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B1YJ39 (DAPA_EXIS2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:Exig_0487
OrganismExiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15) [Complete proteome] [HAMAP]
Taxonomic identifier262543 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillales Family XII. Incertae Sedis › Exiguobacterium

Protein attributes

Sequence length293 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 – 293293Dihydrodipicolinate synthase HAMAP MF_00418
PRO_1000124035

Regions

Region48 – 492Pyruvate binding By similarity

Sites

Active site1611Schiff-base intermediate with substrate By similarity
Binding site1061Pyruvate By similarity
Site1331Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
B1YJ39 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: C81A0FD3E52FCB85

FASTA29330,723
        10         20         30         40         50         60 
MFKGAGTALA TPFTSTGELD LAVFEQLIEQ QLAANIQALV VGGTTGEGST LTNEEFETLL 

        70         80         90        100        110        120 
ETAIRVTAGR VPVIAGTGTN NTAQTIEKTQ TAARLGADAA MLVTPYYNKT SQAGLVAHFT 

       130        140        150        160        170        180 
AVADAVDLPI MLYNVPSRTG VAISVETAVT LAKHPNIQAF KEASGDVSFM GELMTALPDG 

       190        200        210        220        230        240 
FAVFCGNDDQ ILPYMAWGAQ GVISVLSNPY PAETQALAEA LLANDYTTAR RIQSDLMPVI 

       250        260        270        280        290 
SALFSDVNPI PVKAALEEIG LAVGAPRLPL VRQSEAGHAH LLETMRSYKG VVG

« Hide

References

[1]"Complete sequence of chromosome of Exiguobacterium sibiricum 255-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T., Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17290 / JCM 13490 / 255-15.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001022 Genomic DNA. Translation: ACB59969.1.
RefSeqYP_001812986.1. NC_010556.1.

3D structure databases

ProteinModelPortalB1YJ39.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1YJ39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6174490.
GenomeReviewsGene locus Exig_0487 in contig CP001022_GR.
KEGGesi:Exig_0487.
PATRIC32134505. VBIExiSib53410_0501.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG358848.
OMARTDLAYY.
ProtClustDBCLSK2488979.

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_EXIS2
AccessionPrimary (citable) accession number: B1YJ39
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 27 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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