PDXT_GEOSE
ID PDXT_GEOSE Reviewed; 196 AA.
AC P83813;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000255|HAMAP-Rule:MF_01615};
DE EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01615};
DE AltName: Full=Pdx2 {ECO:0000255|HAMAP-Rule:MF_01615};
DE AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000255|HAMAP-Rule:MF_01615};
DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01615};
GN Name=pdxT {ECO:0000255|HAMAP-Rule:MF_01615};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RA Miller D.J., Anderson W.F.;
RT "X-ray structure analysis of a predicted amidotransferase from
RT B.stearothermophilus at 1.9 A resolution.";
RL Submitted (AUG-2003) to the PDB data bank.
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:0000255|HAMAP-Rule:MF_01615}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01615};
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:0000255|HAMAP-Rule:MF_01615};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01615}.
CC -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of heterodimers.
CC Only shows activity in the heterodimer. {ECO:0000255|HAMAP-
CC Rule:MF_01615}.
CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC {ECO:0000255|HAMAP-Rule:MF_01615}.
CC -!- CAUTION: The sequence shown here has been extracted from PDB entry
CC 1Q7R. {ECO:0000305}.
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DR PDB; 1Q7R; X-ray; 1.90 A; A=1-196.
DR PDBsum; 1Q7R; -.
DR SMR; P83813; -.
DR UniPathway; UPA00245; -.
DR EvolutionaryTrace; P83813; -.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006543; P:glutamine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01749; GATase1_PB; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_01615; PdxT; 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 3D-structure; Glutamine amidotransferase; Hydrolase; Lyase;
KW Pyridoxal phosphate.
FT CHAIN 1..196
FT /note="Pyridoxal 5'-phosphate synthase subunit PdxT"
FT /id="PRO_0000135631"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT ACT_SITE 169
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT ACT_SITE 171
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT BINDING 46..48
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT BINDING 105
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT BINDING 133..134
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1Q7R"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:1Q7R"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:1Q7R"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1Q7R"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:1Q7R"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1Q7R"
FT HELIX 48..57
FT /evidence="ECO:0007829|PDB:1Q7R"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:1Q7R"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1Q7R"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:1Q7R"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1Q7R"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1Q7R"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:1Q7R"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:1Q7R"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1Q7R"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:1Q7R"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:1Q7R"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:1Q7R"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:1Q7R"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1Q7R"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1Q7R"
FT HELIX 177..195
FT /evidence="ECO:0007829|PDB:1Q7R"
SQ SEQUENCE 196 AA; 21225 MW; FAE3D389E229A41B CRC64;
MKIGVLGLQG AVREHVRAIE ACGAEAVIVK KSEQLEGLDG LVLPGGESTT XRRLIDRYGL
XEPLKQFAAA GKPXFGTCAG LILLAKRIVG YDEPHLGLXD ITVERNSFGR QRESFEAELS
IKGVGDGFVG VFIRAPHIVE AGDGVDVLAT YNDRIVAARQ GQFLGCSFHP ELTDDHRLXQ
YFLNXVKEAK XASSLK
