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Q83CA6 (DAPA_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
4-hydroxy-tetrahydrodipicolinate synthase

Short name=HTPA synthase
EC=4.3.3.7
Gene names
Name:dapA
Ordered Locus Names:CBU_1222
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) By similarity. HAMAP-Rule MF_00418

Catalytic activity

Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O. HAMAP-Rule MF_00418

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. HAMAP-Rule MF_00418

Subunit structure

Homotetramer; dimer of dimers By similarity. HAMAP-Rule MF_00418

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00418.

Sequence similarities

Belongs to the DapA family.

Caution

Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.

Sequence caution

The sequence AAO90731.2 differs from that shown. Reason: Erroneous initiation.

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-HAMAP

lysine biosynthetic process via diaminopimelate

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4-hydroxy-tetrahydrodipicolinate synthase

Inferred from electronic annotation. Source: UniProtKB-EC

amine-lyase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2892894-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418
PRO_1000050182

Sites

Active site1331Proton donor/acceptor By similarity
Active site1611Schiff-base intermediate with substrate By similarity
Binding site451Pyruvate By similarity
Binding site2001Pyruvate; via carbonyl oxygen By similarity
Site441Part of a proton relay during catalysis By similarity
Site1071Part of a proton relay during catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83CA6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: E88266A24A2CEC6F

FASTA28931,613
        10         20         30         40         50         60 
MFNGSLVALV TPMQENGEID YSNLKELVEW HLENDTDGLV ILGTTGESPT ITAEERHKII 

        70         80         90        100        110        120 
RQVVDQVNKK IPIIVGTGAN STVHTIEMTQ QAMELGADAA LIVTPYYNKP TQEGLFQYFK 

       130        140        150        160        170        180 
TIAEAVPIAQ ILYNVPSRTA CDLLPETVIR IAKCSNVVGL KEATGDIQRV KQLKAEDLDL 

       190        200        210        220        230        240 
LSGDDKTAMD FMLAGGKGVI SVVANVVPKP YHAFCITAVS GNVELAKKEN DQLSPLYDSL 

       250        260        270        280 
FVESNPIPVK WALSQMGVIP KGIRLPLTPL SERYHAKVRE SLQQVGIKC 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016828 Genomic DNA. Translation: AAO90731.2. Different initiation.
RefSeqNP_820217.2. NC_002971.3.

3D structure databases

ProteinModelPortalQ83CA6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227377.CBU_1222.

Proteomic databases

PRIDEQ83CA6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO90731; AAO90731; CBU_1222.
GeneID1209127.
KEGGcbu:CBU_1222.
PATRIC17931181. VBICoxBur82552_1215.

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHOG000173604.
KOK01714.
OMAHQKLFVE.
OrthoDBEOG6W7235.
ProtClustDBPRK03170.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-1209-MONOMER.
UniPathwayUPA00034; UER00017.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00418. DapA.
InterProIPR013785. Aldolase_TIM.
IPR005263. DapA.
IPR002220. DapA-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR020624. Dihydrodipicolinate_synth_CS.
[Graphical view]
PANTHERPTHR12128. PTHR12128. 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_COXBU
AccessionPrimary (citable) accession number: Q83CA6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names