ID A0A1E3S3L3_9MYCO Unreviewed; 198 AA. AC A0A1E3S3L3; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 15-FEB-2017, entry version 2. 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=BHQ20_28595 {ECO:0000313|EMBL:ODQ96763.1}; OS Mycobacterium intermedium. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=28445 {ECO:0000313|EMBL:ODQ96763.1, ECO:0000313|Proteomes:UP000094976}; RN [1] {ECO:0000313|EMBL:ODQ96763.1, ECO:0000313|Proteomes:UP000094976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMC2_M5 {ECO:0000313|EMBL:ODQ96763.1, RC ECO:0000313|Proteomes:UP000094976}; RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.; RL Submitted (SEP-2016) 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 CC PdxS. {ECO:0000256|HAMAP-Rule:MF_01615}. CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate + D-glyceraldehyde 3- CC phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 CC H(2)O + phosphate. {ECO:0000256|HAMAP-Rule:MF_01615}. CC -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3). CC {ECO:0000256|HAMAP-Rule:MF_01615}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01615}. CC -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of CC heterodimers. Only shows activity in the heterodimer. CC {ECO:0000256|HAMAP-Rule:MF_01615}. CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family. CC {ECO:0000256|HAMAP-Rule:MF_01615}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ODQ96763.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MIHB01000100; ODQ96763.1; -; Genomic_DNA. DR RefSeq; WP_069422522.1; NZ_MIHB01000100.1. DR UniPathway; UPA00245; -. DR Proteomes; UP000094976; Unassembled WGS sequence. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. 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 Pfam; PF01174; SNO; 1. DR PIRSF; PIRSF005639; Glut_amidoT_SNO; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR03800; PLP_synth_Pdx2; 1. DR PROSITE; PS01236; PDXT_SNO_1; 1. DR PROSITE; PS51130; PDXT_SNO_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000094976}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01615, KW ECO:0000313|EMBL:ODQ96763.1}; 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 Transferase {ECO:0000313|EMBL:ODQ96763.1}. FT REGION 49 51 L-glutamine binding. {ECO:0000256|HAMAP- FT Rule:MF_01615}. FT REGION 141 142 L-glutamine binding. {ECO:0000256|HAMAP- FT Rule:MF_01615}. FT ACT_SITE 81 81 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01615}. FT ACT_SITE 177 177 Charge relay system. {ECO:0000256|HAMAP- FT Rule:MF_01615}. FT ACT_SITE 179 179 Charge relay system. {ECO:0000256|HAMAP- FT Rule:MF_01615}. FT BINDING 113 113 L-glutamine. {ECO:0000256|HAMAP-Rule: FT MF_01615}. SQ SEQUENCE 198 AA; 21197 MW; C2C25B208553E6AE CRC64; MNRPTVGVLA LQGDTREHLI ALRECGADPI TVRRRSELDA VEALVLPGGE STTMSHLLLE LDLLEPLRAR LADGLPAYGS CAGMIMLASE IVDAGAGGRE ALPLRGIDMT VRRNAFGRQV DSFEGDLAFA GLDEPVRAVF IRAPWVERVG DGVQVLARAA GHAVAVRQGS VLATAFHPEM TGDRRIHQLF VDIVTGRA //