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Protein

Pyridoxine 5'-phosphate synthase

Gene

pdxJ

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 sitei73-amino-2-oxopropyl phosphateUniRule annotation1
Binding sitei183-amino-2-oxopropyl phosphateUniRule annotation1
Active sitei43Proton acceptorUniRule annotation1
Binding sitei451-deoxy-D-xylulose 5-phosphateUniRule annotation1
Binding sitei501-deoxy-D-xylulose 5-phosphateUniRule annotation1
Active sitei70Proton acceptorUniRule annotation1
Binding sitei1001-deoxy-D-xylulose 5-phosphateUniRule annotation1
Sitei151Transition state stabilizerUniRule annotation1
Active sitei191Proton donorUniRule annotation1
Binding sitei1923-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

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:CBU_1494
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
Proteomesi
  • UP000002671 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_00002318001 – 240Pyridoxine 5'-phosphate synthaseAdd BLAST240

Proteomic databases

PRIDEiQ83BL1.

Interactioni

Subunit structurei

Homooctamer; tetramer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi227377.CBU_1494.

Structurei

3D structure databases

ProteinModelPortaliQ83BL1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 101-deoxy-D-xylulose 5-phosphate bindingUniRule annotation2
Regioni213 – 2143-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.

Q83BL1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRLGVNIDH IATLRQARGV DYPDPVEAAM MAIEAGADGI TLHLREDRRH
60 70 80 90 100
IQDDDVRNLK RKLTVPMNLE MATAEDIIQF AEEIKPEHCC LVPEKREELT
110 120 130 140 150
TEGGLDVAGQ QNTLKKVCAR LAKVGIEVSL FIDPEEKQID AAKAAGAPVI
160 170 180 190 200
EIHTGHYANA KTDHEHNQQL KRIADAAAYA DSLGLTVNAG HGLTIHNVQS
210 220 230 240
IAAIPVINEL NIGHSIISRG VLIGLAEAVK EMKTLIAGAQ
Length:240
Mass (Da):26,013
Last modified:June 1, 2003 - v1
Checksum:iE15A78207718D673
GO

Sequence cautioni

The sequence AAO90991 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO90991.2. Different initiation.
RefSeqiNP_820477.2. NC_002971.3.
WP_010958266.1. NC_002971.3.

Genome annotation databases

EnsemblBacteriaiAAO90991; AAO90991; CBU_1494.
GeneIDi1209404.
KEGGicbu:CBU_1494.
PATRICi17931753. VBICoxBur82552_1496.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO90991.2. Different initiation.
RefSeqiNP_820477.2. NC_002971.3.
WP_010958266.1. NC_002971.3.

3D structure databases

ProteinModelPortaliQ83BL1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227377.CBU_1494.

Proteomic databases

PRIDEiQ83BL1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO90991; AAO90991; CBU_1494.
GeneIDi1209404.
KEGGicbu:CBU_1494.
PATRICi17931753. VBICoxBur82552_1496.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00244; UER00313.

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_COXBU
AccessioniPrimary (citable) accession number: Q83BL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 83 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

Complete proteome, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.