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Database: UniProt
Entry: G1W987_9BACT
LinkDB: G1W987_9BACT
Original site: G1W987_9BACT 
ID   G1W987_9BACT            Unreviewed;       191 AA.
AC   G1W987;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 52.
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=HMPREF9431_00388 {ECO:0000313|EMBL:EGV34428.1};
OS   Prevotella oulorum F0390.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=702438 {ECO:0000313|EMBL:EGV34428.1, ECO:0000313|Proteomes:UP000005141};
RN   [1] {ECO:0000313|EMBL:EGV34428.1, ECO:0000313|Proteomes:UP000005141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0390 {ECO:0000313|EMBL:EGV34428.1,
RC   ECO:0000313|Proteomes:UP000005141};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA   Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella oulorum F0390.";
RL   Submitted (JUL-2011) 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:EGV34428.1}.
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DR   EMBL; ADGI01000015; EGV34428.1; -; Genomic_DNA.
DR   RefSeq; WP_004379371.1; NZ_JH114215.1.
DR   AlphaFoldDB; G1W987; -.
DR   PATRIC; fig|702438.4.peg.396; -.
DR   eggNOG; COG0311; Bacteria.
DR   HOGENOM; CLU_069674_2_0_10; -.
DR   OrthoDB; 9810320at2; -.
DR   UniPathway; UPA00245; -.
DR   Proteomes; UP000005141; 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: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:UP000005141}.
FT   ACT_SITE        79
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT                   ECO:0000256|PIRSR:PIRSR005639-1"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        168
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT                   ECO:0000256|PIRSR:PIRSR005639-1"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        170
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01615,
FT                   ECO:0000256|PIRSR:PIRSR005639-1"
FT   BINDING         47..49
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         106
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         132..133
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   191 AA;  21246 MW;  66F4CC476AC71FBB CRC64;
     MRIAVLALQG AFAEHRKMLQ TLGVESFEVR QAVDWEQPKD GLILPGGEST VQSKLLKELY
     LLDALRQDIC NGLPVFGTCA GLILLAQHVE NDVRERLGTM HITVKRNAYG RQTGSFFTED
     NFAGQTIPMS FIRAPYISEV ENDVEVLSTV DGHIVAAQQG CQLVTAFHPE LLTDTTVHRH
     FLSIVKETKI D
//
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