PDXT_LISMO
ID PDXT_LISMO Reviewed; 188 AA.
AC Q8Y5G1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=lmo2102;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL591982; CAD00180.1; -; Genomic_DNA.
DR PIR; AF1337; AF1337.
DR RefSeq; NP_465626.1; NC_003210.1.
DR RefSeq; WP_009932189.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y5G1; -.
DR SMR; Q8Y5G1; -.
DR STRING; 169963.lmo2102; -.
DR PaxDb; Q8Y5G1; -.
DR EnsemblBacteria; CAD00180; CAD00180; CAD00180.
DR GeneID; 984751; -.
DR KEGG; lmo:lmo2102; -.
DR PATRIC; fig|169963.11.peg.2153; -.
DR eggNOG; COG0311; Bacteria.
DR HOGENOM; CLU_069674_2_0_9; -.
DR OMA; VFIRAPI; -.
DR PhylomeDB; Q8Y5G1; -.
DR BioCyc; LMON169963:LMO2102-MON; -.
DR UniPathway; UPA00245; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1903600; C:glutaminase complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008614; P:pyridoxine metabolic process; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1..188
FT /note="Pyridoxal 5'-phosphate synthase subunit PdxT"
FT /id="PRO_0000135645"
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 105
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 188 AA; 20500 MW; 705AC3F8B0639830 CRC64;
MKKIGVLAIQ GAVDEHIQMI ESAGALAFKV KHSNDLAGLD GLVLPGGEST TMRKIMKRYD
LMEPVKAFAS KGKAIFGTCA GLVLLSKEIE GGEESLGLIE ATAIRNGFGR QKESFEAELN
VEAFGEPAFE AIFIRAPYLI EPSNEVAVLA TVENRIVAAK QANILVTAFH PELTNDNRWM
NYFLEKMV
