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

Q65JG7 (Q65JG7_BACLD) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418

Short name=HTPA synthase HAMAP-Rule MF_00418
EC=4.3.3.7 HAMAP-Rule MF_00418
Gene names
Name:dapA1 EMBL AAU40797.1
Synonyms:dapA HAMAP-Rule MF_00418 EMBL AAU23437.2
Ordered Locus Names:BL01208 EMBL AAU23437.2, BLi01902 EMBL AAU40797.1
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP] EMBL AAU40797.1
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

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. SAAS SAAS005263 HAMAP-Rule MF_00418

Catalytic activity

Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O. SAAS SAAS005263 HAMAP-Rule MF_00418

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. SAAS SAAS005263 HAMAP-Rule MF_00418

Subunit structure

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

Subcellular location

Cytoplasm By similarity SAAS SAAS005263 HAMAP-Rule MF_00418.

Sequence similarities

Belongs to the DapA family. PIRNR PIRNR001365 HAMAP-Rule MF_00418

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 (PubMed:8993314 and PubMed:20503968) 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 (PubMed:20503968). HAMAP-Rule MF_00418

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1341Proton donor/acceptor By similarity HAMAP-Rule MF_00418
Active site1621Schiff-base intermediate with substrate By similarity HAMAP-Rule MF_00418
Binding site461Pyruvate By similarity HAMAP-Rule MF_00418
Binding site2041Pyruvate; via carbonyl oxygen By similarity HAMAP-Rule MF_00418
Site451Part of a proton relay during catalysis By similarity HAMAP-Rule MF_00418
Site1081Part of a proton relay during catalysis By similarity HAMAP-Rule MF_00418

Sequences

Sequence LengthMass (Da)Tools
Q65JG7 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 56AC182E3E53BEE5

FASTA28930,917
        10         20         30         40         50         60 
MNFGNIATAM VTPFDKNENI DFQKLSKLID YLLNNGTDSL VVAGTTGESP TLSEEEKVAL 

        70         80         90        100        110        120 
IQYSVKEAAG RAPIIAGTGS NNTKASIKLT KKAEEAGADA VMLVTPYYNK PSQEGMYRHF 

       130        140        150        160        170        180 
RAIAEETSLP VMLYNVPGRT AASLAPETTI RLAEIPNIIA IKEASGDLDA ITKIVAETPE 

       190        200        210        220        230        240 
DFAVYSGDDS LTLPALSVGA RGIVSVASHI IGPEMQEMIK HYTEGNTAQA ALIHQKLLPL 

       250        260        270        280 
MKGLFAAPNP SPLKTALQLK GLDVGSVRLP LIPLNEDERL RLSSLMNGL 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14580 EMBL AAU23437.2 and DSM 13 / ATCC 14580 [Novozymes].
[2]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 EMBL AAU40797.1 and DSM 13 / ATCC 14580 [Goettingen].
[3]Berka R.M., Rey M.W., Ramaiya P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 14580.
[4]Wiegand S., Hertel R., Dietrich S., Volland S., Liesegang H.
Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: DSM 13 EMBL AAU40797.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU23437.2.
AE017333 Genomic DNA. Translation: AAU40797.1.
RefSeqYP_006713278.1. NC_006322.1.
YP_079075.2. NC_006270.3.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL01208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU23437; AAU23437; BL01208.
AAU40797; AAU40797; BLi01902.
GeneID3031112.
3098811.
KEGGbld:BLi01902.
bli:BL01208.
PATRIC18949407. VBIBacLic203714_1907.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHOG000173604.
KOK01714.
OMAMLYSGDD.
OrthoDBEOG6W7235.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-1887-MONOMER.
MetaCyc:MONOMER-6565.
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 nameQ65JG7_BACLD
AccessionPrimary (citable) accession number: Q65JG7
Secondary accession number(s): Q62UX2
Entry history
Integrated into UniProtKB/TrEMBL: October 25, 2004
Last sequence update: October 25, 2004
Last modified: July 9, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)