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Q2S3M1 (DAPA_SALRD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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:SRU_1080
OrganismSalinibacter ruber (strain DSM 13855 / M31)
Taxonomic identifier309807 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidetes Order II. Incertae sedis › Rhodothermaceae › Salinibacter

Protein attributes

Sequence length302 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
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 – 302302Dihydrodipicolinate synthase HAMAP MF_00418
PRO_0000340986

Regions

Region53 – 542Pyruvate binding By similarity

Sites

Active site1671Schiff-base intermediate with substrate By similarity
Binding site1111Pyruvate By similarity
Site1381Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2S3M1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 4343993695A5C12A

FASTA30231,799
        10         20         30         40         50         60 
MAHDMLFRGV APALVTPFTS DDDIDEAAFR RLIDAQIEGG VSALVVLGTT GENPTITEDE 

        70         80         90        100        110        120 
RRRIVDAALD AADGRVPVIV GTGTNNTDES VAFSKAAVDA GADGLLVVGP YYNKPSQAGF 

       130        140        150        160        170        180 
AAHVETIAAA AEAPIILYNV PGRTSFNIAP ETALHLAEEV PHVAGIKEAS GDIEQIDDLL 

       190        200        210        220        230        240 
AHRPDGFGVY SGDDEMTLPL LAMGGDGAVS VISNALPGPF CELVAAGLDD DLATARDRHA 

       250        260        270        280        290        300 
ELLPAMRACF LETNPVPIKD VCAALGWMEP HVRLPLTPMD ERSPVRQRVL SAFDDLIDVT 


VA

« Hide

References

[1]"The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea."
Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., Legault B., Rodriguez-Valera F.
Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005) [PubMed: 16330755] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13855 / M31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000159 Genomic DNA. Translation: ABC45789.1.
RefSeqYP_445210.1. NC_007677.1.

3D structure databases

HSSPHSSP built from PDB template 1O5K based on UniProtKB Q9X1K9.
ProteinModelPortalQ2S3M1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2S3M1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3852044.
GenomeReviewsGene locus SRU_1080 in contig CP000159_GR.
KEGGsru:SRU_1080.
NMPDRfig|309807.5.peg.1012.
PATRIC23424549. VBISalRub86502_1117.
TIGRSRU_1080.

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHBG358848.
OMAFMLCGGH.
PhylomeDBQ2S3M1.
ProtClustDBCLSK2774978.

Enzyme and pathway databases

BioCycSRUB309807:SRU_1080-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_SALRD
AccessionPrimary (citable) accession number: Q2S3M1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 48 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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