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Reviewed, UniProtKB/Swiss-Prot Q5HUY6 (DAPA_CAMJR)

Last modified November 3, 2009. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydrodipicolinate synthase
      Short name=DHDPS
    EC=4.2.1.52
Gene names
Name: dapA
Ordered Locus Names: CJE0897
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subcellular location

Cytoplasm By similarity.

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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiondihydrodipicolinate synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298Dihydrodipicolinate synthase HAMAP MF_00418
PRO_0000103094

Regions

Region51 – 522Pyruvate 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
Q5HUY6-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: A085BA4D057C19E3

FASTA29832,699
        10         20         30         40         50         60 
MDKNIIIGAM TALITPFKNG KVDEQSYARL IKRQIENGID AVVPVGTTGE SATLTHEEHR 

        70         80         90        100        110        120 
TCIEIAVETC KGTKVKVLAG AGSNATHEAV GLAKFAKEHG ADGILSVVPY YNKPTQQGLY 

       130        140        150        160        170        180 
EHYKAIAQSV DIPVLLYNVP GRTGCEISTD TIIKLFRDCE NIYGVKEASG NIDKCVDLLA 

       190        200        210        220        230        240 
HEPRMMLISG EDAINYPILS NGGKGVISVT SNLLPDMISA LTHFALDENY KEAKKINDEL 

       250        260        270        280        290 
YNINKILFCE SNPIPIKTAM YLAGLIESLE FRLPLCSPSK ENFAKIEEVM KKYKIKGF 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed: 15660156] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000025 Genomic DNA. Translation: AAW35234.1.
RefSeqYP_178899.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HUY6.

Genome annotation databases

GeneID3231410.
GenomeReviewsGene locus CJE0897 in contig CP000025_GR.
KEGGcjr:CJE0897.
TIGRCJE0897.

Phylogenomic databases

HOGENOMQ5HUY6.
OMAVAPRLMH.

Enzyme and pathway databases

BioCycCJEJ195099:CJE_0897-MON.

Family and domain databases

HAMAPMF_00418.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR005263. DapA_synth.
IPR002220. DHDPS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR12128. DHDPS. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PRINTSPR00146. DHPICSNTHASE.
ProDomPD001859. DHDPS. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00674. dapA. 1 hit.
PROSITEPS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPA_CAMJR
AccessionPrimary (citable) accession number: Q5HUY6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 15, 2005
Last modified: November 3, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents