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Pyridoxal 5'-phosphate synthase subunit PdxT (EC 4.3.3.6) (Pdx2) (Pyridoxal 5'-phosphate synthase glutaminase subunit) (EC 3.5.1.2)

 A0A0P9HAI6_9CHLR        Unreviewed;       190 AA.
A0A0P9HAI6;
20-JAN-2016, integrated into UniProtKB/TrEMBL.
20-JAN-2016, sequence version 1.
05-DEC-2018, entry version 15.
RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000256|HAMAP-Rule:MF_01615};
EC=4.3.3.6 {ECO:0000256|HAMAP-Rule:MF_01615};
AltName: Full=Pdx2 {ECO:0000256|HAMAP-Rule:MF_01615};
AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000256|HAMAP-Rule:MF_01615};
EC=3.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01615};
Name=pdxT {ECO:0000256|HAMAP-Rule:MF_01615};
ORFNames=SE17_21540 {ECO:0000313|EMBL:KPV51377.1};
Kouleothrix aurantiaca.
Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
Roseiflexaceae; Kouleothrix.
NCBI_TaxID=186479 {ECO:0000313|EMBL:KPV51377.1, ECO:0000313|Proteomes:UP000050509};
[1] {ECO:0000313|EMBL:KPV51377.1, ECO:0000313|Proteomes:UP000050509}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=COM-B {ECO:0000313|EMBL:KPV51377.1,
ECO:0000313|Proteomes:UP000050509};
Hemp J.;
"Draft genome sequence of Kouleothrix aurantiaca JCM 19913.";
Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the hydrolysis of glutamine to glutamate and
ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The
resulting ammonia molecule is channeled to the active site of
PdxS. {ECO:0000256|HAMAP-Rule:MF_01615}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
Evidence={ECO:0000256|HAMAP-Rule:MF_01615};
-!- CATALYTIC ACTIVITY:
Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-
phosphate + L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate
+ pyridoxal 5'-phosphate; Xref=Rhea:RHEA:31507,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
ChEBI:CHEBI:43474, ChEBI:CHEBI:58273, ChEBI:CHEBI:58359,
ChEBI:CHEBI:59776, ChEBI:CHEBI:597326; EC=4.3.3.6;
Evidence={ECO:0000256|HAMAP-Rule:MF_01615};
-!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate
biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01615}.
-!- SUBUNIT: In the presence of PdxS, forms a dodecamer of
heterodimers. Only shows activity in the heterodimer.
{ECO:0000256|HAMAP-Rule:MF_01615}.
-!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
{ECO:0000256|HAMAP-Rule:MF_01615}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KPV51377.1}.
-----------------------------------------------------------------------
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EMBL; LJCR01000939; KPV51377.1; -; Genomic_DNA.
EnsemblBacteria; KPV51377; KPV51377; SE17_21540.
PATRIC; fig|186479.3.peg.10887; -.
UniPathway; UPA00245; -.
Proteomes; UP000050509; Unassembled WGS sequence.
GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-UniRule.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0006543; P:glutamine catabolic process; IEA:UniProtKB-UniRule.
GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
CDD; cd01749; GATase1_PB; 1.
Gene3D; 3.40.50.880; -; 1.
HAMAP; MF_01615; PdxT; 1.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR002161; PdxT/SNO.
InterPro; IPR021196; PdxT/SNO_CS.
PANTHER; PTHR31559; PTHR31559; 1.
Pfam; PF01174; SNO; 1.
PIRSF; PIRSF005639; Glut_amidoT_SNO; 1.
SUPFAM; SSF52317; SSF52317; 1.
TIGRFAMs; TIGR03800; PLP_synth_Pdx2; 1.
PROSITE; PS01236; PDXT_SNO_1; 1.
PROSITE; PS51130; PDXT_SNO_2; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000050509};
Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01615,
ECO:0000313|EMBL:KPV51377.1};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01615};
Lyase {ECO:0000256|HAMAP-Rule:MF_01615};
Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01615};
Reference proteome {ECO:0000313|Proteomes:UP000050509};
Transferase {ECO:0000313|EMBL:KPV51377.1}.
REGION 46 48 L-glutamine binding. {ECO:0000256|HAMAP-
Rule:MF_01615}.
REGION 137 138 L-glutamine binding. {ECO:0000256|HAMAP-
Rule:MF_01615}.
ACT_SITE 78 78 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_01615}.
ACT_SITE 174 174 Charge relay system. {ECO:0000256|HAMAP-
Rule:MF_01615}.
ACT_SITE 176 176 Charge relay system. {ECO:0000256|HAMAP-
Rule:MF_01615}.
BINDING 108 108 L-glutamine. {ECO:0000256|HAMAP-
Rule:MF_01615}.
SEQUENCE 190 AA; 20897 MW; 000B40AE76D15D0D CRC64;
MTIGILALQG DFREHEEMLQ RIGAPTLQVR LPKQLEQIDR LIIPGGESTT IGKLLVLYGL
LEPIRERGKA GMPIWGTCAG AILLARHIAE GRPEGQPALA LMDITARRNA FGRQLDSFEV
NMAIDLLGDE PINTVFIRAP ILENPGAGVT TLATLNDGRI VAAQQSHLLA TCFHPELTGD
ERFHRYFLEL


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