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Q0VP22 (PDXJ_ALCBS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:ABO_1628
OrganismAlcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]
Taxonomic identifier393595 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesAlcanivoracaceaeAlcanivorax

Protein attributes

Sequence length244 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
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 – 244244Pyridoxine 5'-phosphate synthase HAMAP-Rule MF_00279
PRO_1000059228

Regions

Region14 – 1521-deoxy-D-xylulose 5-phosphate binding By similarity
Region218 – 21923-amino-2-oxopropyl phosphate binding By similarity

Sites

Active site481Proton acceptor By similarity
Active site751Proton acceptor By similarity
Active site1961Proton donor By similarity
Binding site1213-amino-2-oxopropyl phosphate By similarity
Binding site2313-amino-2-oxopropyl phosphate By similarity
Binding site5011-deoxy-D-xylulose 5-phosphate By similarity
Binding site5511-deoxy-D-xylulose 5-phosphate By similarity
Binding site10511-deoxy-D-xylulose 5-phosphate By similarity
Binding site19713-amino-2-oxopropyl phosphate; via amide nitrogen By similarity
Site1561Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0VP22 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: CC67C57A7AED532B

FASTA24426,509
        10         20         30         40         50         60 
MSFMSRVLLG VNIDHIATLR QARGTRYPEP VQAALVAEQA GADGITVHLR EDRRHINDRD 

        70         80         90        100        110        120 
VELLAQTLQT RMNLEMAATE EMVVIACRIQ PPHCCLVPEK REELTTEGGL DVVGNKAWIA 

       130        140        150        160        170        180 
QCCQRLGQAG IEVSLFIDAE ESQILAAREC GAPAIEIHTG GYADAQTIDQ QQQELARIRS 

       190        200        210        220        230        240 
AVAFALAQGL IVNAGHGLHY HNTLAIAEIP GINELNIGHS IIARAAITGL DEAVRSMRSL 


LDTV 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286690 Genomic DNA. Translation: CAL17076.1.
RefSeqYP_693348.1. NC_008260.1.

3D structure databases

ProteinModelPortalQ0VP22.
SMRQ0VP22. Positions 5-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393595.ABO_1628.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL17076; CAL17076; ABO_1628.
GeneID4212451.
KEGGabo:ABO_1628.
PATRIC20841055. VBIAlcBor124741_1705.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0854.
HOGENOMHOG000258094.
KOK03474.
OMAVPETRQE.
OrthoDBEOG6M9F0H.

Enzyme and pathway databases

BioCycABOR393595:GHRI-1668-MONOMER.
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_ALCBS
AccessionPrimary (citable) accession number: Q0VP22
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: May 14, 2014
This is version 54 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