AC   MF_01615;
DC   Protein; auto
TR   HAMAP; MF_01615; -; 1; level=0
XX
Names: PdxT
XX
ID   PDXT
DE   RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT;
DE            EC=4.3.3.6;
DE   AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit;
DE            EC=3.5.1.2;
DE   AltName: Full=Pdx2;
GN   Name=pdxT;
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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   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate +
CC         L-glutamine = pyridoxal 5'-phosphate + L-glutamate + phosphate + 3
CC         H2O + H(+); 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamine + H2O = 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   -!- 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.
CC   -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
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DR   Pfam; PF01174; SNO; 1; trigger=no
DR   PRINTS; PR00096; GATASE; 1; trigger=no
DR   PROSITE; PS01236; PDXT_SNO_1; 1; trigger=no
DR   PROSITE; PS51130; PDXT_SNO_2; 1; trigger=no
DR   NCBIfam; TIGR03800; PLP_synth_Pdx2; 1; trigger=no
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KW   Glutamine amidotransferase
KW   Pyridoxal phosphate
KW   Hydrolase
KW   Lyase
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GO   GO:0004359; F:glutaminase activity
GO   GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity
GO   GO:0006543; P:L-glutamine catabolic process
GO   GO:0042823; P:pyridoxal phosphate biosynthetic process
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FT   From: PDXT_BACSU (P37528)
FT   BINDING         47..49
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT   Condition: G-x-S
FT   BINDING         134..135
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT   Condition: I-R
FT   ACT_SITE        79
FT                   /note="Nucleophile"
FT   Condition: C
FT   ACT_SITE        170
FT                   /note="Charge relay system"
FT   Condition: H
FT   ACT_SITE        172
FT                   /note="Charge relay system"
FT   Condition: E
FT   BINDING         106
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT   Condition: R
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Size: 173-236;
Related: None;
Template: P37528; Q9WYU3;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Version: 29
# Last updated date: 2025-09-18
# Created date: 2005-06-13
//