PDX2_PLABE
ID PDX2_PLABE Reviewed; 226 AA.
AC Q4PJX5;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit Pdx2;
DE EC=4.3.3.6 {ECO:0000269|PubMed:22244765};
DE AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit;
DE EC=3.5.1.2 {ECO:0000269|PubMed:22244765};
GN Name=pdx2 {ECO:0000303|PubMed:16339145};
OS Plasmodium berghei.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=5821;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NK65;
RX PubMed=16339145; DOI=10.1074/jbc.m508696200;
RA Gengenbacher M., Fitzpatrick T.B., Raschle T., Flicker K., Sinning I.,
RA Muller S., Macheroux P., Tews I., Kappes B.;
RT "Vitamin B6 biosynthesis by the malaria parasite Plasmodium falciparum:
RT biochemical and structural insights.";
RL J. Biol. Chem. 281:3633-3641(2006).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=NK65;
RX PubMed=22244765; DOI=10.1016/j.str.2011.11.015;
RA Guedez G., Hipp K., Windeisen V., Derrer B., Gengenbacher M., Bottcher B.,
RA Sinning I., Kappes B., Tews I.;
RT "Assembly of the eukaryotic PLP-synthase complex from Plasmodium and
RT activation of the Pdx1 enzyme.";
RL Structure 20:172-184(2012).
CC -!- FUNCTION: Catalyzes the hydrolysis of glutamine to glutamate and
CC ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The
CC resulting ammonia molecule is channeled to the active site of PdxS.
CC {ECO:0000269|PubMed:22244765}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate +
CC L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-
CC phosphate; Xref=Rhea:RHEA:31507, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:58359, ChEBI:CHEBI:59776,
CC ChEBI:CHEBI:597326; EC=4.3.3.6;
CC Evidence={ECO:0000269|PubMed:22244765};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000269|PubMed:22244765};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of heterodimers.
CC Only shows activity in the heterodimer. {ECO:0000250|UniProtKB:Q8IIK4}.
CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ077732; AAY83290.1; -; mRNA.
DR AlphaFoldDB; Q4PJX5; -.
DR SMR; Q4PJX5; -.
DR MEROPS; C26.A35; -.
DR VEuPathDB; PlasmoDB:PBANKA_0931800; -.
DR HOGENOM; CLU_069674_0_0_1; -.
DR OMA; VFIRAPI; -.
DR UniPathway; UPA00245; -.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002161; PdxT/SNO.
DR InterPro; IPR021196; PdxT/SNO_CS.
DR PANTHER; PTHR31559; PTHR31559; 1.
DR Pfam; PF01174; SNO; 1.
DR PIRSF; PIRSF005639; Glut_amidoT_SNO; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR03800; PLP_synth_Pdx2; 1.
DR PROSITE; PS01236; PDXT_SNO_1; 1.
DR PROSITE; PS51130; PDXT_SNO_2; 1.
PE 1: Evidence at protein level;
KW Glutamine amidotransferase; Hydrolase; Lyase; Pyridoxal phosphate.
FT CHAIN 1..226
FT /note="Pyridoxal 5'-phosphate synthase subunit Pdx2"
FT /id="PRO_0000431779"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT ACT_SITE 199
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT ACT_SITE 201
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT BINDING 52..54
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT BINDING 124
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT BINDING 156..157
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P37528"
SQ SEQUENCE 226 AA; 25675 MW; 590F133D8417E3B4 CRC64;
MEKLTIGVLS LQGNFQSHIN HFLQLQNPSL KVIEVRNKTN LRECDGIVIP GGESTTLRKC
MSYDNDSLYN ALKNYIHVKK KPVWGTCAGC ILLSEKVEKN KDDNIENEYG NDFSLGGLDI
EITRNYYGSQ NDSFICSLDI KSQDPIFKKN IRAPCIRAPF IKKISSDKVV TIATFSHESF
GKNIIGAVEQ DNCMGTIFHP ELMPYTCFHD YFLEKVKKHI KDSREA
