PDXT_GEOSW
ID PDXT_GEOSW Reviewed; 192 AA.
AC C5D338;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=GWCH70_0012;
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC unclassified Geobacillus.
OX NCBI_TaxID=471223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001638; ACS22954.1; -; Genomic_DNA.
DR RefSeq; WP_012748791.1; NC_012793.1.
DR AlphaFoldDB; C5D338; -.
DR SMR; C5D338; -.
DR STRING; 471223.GWCH70_0012; -.
DR EnsemblBacteria; ACS22954; ACS22954; GWCH70_0012.
DR KEGG; gwc:GWCH70_0012; -.
DR eggNOG; COG0311; Bacteria.
DR HOGENOM; CLU_069674_2_0_9; -.
DR OMA; VFIRAPI; -.
DR OrthoDB; 1628378at2; -.
DR UniPathway; UPA00245; -.
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 3: Inferred from homology;
KW Glutamine amidotransferase; Hydrolase; Lyase; Pyridoxal phosphate.
FT CHAIN 1..192
FT /note="Pyridoxal 5'-phosphate synthase subunit PdxT"
FT /id="PRO_1000215715"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT ACT_SITE 170
FT /note="Charge relay system"
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 BINDING 47..49
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT BINDING 106
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
FT BINDING 134..135
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615"
SQ SEQUENCE 192 AA; 21182 MW; 1EE6C1084D0E0C6C CRC64;
MMKIGVLGLQ GAVQEHVRSI EACGAEAVVV KKIEQLEEID GLILPGGEST TMRRLMDKYG
FIEPLKQFAA AGKPMFGTCA GLILLAKRIV GYDEPHLGLM DITVERNSFG RQRESFEAEL
SIAGVADDFI GVFIRAPHIV EVGEDVEVLA KYEGRIVAAR QGQFLGCSFH PELTDDYRMT
QYFLNMVKEA KA
