World-2DPAGE0001:P19808.

Proteomic databases

PRIDEP19808.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1019928.
3345490.
GenomeReviewsGene locus Cgl1971 in contig BA000036_GR.
Gene locus cg2161 in contig BX927147_GR.
KEGGcgb:cg2161.
cgl:NCgl1896.
PATRIC21495944. VBICorGlu203724_1908.

Phylogenomic databases

HOGENOMHBG358848.
OMAHGCISVV.
PhylomeDBP19808.
ProtClustDBPRK03170.

Enzyme and pathway databases

BioCycCGLU196627:CG2161-MONOMER.
MetaCyc:MONOMER-6444.

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_CORGL
AccessionPrimary (citable) accession number: P19808
Secondary accession number(s): P40109
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 11, 2002
Last modified: January 25, 2012
This is version 87 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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