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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}.
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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
 
 
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