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Reviewed, UniProtKB/Swiss-Prot Q6G468 (DAPA_BARHE)

Last modified February 9, 2010. Version 41. 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: BH05000
OrganismBartonella henselae (Rochalimaea henselae) [Complete proteome] [HAMAP]
Taxonomic identifier38323 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length294 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: 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 – 294294Dihydrodipicolinate synthase HAMAP MF_00418
PRO_1000050166

Regions

Region48 – 492Pyruvate binding By similarity

Sites

Active site1621Schiff-base intermediate with substrate By similarity
Binding site1061Pyruvate By similarity
Site1331Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G468-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: CDD074F2CDE871AE

FASTA29431,483
        10         20         30         40         50         60 
MLKGAVTALI TPFDDNGAID EKAFCNFVEW QITQGINGVS PVGTTGESPT LTHEEHKRII 

        70         80         90        100        110        120 
ELCVEQVAKR VPVVAGAGSN STSEAVELAK HAEKAGADAV LVVTPYYNRP NQRGLYTHFS 

       130        140        150        160        170        180 
SIAKAISIPI IIYNIPSRSV IDMAVETMRD LCRDFKNIIG VKDATGKIER ASEQREKCGK 

       190        200        210        220        230        240 
DFVQLSGDDC TALGFNAHGG VGCISVSSNV APKLCAQLHA ACLCSDYKTA LKLNDLLMPL 

       250        260        270        280        290 
NRAVFIEPSP AGIKYAAAKL GLCGTIVRSP IVPLSDTTKK IIDEALYHAG LLKE 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49882 / Houston 1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897699 Genomic DNA. Translation: CAF27308.1.
RefSeqYP_033336.1.

3D structure databases

HSSPHSSP built from PDB template 2A6N based on UniProtKB P0A6L2.
SMRQ6G468. Positions 1-288.
ModBaseSearch...

Genome annotation databases

GeneID2864503.
GenomeReviewsGene locus BH05000 in contig BX897699_GR.
KEGGbhe:BH05000.
NMPDRfig|283166.1.peg.464.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG358848.
OMAIYNIPPR.
PhylomeDBQ6G468.

Enzyme and pathway databases

BioCycBHEN283166:BH05000-MONOMER.
BRENDA4.2.1.52. 277357.

Family and domain databases

HAMAPMF_00418. DapA.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR005263. DapA_synth.
IPR002220. Dihydrodipicolinate_synth.
IPR020625. Dihydrodipicolinate_synth_AS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR12128. DHDPS. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PRINTSPR00146. DHPICSNTHASE.
TIGRFAMsTIGR00674. dapA. 1 hit.
PROSITEPS00665. DHDPS_1. False negative.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPA_BARHE
AccessionPrimary (citable) accession number: Q6G468
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2004
Last modified: February 9, 2010
This is version 41 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