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Q6MDD9 (DAPA_PARUW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:pc0686
OrganismProtochlamydia amoebophila (strain UWE25) [Complete proteome] [HAMAP]
Taxonomic identifier264201 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesParachlamydiaceaeCandidatus Protochlamydia

Protein attributes

Sequence length300 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 – 300300Dihydrodipicolinate synthase HAMAP MF_00418
PRO_0000340980

Regions

Region49 – 502Pyruvate binding By similarity

Sites

Active site1621Schiff-base intermediate with substrate By similarity
Binding site1071Pyruvate By similarity
Site1341Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6MDD9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 9914D0A1DAED0492

FASTA30032,755
        10         20         30         40         50         60 
MYLKGLYTAL ITPFTPTGQL DEEGLKKLIQ IQLHHQVDGV VVLGTTGESP TLTQIEKRRI 

        70         80         90        100        110        120 
IEIALEEIQG RIKVIVGTGS YSTQQAIEQT LQAKQMGADA ALIVTPYYNK PTQEGIFKHF 

       130        140        150        160        170        180 
EAINQAVSFP ICLYNIQGRT GQNIQTHTLK RISTLSSIIG VKETSGDINQ IMDVIEAFRQ 

       190        200        210        220        230        240 
SHPNFAILSG DDALTLPMIA LGGHGIISVV SNLVPAAMKS LVNAALNGNF KKARIIHNQL 

       250        260        270        280        290        300 
YSFIKAAFIE TNPIPIKAAL SLSKLPAGSC RLPLCDLSQN HSQKLAQILN ELPQEWISHG 

« Hide

References

[1]"Illuminating the evolutionary history of chlamydiae."
Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U., Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T., Mewes H.-W., Wagner M.
Science 304:728-730(2004) [PubMed: 15073324] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UWE25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX908798 Genomic DNA. Translation: CAF23410.1.
RefSeqYP_007685.1. NC_005861.1.

3D structure databases

HSSPHSSP built from PDB template 1O5K based on UniProtKB Q9X1K9.
ProteinModelPortalQ6MDD9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6MDD9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2780461.
GenomeReviewsGene locus pc0686 in contig BX908798_GR.
KEGGpcu:pc0686.
NMPDRfig|264201.1.peg.686.
PATRIC31996684. VBICanPro72727_0690.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG132040.
HOGENOMHBG358848.
OMACEMEDSN.
PhylomeDBQ6MDD9.

Enzyme and pathway databases

BioCycCPRO264201:PC0686-MONOMER.

Family and domain databases

HAMAPMF_00418. DapA.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR002220. Dihydrodipicolinate_synth-like.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPA_PARUW
AccessionPrimary (citable) accession number: Q6MDD9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 50 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