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B3PTB6 (B3PTB6_RHIE6) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyridoxine 5'-phosphate synthase HAMAP-Rule MF_00279

Short name=PNP synthase HAMAP-Rule MF_00279
EC=2.6.99.2 HAMAP-Rule MF_00279
Gene names
Name:pdxJ HAMAP-Rule MF_00279 EMBL ACE91861.1
Ordered Locus Names:RHECIAT_CH0002911 EMBL ACE91861.1
OrganismRhizobium etli (strain CIAT 652) [Complete proteome] [HAMAP] EMBL ACE91861.1
Taxonomic identifier491916 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length250 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 SAAS SAAS004569

Catalytic activity

1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2 H2O. HAMAP-Rule MF_00279 SAAS SAAS004569

Pathway

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5. HAMAP-Rule MF_00279 SAAS SAAS004569

Subunit structure

Homooctamer; tetramer of dimers By similarity. HAMAP-Rule MF_00279 SAAS SAAS004569

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00279 SAAS SAAS004569.

Sequence similarities

Belongs to the PNP synthase family. HAMAP-Rule MF_00279

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region223 – 22423-amino-2-oxopropyl phosphate binding By similarity HAMAP-Rule MF_00279

Sites

Active site441Proton acceptor By similarity HAMAP-Rule MF_00279
Active site761Proton acceptor By similarity HAMAP-Rule MF_00279
Active site2001Proton donor By similarity HAMAP-Rule MF_00279
Binding site813-amino-2-oxopropyl phosphate By similarity HAMAP-Rule MF_00279
Binding site1913-amino-2-oxopropyl phosphate By similarity HAMAP-Rule MF_00279
Binding site4611-deoxy-D-xylulose 5-phosphate By similarity HAMAP-Rule MF_00279
Binding site5111-deoxy-D-xylulose 5-phosphate By similarity HAMAP-Rule MF_00279
Binding site10611-deoxy-D-xylulose 5-phosphate By similarity HAMAP-Rule MF_00279
Binding site20113-amino-2-oxopropyl phosphate; via amide nitrogen By similarity HAMAP-Rule MF_00279
Site1591Transition state stabilizer By similarity HAMAP-Rule MF_00279

Sequences

Sequence LengthMass (Da)Tools
B3PTB6 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: FDBB6579B350E8FC

FASTA25026,651
        10         20         30         40         50         60 
MPAKLSVNLN AIAMLRNRRD LPWPSVEALG RIALAAGASG LTVHPRPDQR HIRFSDLPVI 

        70         80         90        100        110        120 
RNLIDDEFPN AEFNIEGYPT AEFLDLCAGA APEQVTLVPD DPSQATSDHG WDFRKHQAFL 

       130        140        150        160        170        180 
TDVVGRLKTM GCRVSLFADG DGDAQAVTIA KAVGADRIEL YTGPYGGCYD APERAAPILE 

       190        200        210        220        230        240 
ALGKTADAAL AIGLAVNAGH DLTVANLPAL VKRIPDLAEV SIGHGLTADA LEYGMAETVR 

       250 
RFCRACGQVV 

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References

[1]"Genome diversity and DNA divergence of Rhizobium etli."
Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J., Palacios R., Davila G.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CIAT 652 EMBL ACE91861.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001074 Genomic DNA. Translation: ACE91861.1.
RefSeqYP_001979039.1. NC_010994.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING491916.RHECIAT_CH0002911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE91861; ACE91861; RHECIAT_CH0002911.
GeneID6400998.
KEGGrec:RHECIAT_CH0002911.
PATRIC23099307. VBIRhiEtl120572_2886.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0854.
HOGENOMHOG000258095.
KOK03474.
OMAVRRFCRA.
ProtClustDBPRK05265.

Enzyme and pathway databases

BioCycRETL491916:GH4T-4663-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.
ProtoNetSearch...

Entry information

Entry nameB3PTB6_RHIE6
AccessionPrimary (citable) accession number: B3PTB6
Entry history
Integrated into UniProtKB/TrEMBL: September 2, 2008
Last sequence update: September 2, 2008
Last modified: May 1, 2013
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)