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Q1CR25 (PDXJ_HELPH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:HPAG1_1530
OrganismHelicobacter pylori (strain HPAG1) [Complete proteome] [HAMAP]
Taxonomic identifier357544 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length262 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 – 262262Pyridoxine 5'-phosphate synthase HAMAP-Rule MF_00279
PRO_1000022375

Regions

Region8 – 921-deoxy-D-xylulose 5-phosphate binding By similarity
Region237 – 23823-amino-2-oxopropyl phosphate binding By similarity

Sites

Active site431Proton acceptor By similarity
Active site701Proton acceptor By similarity
Active site2151Proton donor By similarity
Binding site613-amino-2-oxopropyl phosphate By similarity
Binding site1713-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 site10211-deoxy-D-xylulose 5-phosphate By similarity
Binding site21613-amino-2-oxopropyl phosphate; via amide nitrogen By similarity
Site1511Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1CR25 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: CFC43A73505EC354

FASTA26229,663
        10         20         30         40         50         60 
MRFGLNIDHI VTLREIRKTY EPEILEALFI AKNTHKVDLI TIHLREDKRH IQNEDVLRLL 

        70         80         90        100        110        120 
EISPLPINIE CSINVAITDF LCSLKNKPSK VTIVPENRNE VTTEGGLDCS LKGLGEVIRA 

       130        140        150        160        170        180 
YHNKGIEVSL FVDPLKDALH FAKEHQVKQV EFHTGVYANL HNALYSNANN QIHAISALKD 

       190        200        210        220        230        240 
KCPKELKEEL HNAFLQLRRM SKEAFFMGIV VCAGHGLNYT NVKELLKIPS LRELNIGHSV 

       250        260 
VSKAVLVGLE KAILEMAQLI KR 

« Hide

References

[1]"The complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression."
Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HPAG1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000241 Genomic DNA. Translation: ABF85597.1.
RefSeqYP_628271.1. NC_008086.1.

3D structure databases

ProteinModelPortalQ1CR25.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING357544.HPAG1_1530.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF85597; ABF85597; HPAG1_1530.
GeneID4098402.
KEGGhpa:HPAG1_1530.
PATRIC20604533. VBIHelPyl56048_1585.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0854.
HOGENOMHOG000258094.
KOK03474.
OMANFEMAAT.
OrthoDBEOG6M9F0H.
ProtClustDBPRK05265.

Enzyme and pathway databases

BioCycHPYL357544:GH1F-1568-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_HELPH
AccessionPrimary (citable) accession number: Q1CR25
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: February 19, 2014
This is version 52 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