Skip Header

Contribute Send feedback
Read comments (?) or add your own

A5FJ95 (PDXJ_FLAJ1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 41. 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
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:Fjoh_1695
OrganismFlavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae) [Complete proteome] [HAMAP]
Taxonomic identifier376686 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Flavobacterium ›

Protein attributes

Sequence length237 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.

Subcellular location

Cytoplasm By similarity.

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: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpyridoxine 5'-phosphate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 237237Pyridoxine 5'-phosphate synthase HAMAP-Rule MF_00279
PRO_1000078818

Regions

Region213 – 21423-amino-2-oxopropyl phosphate binding By similarity

Sites

Active site431Proton acceptor By similarity
Active site701Proton acceptor By similarity
Active site1901Proton 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 site19113-amino-2-oxopropyl phosphate; via amide nitrogen By similarity
Site1511Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FJ95 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: C7A6869CEF1EC6F5

FASTA23726,351
        10         20         30         40         50         60 
MTKLSVNINK IATLRNARGG NVPDLLKVAA DIQRFGGQGI TIHPRPDERH IRYQDARDLK 

        70         80         90        100        110        120 
AIVTTEYNIE GNPQHNFIDL VLECKPDQVT LVPDAIGAIT SSAGWDTIKN QEYLKEVIQE 

       130        140        150        160        170        180 
FQRNGIRTSI FVDPVLEMIE GAKKTGTDRI ELYTEAFAHQ YDLGNKNGID PYVKAAELAN 

       190        200        210        220        230 
ELGLGINAGH DLSLDNIQFF KQNIPGLLEV SIGHALISEA LYLGLDNVVN MYLKKLK

« Hide

References

[1]"Complete sequence of Flavobacterium johnsoniae UW101."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Xie G., McBride M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17061 / DSM 2064 / UW101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000685 Genomic DNA. Translation: ABQ04727.1.
RefSeqYP_001194046.1. NC_009441.1.

3D structure databases

ProteinModelPortalA5FJ95.
ModBaseSearch...

Protein-protein interaction databases

STRING376686.Fjoh_1695.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ04727; ABQ04727; Fjoh_1695.
GeneID5091154.
KEGGfjo:Fjoh_1695.
PATRIC21897737. VBIFlaJoh53613_1742.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0854.
HOGENOMHOG000258095.
KOK03474.
OMALHYHNVK.
ProtClustDBPRK05265.

Enzyme and pathway databases

BioCycFJOH376686:GIXN-1728-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. PyrdxlP_synth_PdxJ. 1 hit.
TIGRFAMsTIGR00559. pdxJ. 1 hit.
ProtoNetSearch...

Entry information

Entry namePDXJ_FLAJ1
AccessionPrimary (citable) accession number: A5FJ95
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: May 1, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents