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Q71ZN5 (DAPA_LISMF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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

Names and origin

Protein namesRecommended name:
Dihydrodipicolinate synthase

Short name=DHDPS
EC=4.2.1.52
Gene names
Name:dapA
Ordered Locus Names:LMOf2365_1454
OrganismListeria monocytogenes serotype 4b (strain F2365) [Complete proteome] [HAMAP]
Taxonomic identifier265669 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesListeriaceaeListeria

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_0000103124

Regions

Region50 – 512Pyruvate binding By similarity

Sites

Active site1641Schiff-base intermediate with substrate By similarity
Binding site1091Pyruvate By similarity
Site1361Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
Q71ZN5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 78485DDA56B51394

FASTA29331,420
        10         20         30         40         50         60 
MDLGKVITAM VTPIHPEKDK VCKKRIHHLV NHLIKNGSDG LVIAGTTGES PTLSHDEKIK 

        70         80         90        100        110        120 
LFRQVIETND GRAKLIAGTG SNNTAETIAF TKEVAELGGI DAVLIVAPYY NKPNQDGLYA 

       130        140        150        160        170        180 
HFAAVSEASD LPVVIYNIPG RSVVNIEPET IIRLAKLPNI VGVKESSGNL DNISKIIAET 

       190        200        210        220        230        240 
SDDFQVYSGD DSLTLPILAV GGNGVISVAS HVVGNEMQEM IQAFERGEVQ KAAQIHRELL 

       250        260        270        280        290 
PLMNGLFSVP NPAPTKYLLN QQGISVGPVR LPLVDLNAEQ GTKLQAILEG LSK 

« Hide

References

[1]"Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne pathogen Listeria monocytogenes reveal new insights into the core genome components of this species."
Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., Daugherty S.C., Dodson R.J. expand/collapse author list , Durkin A.S., Madupu R., Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O., Luchansky J.B., Fraser C.M.
Nucleic Acids Res. 32:2386-2395(2004) [PubMed: 15115801] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: F2365.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017262 Genomic DNA. Translation: AAT04229.1.
RefSeqYP_014052.1. NC_002973.6.

3D structure databases

ProteinModelPortalQ71ZN5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ71ZN5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2799279.
GenomeReviewsGene locus LMOf2365_1454 in contig AE017262_GR.
KEGGlmf:LMOf2365_1454.
PATRIC20324147. VBILisMon105049_1461.
TIGRLMOf2365_1454.

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHBG358848.
OMACEMEDSN.
PhylomeDBQ71ZN5.
ProtClustDBPRK03170.

Enzyme and pathway databases

BioCycLMON265669:LMOF2365_1454-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_LISMF
AccessionPrimary (citable) accession number: Q71ZN5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 52 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