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A4XJU0 (DAPA_CALS8) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydrodipicolinate synthase
Short name=DHDPS
EC=4.2.1.52
Gene names
Name:dapA
Ordered Locus Names:Csac_1583
OrganismCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]
Taxonomic identifier351627 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor

Protein attributes

Sequence length295 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 – 295295Dihydrodipicolinate synthase HAMAP MF_00418
PRO_1000050170

Regions

Region50 – 512Pyruvate binding By similarity

Sites

Active site1631Schiff-base intermediate with substrate By similarity
Binding site1081Pyruvate By similarity
Site1351Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
A4XJU0 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: B0A8EA0B88F546D0

FASTA29532,539
        10         20         30         40         50         60 
MPIFKGSGVA LITPFKDEES VDFEVLGRLV DFHLEHKTDA IIVCGTTGEP STMPDDEHLE 

        70         80         90        100        110        120 
VIRFVIDRVA GRKPVIAGVG SNHTKHAVYL SKKAQELGAD GLLHVTPYYN KTTQKGLIEH 

       130        140        150        160        170        180 
FKEINDAVSI PIIVYNVPSR TGLNILPETM KELSKLPNIR AIKEASGNIT QVAEIAMLCP 

       190        200        210        220        230        240 
DIDIYSGNDD QIVPVLSVGG IGVISVLANI LPDETHDIVE YFLNGQVEKA KELQLKLLPI 

       250        260        270        280        290 
IKALFIEVNP IPVKEAMNMM GFNVGRPRLP LTTMTEKNRE ILKKALIDYG INIKE

« Hide

References

[1]"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000679 Genomic DNA. Translation: ABP67175.1.
RefSeqYP_001180366.1. NC_009437.1.

3D structure databases

ProteinModelPortalA4XJU0.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4XJU0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5087284.
GenomeReviewsGene locus Csac_1583 in contig CP000679_GR.
KEGGcsc:Csac_1583.
PATRIC21252871. VBICalSac56748_1745.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHBG358848.
OMACEMEDSN.
ProtClustDBCLSK2473146.

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_CALS8
AccessionPrimary (citable) accession number: A4XJU0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: December 14, 2011
This is version 30 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

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