PDXT_THET8
ID PDXT_THET8 Reviewed; 191 AA.
AC Q5SKD6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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}; OrderedLocusNames=TTHA0707;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
RA Manzoku M., Ebihara A., Fujimoto Y., Yokoyama S., Kuramitsu S.;
RT "Crystal structure of glutamine amidotransferase.";
RL Submitted (APR-2007) 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}.
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DR EMBL; AP008226; BAD70530.1; -; Genomic_DNA.
DR RefSeq; WP_011228136.1; NC_006461.1.
DR RefSeq; YP_143973.1; NC_006461.1.
DR PDB; 2YWD; X-ray; 1.90 A; A=1-191.
DR PDBsum; 2YWD; -.
DR AlphaFoldDB; Q5SKD6; -.
DR SMR; Q5SKD6; -.
DR STRING; 300852.55772089; -.
DR EnsemblBacteria; BAD70530; BAD70530; BAD70530.
DR GeneID; 3168933; -.
DR KEGG; ttj:TTHA0707; -.
DR PATRIC; fig|300852.9.peg.701; -.
DR eggNOG; COG0311; Bacteria.
DR HOGENOM; CLU_069674_2_0_0; -.
DR OMA; VFIRAPI; -.
DR PhylomeDB; Q5SKD6; -.
DR UniPathway; UPA00245; -.
DR EvolutionaryTrace; Q5SKD6; -.
DR Proteomes; UP000000532; Chromosome.
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; Reference proteome.
FT CHAIN 1..191
FT /note="Pyridoxal 5'-phosphate synthase subunit PdxT"
FT /id="PRO_0000135671"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT ACT_SITE 174
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT BINDING 48..50
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT BINDING 109
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT BINDING 136..137
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:2YWD"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:2YWD"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:2YWD"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:2YWD"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2YWD"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:2YWD"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2YWD"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:2YWD"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:2YWD"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2YWD"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:2YWD"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2YWD"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:2YWD"
FT STRAND 115..125
FT /evidence="ECO:0007829|PDB:2YWD"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:2YWD"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:2YWD"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:2YWD"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:2YWD"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:2YWD"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:2YWD"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:2YWD"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:2YWD"
SQ SEQUENCE 191 AA; 21209 MW; 75AF27D33AEE95E1 CRC64;
MRGVVGVLAL QGDFREHKEA LKRLGIEAKE VRKKEHLEGL KALIVPGGES TTIGKLAREY
GIEDEVRKRV EEGSLALFGT CAGAIWLAKE IVGYPEQPRL GVLEAWVERN AFGRQVESFE
EDLEVEGLGS FHGVFIRAPV FRRLGEGVEV LARLGDLPVL VRQGKVLASS FHPELTEDPR
LHRYFLELAG V
