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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei6 – 613-amino-2-oxopropyl phosphateUniRule annotation
Binding sitei17 – 1713-amino-2-oxopropyl phosphateUniRule annotation
Active sitei41 – 411Proton acceptorUniRule annotation
Binding sitei43 – 4311-deoxy-D-xylulose 5-phosphateUniRule annotation
Binding sitei48 – 4811-deoxy-D-xylulose 5-phosphateUniRule annotation
Active sitei68 – 681Proton acceptorUniRule annotation
Binding sitei98 – 9811-deoxy-D-xylulose 5-phosphateUniRule annotation
Sitei147 – 1471Transition state stabilizerUniRule annotation
Active sitei210 – 2101Proton donorUniRule annotation
Binding sitei211 – 21113-amino-2-oxopropyl phosphate; via amide nitrogenUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pyridoxine biosynthesis

Enzyme and pathway databases

BioCyciCJEJ192222:GJTS-1210-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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257Pyridoxine 5'-phosphate synthasePRO_0000190111Add
BLAST

Proteomic databases

PaxDbiQ9PN59.

Interactioni

Subunit structurei

Homooctamer; tetramer of dimers.UniRule annotation

Protein-protein interaction databases

IntActiQ9PN59. 25 interactions.
STRINGi192222.Cj1238.

Structurei

Secondary structure

1
257
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi8 – 1710Combined sources
Helixi24 – 3411Combined sources
Beta strandi35 – 417Combined sources
Beta strandi47 – 493Combined sources
Helixi51 – 6010Combined sources
Beta strandi65 – 695Combined sources
Helixi73 – 8210Combined sources
Beta strandi85 – 895Combined sources
Helixi94 – 963Combined sources
Beta strandi101 – 1033Combined sources
Helixi110 – 11910Combined sources
Beta strandi123 – 1286Combined sources
Helixi132 – 1409Combined sources
Beta strandi144 – 1485Combined sources
Helixi151 – 16111Combined sources
Helixi164 – 1663Combined sources
Helixi172 – 1743Combined sources
Helixi178 – 20124Combined sources
Beta strandi205 – 2084Combined sources
Turni214 – 2174Combined sources
Helixi218 – 2214Combined sources
Beta strandi228 – 2314Combined sources
Helixi233 – 24210Combined sources
Helixi244 – 25411Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9PN59.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 921-deoxy-D-xylulose 5-phosphate bindingUniRule annotation
Regioni232 – 23323-amino-2-oxopropyl phosphate bindingUniRule annotation

Sequence similaritiesi

Belongs to the PNP synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CSZ. Bacteria.
COG0854. LUCA.
HOGENOMiHOG000258094.
KOiK03474.
OMAiERHIRYQ.
OrthoDBiEOG6M9F0H.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00279. PdxJ.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
3O6CX-ray1.87A1-257[»]
3O6DX-ray1.95A1-257[»]
ProteinModelPortaliQ9PN59.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9PN59. 25 interactions.
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.
OrthoDBiEOG6M9F0H.

Enzyme and pathway databases

UniPathwayiUPA00244; UER00313.
BioCyciCJEJ192222:GJTS-1210-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9PN59.

Family and domain databases

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

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700819 / NCTC 11168.

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: January 20, 2016
This is version 90 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.