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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)

 PDXT_MYCTU              Reviewed;         198 AA.
P9WII7; L0TAD2; O06210; Q7D6X1;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
10-OCT-2018, entry version 25.
RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000255|HAMAP-Rule:MF_01615};
EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01615};
AltName: Full=Pdx2 {ECO:0000255|HAMAP-Rule:MF_01615};
AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000255|HAMAP-Rule:MF_01615};
EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01615};
Name=pdxT {ECO:0000255|HAMAP-Rule:MF_01615};
OrderedLocusNames=Rv2604c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(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:0000255|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:0000255|HAMAP-Rule:MF_01615}.
-!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3).
{ECO:0000255|HAMAP-Rule:MF_01615}.
-!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate
biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01615}.
-!- SUBUNIT: In the presence of PdxS, forms a dodecamer of
heterodimers. Only shows activity in the heterodimer.
{ECO:0000255|HAMAP-Rule:MF_01615}.
-!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
{ECO:0000255|HAMAP-Rule:MF_01615}.
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EMBL; AL123456; CCP45401.1; -; Genomic_DNA.
PIR; C70570; C70570.
RefSeq; NP_217120.1; NC_000962.3.
RefSeq; WP_003413465.1; NZ_CP009480.1.
ProteinModelPortal; P9WII7; -.
SMR; P9WII7; -.
STRING; 83332.Rv2604c; -.
PaxDb; P9WII7; -.
EnsemblBacteria; CCP45401; CCP45401; Rv2604c.
GeneID; 887371; -.
KEGG; mtu:Rv2604c; -.
TubercuList; Rv2604c; -.
eggNOG; ENOG4108UHX; Bacteria.
eggNOG; COG0311; LUCA.
KO; K08681; -.
OMA; VFIRAPI; -.
PhylomeDB; P9WII7; -.
UniPathway; UPA00245; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:1903600; C:glutaminase complex; IBA:GO_Central.
GO; GO:0016843; F:amine-lyase activity; IDA:MTBBASE.
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:0006543; P:glutamine catabolic process; IEA:UniProtKB-UniRule.
GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IDA:MTBBASE.
GO; GO:0008614; P:pyridoxine metabolic process; IBA:GO_Central.
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.
1: Evidence at protein level;
Complete proteome; Glutamine amidotransferase; Hydrolase; Lyase;
Pyridoxal phosphate; Reference proteome.
CHAIN 1 198 Pyridoxal 5'-phosphate synthase subunit
PdxT.
/FTId=PRO_0000135649.
REGION 49 51 L-glutamine binding. {ECO:0000255|HAMAP-
Rule:MF_01615}.
REGION 141 142 L-glutamine binding. {ECO:0000255|HAMAP-
Rule:MF_01615}.
ACT_SITE 81 81 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01615}.
ACT_SITE 177 177 Charge relay system. {ECO:0000255|HAMAP-
Rule:MF_01615}.
ACT_SITE 179 179 Charge relay system. {ECO:0000255|HAMAP-
Rule:MF_01615}.
BINDING 113 113 L-glutamine. {ECO:0000255|HAMAP-
Rule:MF_01615}.
SEQUENCE 198 AA; 21072 MW; 1B143808EB05CD4F CRC64;
MSVPRVGVLA LQGDTREHLA ALRECGAEPM TVRRRDELDA VDALVIPGGE STTMSHLLLD
LDLLGPLRAR LADGLPAYGS CAGMILLASE ILDAGAAGRQ ALPLRAMNMT VRRNAFGSQV
DSFEGDIEFA GLDDPVRAVF IRAPWVERVG DGVQVLARAA GHIVAVRQGA VLATAFHPEM
TGDRRIHQLF VDIVTSAA


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