Skip Header

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

B3EH29 (DAPA_CHLL2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. 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
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:Clim_0622
OrganismChlorobium limicola (strain DSM 245 / NBRC 103803) [Complete proteome] [HAMAP]
Taxonomic identifier290315 [NCBI]
Taxonomic lineageBacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobium/Pelodictyon group › Chlorobium

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_1000124021

Regions

Region52 – 532Pyruvate binding By similarity

Sites

Active site1661Schiff-base intermediate with substrate By similarity
Binding site1101Pyruvate By similarity
Site1371Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
B3EH29 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: F105BE73DA3C03D2

FASTA29632,025
        10         20         30         40         50         60 
MSTRLISGSA VALVTPFRQD CSVDTVALRQ LVRFHIAAGT DIIIPCGTTG ESPTLSMEEQ 

        70         80         90        100        110        120 
SRIIRTVKEE AGEQIMVAAG AGTNATDHAV ELAKNAEKAG ASAILSVAPY YNKPSQEGIY 

       130        140        150        160        170        180 
QHYARIAEAV SVPIIIYNVP GRTGSNVAAS TILRLARDFG NIAAVKEASD NMAQITELLE 

       190        200        210        220        230        240 
ERPENFSVLT GEDMLILPFM AMGGDGVISV AANQVPSAVK RLVEAARTGR LDEARAINTR 

       250        260        270        280        290 
YRRLFRLNFI ESNPVPVKYA LALMGMIEEV YRLPLVPLAD ENKRILKEEL QSLGLV

« Hide

References

[1]"Complete sequence of Chlorobium limicola DSM 245."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 245 / NBRC 103803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001097 Genomic DNA. Translation: ACD89709.1.
RefSeqYP_001942688.1. NC_010803.1.

3D structure databases

ProteinModelPortalB3EH29.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3EH29.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6354070.
GenomeReviewsGene locus Clim_0622 in contig CP001097_GR.
KEGGcli:Clim_0622.
PATRIC21373243. VBIChlLim118737_0664.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG358848.
OMAITRELCG.
ProtClustDBPRK03170.

Family and domain databases

HAMAPMF_00418. DapA.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR002220. Dihydrodipicolinate_synth-like.
IPR020625. Dihydrodipicolinate_synth_AS.
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. False negative.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPA_CHLL2
AccessionPrimary (citable) accession number: B3EH29
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 22, 2008
Last modified: January 25, 2012
This is version 26 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents