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Protein

Pyridoxine 5'-phosphate synthase

Gene

pdxJ

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2 H2O.UniRule annotation

Pathwayi: pyridoxine 5'-phosphate biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Phosphoserine aminotransferase (serC)
  4. 4-hydroxythreonine-4-phosphate dehydrogenase (pdxA)
  5. Pyridoxine 5'-phosphate synthase (pdxJ)
This subpathway is part of the pathway pyridoxine 5'-phosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate, the pathway pyridoxine 5'-phosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei63-amino-2-oxopropyl phosphateUniRule annotation1
Binding sitei173-amino-2-oxopropyl phosphateUniRule annotation1
Active sitei41Proton acceptorUniRule annotation1
Binding sitei431-deoxy-D-xylulose 5-phosphateUniRule annotation1
Binding sitei481-deoxy-D-xylulose 5-phosphateUniRule annotation1
Active sitei68Proton acceptorUniRule annotation1
Binding sitei981-deoxy-D-xylulose 5-phosphateUniRule annotation1
Sitei147Transition state stabilizerUniRule annotation1
Active sitei210Proton donorUniRule annotation1
Binding sitei2113-amino-2-oxopropyl phosphate; via amide nitrogenUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pyridoxine biosynthesis

Enzyme and pathway databases

BioCyciCJEJ192222:GJTS-1166-MONOMER.
UniPathwayiUPA00244; UER00313.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxine 5'-phosphate synthaseUniRule annotation (EC:2.6.99.2UniRule annotation)
Short name:
PNP synthaseUniRule annotation
Gene namesi
Name:pdxJUniRule annotation
Ordered Locus Names:Cj1238
OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Taxonomic identifieri192222 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
Proteomesi
  • UP000000799 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001901111 – 257Pyridoxine 5'-phosphate synthaseAdd BLAST257

Proteomic databases

PaxDbiQ9PN59.

Interactioni

Subunit structurei

Homooctamer; tetramer of dimers.UniRule annotation

Protein-protein interaction databases

IntActiQ9PN59. 25 interactors.
STRINGi192222.Cj1238.

Structurei

Secondary structure

1257
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Helixi8 – 17Combined sources10
Helixi24 – 34Combined sources11
Beta strandi35 – 41Combined sources7
Beta strandi47 – 49Combined sources3
Helixi51 – 60Combined sources10
Beta strandi65 – 69Combined sources5
Helixi73 – 82Combined sources10
Beta strandi85 – 89Combined sources5
Helixi94 – 96Combined sources3
Beta strandi101 – 103Combined sources3
Helixi110 – 119Combined sources10
Beta strandi123 – 128Combined sources6
Helixi132 – 140Combined sources9
Beta strandi144 – 148Combined sources5
Helixi151 – 161Combined sources11
Helixi164 – 166Combined sources3
Helixi172 – 174Combined sources3
Helixi178 – 201Combined sources24
Beta strandi205 – 208Combined sources4
Turni214 – 217Combined sources4
Helixi218 – 221Combined sources4
Beta strandi228 – 231Combined sources4
Helixi233 – 242Combined sources10
Helixi244 – 254Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3O6CX-ray1.87A1-257[»]
3O6DX-ray1.95A1-257[»]
ProteinModelPortaliQ9PN59.
SMRiQ9PN59.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9PN59.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni8 – 91-deoxy-D-xylulose 5-phosphate bindingUniRule annotation2
Regioni232 – 2333-amino-2-oxopropyl phosphate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the PNP synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CSZ. Bacteria.
COG0854. LUCA.
HOGENOMiHOG000258094.
KOiK03474.
OMAiERHIRYQ.

Family and domain databases

CDDicd00003. PNPsynthase. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00279. PdxJ. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR004569. PyrdxlP_synth_PdxJ.
[Graphical view]
PfamiPF03740. PdxJ. 1 hit.
[Graphical view]
SUPFAMiSSF63892. SSF63892. 1 hit.
TIGRFAMsiTIGR00559. pdxJ. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9PN59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLGVNIDHI AVLRQARMVN DPDLLEAAFI VARHGDQITL HVREDRRHAQ
60 70 80 90 100
DFDLENIIKF CKSPVNLECA LNDEILNLAL KLKPHRVTLV PEKREELTTE
110 120 130 140 150
GGLCLNHAKL KQSIEKLQNA NIEVSLFINP SLEDIEKSKI LKAQFIELHT
160 170 180 190 200
GHYANLHNAL FSNISHTAFA LKELDQDKKT LQAQFEKELQ NLELCAKKGL
210 220 230 240 250
ELGLKVAAGH GLNYKNVKPV VKIKEICELN IGQSIVARSV FTGLQNAILE

MKELIKR
Length:257
Mass (Da):29,011
Last modified:October 1, 2000 - v1
Checksum:i19C480DA3B96012F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35353.1.
PIRiH81330.
RefSeqiWP_002853163.1. NC_002163.1.
YP_002344629.1. NC_002163.1.

Genome annotation databases

EnsemblBacteriaiCAL35353; CAL35353; Cj1238.
GeneIDi905529.
KEGGicje:Cj1238.
PATRICi20059436. VBICamJej33762_1220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35353.1.
PIRiH81330.
RefSeqiWP_002853163.1. NC_002163.1.
YP_002344629.1. NC_002163.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3O6CX-ray1.87A1-257[»]
3O6DX-ray1.95A1-257[»]
ProteinModelPortaliQ9PN59.
SMRiQ9PN59.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9PN59. 25 interactors.
STRINGi192222.Cj1238.

Proteomic databases

PaxDbiQ9PN59.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL35353; CAL35353; Cj1238.
GeneIDi905529.
KEGGicje:Cj1238.
PATRICi20059436. VBICamJej33762_1220.

Phylogenomic databases

eggNOGiENOG4105CSZ. Bacteria.
COG0854. LUCA.
HOGENOMiHOG000258094.
KOiK03474.
OMAiERHIRYQ.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00313.
BioCyciCJEJ192222:GJTS-1166-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9PN59.

Family and domain databases

CDDicd00003. PNPsynthase. 1 hit.
Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00279. PdxJ. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR004569. PyrdxlP_synth_PdxJ.
[Graphical view]
PfamiPF03740. PdxJ. 1 hit.
[Graphical view]
SUPFAMiSSF63892. SSF63892. 1 hit.
TIGRFAMsiTIGR00559. pdxJ. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPDXJ_CAMJE
AccessioniPrimary (citable) accession number: Q9PN59
Secondary accession number(s): Q0P918
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.