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Q8DKM1 (PDXJ_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. 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:
Pyridoxine 5'-phosphate synthase

Short name=PNP synthase
EC=2.6.99.2
Gene names
Name:pdxJ
Ordered Locus Names:tlr0838
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate By similarity. HAMAP-Rule MF_00279

Catalytic activity

1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2 H2O. HAMAP-Rule MF_00279

Pathway

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5. HAMAP-Rule MF_00279

Subunit structure

Homooctamer; tetramer of dimers By similarity. HAMAP-Rule MF_00279

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00279.

Sequence similarities

Belongs to the PNP synthase family.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpyridoxine 5'-phosphate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 238238Pyridoxine 5'-phosphate synthase HAMAP-Rule MF_00279
PRO_0000190132

Regions

Region9 – 1021-deoxy-D-xylulose 5-phosphate binding By similarity
Region213 – 21423-amino-2-oxopropyl phosphate binding By similarity

Sites

Active site431Proton acceptor By similarity
Active site701Proton acceptor By similarity
Active site1911Proton donor By similarity
Binding site713-amino-2-oxopropyl phosphate By similarity
Binding site1813-amino-2-oxopropyl phosphate By similarity
Binding site4511-deoxy-D-xylulose 5-phosphate By similarity
Binding site5011-deoxy-D-xylulose 5-phosphate By similarity
Binding site10011-deoxy-D-xylulose 5-phosphate By similarity
Binding site19213-amino-2-oxopropyl phosphate; via amide nitrogen By similarity
Site1511Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DKM1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 6B5C6061C59D65DD

FASTA23825,658
        10         20         30         40         50         60 
MATLGVNIDH VATIRQARRT VEPDPVAAAL LAELGGADGI TVHLREDRRH IQERDVRLLR 

        70         80         90        100        110        120 
QTVRTHLNLE MAATPEMVAI ALDIRPDYVT LVPERREEVT TEGGLDVVSQ QEPLTQVVQT 

       130        140        150        160        170        180 
LQGAGIPVSL FIDADPTQLA AAAKTTAQFI ELHTGRYAEA KGEVAQQREL AILADGVQQA 

       190        200        210        220        230 
KALGLRVNAG HGLTYSNVGA IARLEGIEEL NIGHTIISRA VLVGMVQAVR DMKALISP 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC08390.1.
RefSeqNP_681628.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DKM1.
SMRQ8DKM1. Positions 4-236.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tlr0838.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC08390; BAC08390; BAC08390.
GeneID1011556.
KEGGtel:tlr0838.
PATRIC23926966. VBITheElo119873_0883.

Phylogenomic databases

eggNOGCOG0854.
HOGENOMHOG000258094.
KOK03474.
OMAVPETRQE.
OrthoDBEOG6M9F0H.

Enzyme and pathway databases

UniPathwayUPA00244; UER00313.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00279. PdxJ.
InterProIPR013785. Aldolase_TIM.
IPR004569. PyrdxlP_synth_PdxJ.
[Graphical view]
PfamPF03740. PdxJ. 1 hit.
[Graphical view]
SUPFAMSSF63892. SSF63892. 1 hit.
TIGRFAMsTIGR00559. pdxJ. 1 hit.
ProtoNetSearch...

Entry information

Entry namePDXJ_THEEB
AccessionPrimary (citable) accession number: Q8DKM1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 65 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