Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C6E9Q9 (DAPA_GEOSM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:
4-hydroxy-tetrahydrodipicolinate synthase

Short name=HTPA synthase
EC=4.3.3.7
Gene names
Name:dapA
Ordered Locus Names:GM21_4144
OrganismGeobacter sp. (strain M21) [Complete proteome] [HAMAP]
Taxonomic identifier443144 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length290 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.

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-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 – 2902904-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418
PRO_1000206032

Sites

Active site1321Proton donor/acceptor By similarity
Active site1601Schiff-base intermediate with substrate By similarity
Binding site441Pyruvate By similarity
Binding site2021Pyruvate; via carbonyl oxygen By similarity
Site431Part of a proton relay during catalysis By similarity
Site1061Part of a proton relay during catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
C6E9Q9 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: DAE5F200048602D7

FASTA29031,103
        10         20         30         40         50         60 
MFQGSIVAIV TPFKNGAVDE EKLRELVEFQ IENGTDAIVP CGTTGESSTL SYVEHDRVIQ 

        70         80         90        100        110        120 
VVVEQVNKRV PVIAGTGSNS THEAIEITQH AKELGADGAL LVTPYYNKPS QEGLFRHYKA 

       130        140        150        160        170        180 
VADAVALPQI LYNVPGRTGV NLLPETVARL SVHQNIVAIK EATGSLQQAS EVLALCGDKI 

       190        200        210        220        230        240 
DVLSGDDFIT LPIMAAGGKG VISVTANIMP KEVSSLVDAF NAGNLEEARR LHLYLLKISN 

       250        260        270        280        290 
AMFIESNPVP VKAAVSLMGK CSSEVRLPLA PLMEANLAKL TAIMKEYKLI 

« Hide

References

[1]"Complete sequence of Geobacter sp. M21."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Lovley D.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M21.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001661 Genomic DNA. Translation: ACT20159.1.
RefSeqYP_003023917.1. NC_012918.1.

3D structure databases

ProteinModelPortalC6E9Q9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING443144.GM21_4144.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT20159; ACT20159; GM21_4144.
GeneID8139518.
KEGGgem:GM21_4144.
PATRIC22022718. VBIGeoSp56140_4049.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycGSP443144:GHKM-4220-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_GEOSM
AccessionPrimary (citable) accession number: C6E9Q9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: February 19, 2014
This is version 36 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