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Protein

Pyridoxine 5'-phosphate synthase

Gene

pdxJ

Organism
Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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. Erythronate-4-phosphate dehydrogenase (pdxB)
  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 sitei123-amino-2-oxopropyl phosphateUniRule annotation1
Binding sitei233-amino-2-oxopropyl phosphateUniRule annotation1
Active sitei48Proton acceptorUniRule annotation1
Binding sitei501-deoxy-D-xylulose 5-phosphateUniRule annotation1
Binding sitei551-deoxy-D-xylulose 5-phosphateUniRule annotation1
Active sitei75Proton acceptorUniRule annotation1
Binding sitei1051-deoxy-D-xylulose 5-phosphateUniRule annotation1
Sitei156Transition state stabilizerUniRule annotation1
Active sitei196Proton donorUniRule annotation1
Binding sitei1973-amino-2-oxopropyl phosphate; via amide nitrogenUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processPyridoxine biosynthesis

Enzyme and pathway databases

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:ABO_1628
OrganismiAlcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
Taxonomic identifieri393595 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesAlcanivoracaceaeAlcanivorax
Proteomesi
  • UP000008871 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000592281 – 244Pyridoxine 5'-phosphate synthaseAdd BLAST244

Proteomic databases

PRIDEiQ0VP22

Interactioni

Subunit structurei

Homooctamer; tetramer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi393595.ABO_1628

Structurei

3D structure databases

ProteinModelPortaliQ0VP22
SMRiQ0VP22
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni14 – 151-deoxy-D-xylulose 5-phosphate bindingUniRule annotation2
Regioni218 – 2193-amino-2-oxopropyl phosphate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the PNP synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CSZ Bacteria
COG0854 LUCA
HOGENOMiHOG000258094
KOiK03474
OMAiTSNAGWD
OrthoDBiPOG091H03D1

Family and domain databases

CDDicd00003 PNPsynthase, 1 hit
Gene3Di3.20.20.70, 1 hit
HAMAPiMF_00279 PdxJ, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR004569 PyrdxlP_synth_PdxJ
IPR036130 Pyridoxine-5'_phos_synth
PANTHERiPTHR30456 PTHR30456, 1 hit
PfamiView protein in Pfam
PF03740 PdxJ, 1 hit
SUPFAMiSSF63892 SSF63892, 1 hit
TIGRFAMsiTIGR00559 pdxJ, 1 hit

Sequencei

Sequence statusi: Complete.

Q0VP22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFMSRVLLG VNIDHIATLR QARGTRYPEP VQAALVAEQA GADGITVHLR
60 70 80 90 100
EDRRHINDRD VELLAQTLQT RMNLEMAATE EMVVIACRIQ PPHCCLVPEK
110 120 130 140 150
REELTTEGGL DVVGNKAWIA QCCQRLGQAG IEVSLFIDAE ESQILAAREC
160 170 180 190 200
GAPAIEIHTG GYADAQTIDQ QQQELARIRS AVAFALAQGL IVNAGHGLHY
210 220 230 240
HNTLAIAEIP GINELNIGHS IIARAAITGL DEAVRSMRSL LDTV
Length:244
Mass (Da):26,509
Last modified:September 5, 2006 - v1
Checksum:iCC67C57A7AED532B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM286690 Genomic DNA Translation: CAL17076.1

Genome annotation databases

EnsemblBacteriaiCAL17076; CAL17076; ABO_1628
KEGGiabo:ABO_1628

Similar proteinsi

Entry informationi

Entry nameiPDXJ_ALCBS
AccessioniPrimary (citable) accession number: Q0VP22
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: May 23, 2018
This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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