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C7BJY6 (C7BJY6_PHOAA) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate By similarity. HAMAP-Rule MF_00102 SAAS SAAS023940

Catalytic activity

(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H + H+. HAMAP-Rule MF_00102 SAAS SAAS023940

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. HAMAP-Rule MF_00102 SAAS SAAS023940

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00102

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00102 SAAS SAAS023940.

Sequence similarities

Belongs to the DapB family. HAMAP-Rule MF_00102

Caution

Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli (PubMed:20503968) that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction. HAMAP-Rule MF_00102

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding12 – 176NAD(P) By similarity HAMAP-Rule MF_00102
Nucleotide binding102 – 1043NAD(P) By similarity HAMAP-Rule MF_00102
Nucleotide binding126 – 1294NAD(P) By similarity HAMAP-Rule MF_00102
Region169 – 1702Substrate binding By similarity HAMAP-Rule MF_00102

Sites

Active site1591Proton donor/acceptor By similarity HAMAP-Rule MF_00102
Active site1631Proton donor By similarity HAMAP-Rule MF_00102
Binding site381NAD By similarity HAMAP-Rule MF_00102
Binding site391NADP By similarity HAMAP-Rule MF_00102
Binding site1601Substrate By similarity HAMAP-Rule MF_00102

Sequences

Sequence LengthMass (Da)Tools
C7BJY6 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: 9C657FA42BE8EEB5

FASTA27328,957
        10         20         30         40         50         60 
MADTDIRVAI VGAGGRMGRQ LIQAVHQLSG VVLGVALERS GSSLLGTDAG ELAGIGHIGV 

        70         80         90        100        110        120 
TVCDDLKNVV DDFDVLIDFT RPEGTLAHLE ICRRHSKAIV IGTTGFDDEG KQAIKDASAN 

       130        140        150        160        170        180 
IPIVFAANFS VGVNLVLKLL EKAAKVMGEY TDIEIIEAHH RHKVDAPSGT ALAMGESIAH 

       190        200        210        220        230        240 
ALGRDLKECA VYAREGYTGE RDPKSIGFAT IRAGDIVGEH TAMFADVGER VEITHKASSR 

       250        260        270 
MTFANGAVKA ALWLNGKNSG LFTMKDVLNL DLI

« Hide

References

[1]"Comparative genomics of the emerging human pathogen Photorhabdus asymbiotica with the insect pathogen Photorhabdus luminescens."
Wilkinson P., Waterfield N.R., Crossman L., Corton C., Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L., Doggett J., Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Arrowsmith C., Churcher C., Harris D. expand/collapse author list , Thompson N.R., Quail M., Parkhill J., Ffrench-Constant R.H.
BMC Genomics 10:302-302(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43949 / 3105-77.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM162591 Genomic DNA. Translation: CAQ82652.1.
RefSeqYP_003039397.1. NC_012962.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING291112.PAU_00560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ82652; CAQ82652; PAU_00560.
GeneID13863305.
KEGGpay:PAU_00560.
PATRIC20494709. VBIPhoAsy71438_0644.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000227153.
KOK00215.
OMAIVMAPNM.
ProtClustDBPRK00048.

Enzyme and pathway databases

BioCycPASY291112:GJQ0-577-MONOMER.
UniPathwayUPA00034; UER00018.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00102. DapB.
InterProIPR022663. DapB_C.
IPR000846. DapB_N.
IPR022664. DapB_N_CS.
IPR011770. Dihydrodipicolinate_Rdtase.
IPR023940. Dihydrodipicolinate_Rdtase_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR20836. PTHR20836. 1 hit.
PfamPF05173. DapB_C. 1 hit.
PF01113. DapB_N. 1 hit.
[Graphical view]
PIRSFPIRSF000161. DHPR. 1 hit.
TIGRFAMsTIGR00036. dapB. 1 hit.
PROSITEPS01298. DAPB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC7BJY6_PHOAA
AccessionPrimary (citable) accession number: C7BJY6
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info