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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)

 B7QZS8_9EURY            Unreviewed;       197 AA.
B7QZS8;
10-FEB-2009, integrated into UniProtKB/TrEMBL.
10-FEB-2009, sequence version 1.
28-FEB-2018, entry version 44.
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=TAM4_685 {ECO:0000313|EMBL:EEB74740.1};
Thermococcus sp. AM4.
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Thermococcus.
NCBI_TaxID=246969 {ECO:0000313|EMBL:EEB74740.1, ECO:0000313|Proteomes:UP000009277};
[1] {ECO:0000313|EMBL:EEB74740.1, ECO:0000313|Proteomes:UP000009277}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AM4 {ECO:0000313|EMBL:EEB74740.1};
PubMed=22123768; DOI=10.1128/JB.06259-11;
Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A.,
Bartlett D.H., Bonch-Osmolovskaya E.A., Lebedinsky A.V.;
"Complete Genome Sequence of the Hyperthermophilic Archaeon
Thermococcus sp. Strain AM4, Capable of Organotrophic Growth and
Growth at the Expense of Hydrogenogenic or Sulfidogenic Oxidation of
Carbon Monoxide.";
J. Bacteriol. 193:7019-7020(2011).
-!- 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: D-ribose 5-phosphate + D-glyceraldehyde 3-
phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3
H(2)O + phosphate. {ECO:0000256|HAMAP-Rule:MF_01615}.
-!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3).
{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}.
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EMBL; CP002952; EEB74740.1; -; Genomic_DNA.
RefSeq; WP_014123375.1; NC_016051.1.
ProteinModelPortal; B7QZS8; -.
STRING; 246969.TAM4_685; -.
MEROPS; C26.A32; -.
EnsemblBacteria; EEB74740; EEB74740; TAM4_685.
GeneID; 7418439; -.
KEGG; tha:TAM4_685; -.
eggNOG; arCOG00034; Archaea.
eggNOG; COG0311; LUCA.
KO; K08681; -.
OrthoDB; POG093Z0AY8; -.
BioCyc; TSP246969:G1GNJ-2281-MONOMER; -.
UniPathway; UPA00245; -.
Proteomes; UP000009277; Chromosome.
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:UP000009277};
Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01615,
ECO:0000313|EMBL:EEB74740.1};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01615};
Lyase {ECO:0000256|HAMAP-Rule:MF_01615};
Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01615};
Transferase {ECO:0000313|EMBL:EEB74740.1}.
REGION 53 55 L-glutamine binding. {ECO:0000256|HAMAP-
Rule:MF_01615}.
REGION 142 143 L-glutamine binding. {ECO:0000256|HAMAP-
Rule:MF_01615}.
ACT_SITE 85 85 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_01615}.
ACT_SITE 179 179 Charge relay system. {ECO:0000256|HAMAP-
Rule:MF_01615}.
ACT_SITE 181 181 Charge relay system. {ECO:0000256|HAMAP-
Rule:MF_01615}.
BINDING 114 114 L-glutamine. {ECO:0000256|HAMAP-
Rule:MF_01615}.
SEQUENCE 197 AA; 21644 MW; 5E2971B04DACF984 CRC64;
MVKVGVIGLQ GDVSEHIEAS KKALENLGVT GEVIWLRKPE QLEGISAIII PGGESTTISK
LMVKTGLFEP VKKLGEEGLP IMGTCAGLIM LSKDVIGATP EQRFLELLDV KVNRNAYGRQ
VDSFEAPVKL AFSDEPFPGV FIRAPRIVEL LSDKVKPIAW LGDRVVGVEQ DNLIGLEFHP
ELTDDTRVHE YFLRKAL


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