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Database: UniProt
Entry: A0A0U1PR19_9MICO
LinkDB: A0A0U1PR19_9MICO
Original site: A0A0U1PR19_9MICO 
ID   A0A0U1PR19_9MICO        Unreviewed;       200 AA.
AC   A0A0U1PR19;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000256|HAMAP-Rule:MF_01615};
DE            EC=4.3.3.6 {ECO:0000256|HAMAP-Rule:MF_01615};
DE   AltName: Full=Pdx2 {ECO:0000256|HAMAP-Rule:MF_01615};
DE   AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000256|HAMAP-Rule:MF_01615};
DE            EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01615};
GN   Name=pdxT {ECO:0000256|HAMAP-Rule:MF_01615};
GN   ORFNames=VT73_10245 {ECO:0000313|EMBL:KKM44349.1};
OS   Rathayibacter toxicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=145458 {ECO:0000313|EMBL:KKM44349.1, ECO:0000313|Proteomes:UP000052979};
RN   [1] {ECO:0000313|EMBL:KKM44349.1, ECO:0000313|Proteomes:UP000052979}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FH142 {ECO:0000313|EMBL:KKM44349.1,
RC   ECO:0000313|Proteomes:UP000052979};
RG   Consortium for Microbial Forensics and Genomics (microFORGE);
RA   Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA   Blagden T., Luster D.G., Sechler A.J., Schneider W.L., Winegar R.A.;
RT   "Draft genome sequence of Rathayibacter toxicus strain FH-142 (AKA 70134 or
RT   CS 32), a Western Australian isolate.";
RL   Submitted (APR-2015) 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:0000256|HAMAP-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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01615};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01615}.
CC   -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of heterodimers.
CC       Only shows activity in the heterodimer. {ECO:0000256|HAMAP-
CC       Rule:MF_01615}.
CC   -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC       {ECO:0000256|ARBA:ARBA00008345, ECO:0000256|HAMAP-Rule:MF_01615}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKM44349.1}.
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DR   EMBL; LBFI01000057; KKM44349.1; -; Genomic_DNA.
DR   RefSeq; WP_027691507.1; NZ_PSXM01000010.1.
DR   AlphaFoldDB; A0A0U1PR19; -.
DR   STRING; 145458.APU90_09780; -.
DR   GeneID; 66873992; -.
DR   KEGG; rtc:APU90_09780; -.
DR   PATRIC; fig|145458.8.peg.2329; -.
DR   eggNOG; COG0311; Bacteria.
DR   UniPathway; UPA00245; -.
DR   Proteomes; UP000052979; Unassembled WGS sequence.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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   NCBIfam; TIGR03800; PLP_synth_Pdx2; 1.
DR   PANTHER; PTHR31559; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO; 1.
DR   PANTHER; PTHR31559:SF0; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED; 1.
DR   Pfam; PF01174; SNO; 1.
DR   PIRSF; PIRSF005639; Glut_amidoT_SNO; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS01236; PDXT_SNO_1; 1.
DR   PROSITE; PS51130; PDXT_SNO_2; 1.
PE   3: Inferred from homology;
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01615,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01615};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01615};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01615};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052979};
KW   Transferase {ECO:0000313|EMBL:KKM44349.1}.
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT                   ECO:0000256|PIRSR:PIRSR005639-1"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        176
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT                   ECO:0000256|PIRSR:PIRSR005639-1"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        178
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT                   ECO:0000256|PIRSR:PIRSR005639-1"
FT   BINDING         49..51
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT                   ECO:0000256|PIRSR:PIRSR005639-2"
FT   BINDING         110
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT                   ECO:0000256|PIRSR:PIRSR005639-2"
FT   BINDING         139..140
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT                   ECO:0000256|PIRSR:PIRSR005639-2"
SQ   SEQUENCE   200 AA;  21517 MW;  A2B32501F9F8B74D CRC64;
     MEGLRVGVLA LQGDFREHAH VLRELGAEVV LVRRPEEFAS VAGLVIPGGE SSVMDKLSRL
     FGLAEPVQEA IRAGLPVYGT CAGLIMLADR VLDRIDGQRS FGGLDISVRR NAFGNQLDSF
     ETDLDVPEIG DPPVHAVFIR APVVEELGER ATALASVADG RVVAVEQGTL LGTAFHPEIT
     GDYRFHELFL RTVAATRFGA
//
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