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Protein

Pyridoxal 5'-phosphate synthase subunit Pdx2

Gene

pdx2

Organism
Plasmodium berghei
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.1 Publication

Catalytic activityi

D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate.1 Publication
L-glutamine + H2O = L-glutamate + NH3.1 Publication

Pathwayi: pyridoxal 5'-phosphate biosynthesis

This protein is involved in the pathway pyridoxal 5'-phosphate biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway pyridoxal 5'-phosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei87NucleophileBy similarity1
Binding sitei124L-glutamineBy similarity1
Active sitei199Charge relay systemBy similarity1
Active sitei201Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Lyase
LigandPyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00245

Protein family/group databases

MEROPSiC26.A35

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxal 5'-phosphate synthase subunit Pdx2 (EC:4.3.3.61 Publication)
Alternative name(s):
Pyridoxal 5'-phosphate synthase glutaminase subunit (EC:3.5.1.21 Publication)
Gene namesi
Name:pdx21 Publication
OrganismiPlasmodium berghei
Taxonomic identifieri5821 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Vinckeia)

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004317791 – 226Pyridoxal 5'-phosphate synthase subunit Pdx2Add BLAST226

Interactioni

Subunit structurei

In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ4PJX5
SMRiQ4PJX5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni52 – 54L-glutamine bindingBy similarity3
Regioni156 – 157L-glutamine bindingBy similarity2

Sequence similaritiesi

Belongs to the glutaminase PdxT/SNO family.Curated

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiKOG3210 Eukaryota
COG0311 LUCA
HOGENOMiHOG000039949

Family and domain databases

Gene3Di3.40.50.880, 1 hit
InterProiView protein in InterPro
IPR029062 Class_I_gatase-like
IPR002161 PdxT/SNO
IPR021196 PdxT/SNO_CS
PANTHERiPTHR31559 PTHR31559, 1 hit
PfamiView protein in Pfam
PF01174 SNO, 1 hit
PIRSFiPIRSF005639 Glut_amidoT_SNO, 1 hit
SUPFAMiSSF52317 SSF52317, 1 hit
TIGRFAMsiTIGR03800 PLP_synth_Pdx2, 1 hit
PROSITEiView protein in PROSITE
PS01236 PDXT_SNO_1, 1 hit
PS51130 PDXT_SNO_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q4PJX5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKLTIGVLS LQGNFQSHIN HFLQLQNPSL KVIEVRNKTN LRECDGIVIP
60 70 80 90 100
GGESTTLRKC MSYDNDSLYN ALKNYIHVKK KPVWGTCAGC ILLSEKVEKN
110 120 130 140 150
KDDNIENEYG NDFSLGGLDI EITRNYYGSQ NDSFICSLDI KSQDPIFKKN
160 170 180 190 200
IRAPCIRAPF IKKISSDKVV TIATFSHESF GKNIIGAVEQ DNCMGTIFHP
210 220
ELMPYTCFHD YFLEKVKKHI KDSREA
Length:226
Mass (Da):25,675
Last modified:July 19, 2005 - v1
Checksum:i590F133D8417E3B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ077732 mRNA Translation: AAY83290.1

Similar proteinsi

Entry informationi

Entry nameiPDX2_PLABE
AccessioniPrimary (citable) accession number: Q4PJX5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 4, 2015
Last sequence update: July 19, 2005
Last modified: November 22, 2017
This is version 43 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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