ID A0A1E3S3L3_MYCIE Unreviewed; 198 AA. AC A0A1E3S3L3; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 03-MAY-2023, entry version 30. 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}, BST27_29010 GN {ECO:0000313|EMBL:ORA93294.1}; OS Mycobacterium intermedium. OC Bacteria; Actinomycetota; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium simiae complex. OX NCBI_TaxID=28445 {ECO:0000313|EMBL:ODQ96763.1, ECO:0000313|Proteomes:UP000094976}; RN [1] {ECO:0000313|EMBL:ODQ96763.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMC2_M5 {ECO:0000313|EMBL:ODQ96763.1}; RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000094976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMC2_M5 {ECO:0000313|Proteomes:UP000094976}; RA Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ORA93294.1, ECO:0000313|Proteomes:UP000192739} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44049 {ECO:0000313|EMBL:ORA93294.1, RC ECO:0000313|Proteomes:UP000192739}; RA Tortoli E., Trovato A., Cirillo D.M.; RT "The new phylogeny of genus Mycobacterium."; RL Submitted (FEB-2017) 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|ARBA:ARBA00001062, ECO:0000256|HAMAP- CC 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: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 EMBL; MVHT01000146; ORA93294.1; -; Genomic_DNA. DR RefSeq; WP_069422522.1; NZ_MVHT01000146.1. DR STRING; 28445.BHQ20_28595; -. DR EnsemblBacteria; ODQ96763; ODQ96763; BHQ20_28595. DR EnsemblBacteria; OPE45742; OPE45742; BV508_28520. DR EnsemblBacteria; ORA93294; ORA93294; BST27_29010. DR OrthoDB; 9810320at2; -. DR UniPathway; UPA00245; -. DR Proteomes; UP000094976; Unassembled WGS sequence. DR Proteomes; UP000192739; 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:0016740; F:transferase activity; IEA:UniProtKB-KW. 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 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 TIGRFAMs; TIGR03800; PLP_synth_Pdx2; 1. DR PROSITE; PS51274; GATASE_COBBQ; 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:PRU00606}; 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:UP000094976}; KW Transferase {ECO:0000313|EMBL:ODQ96763.1}. FT ACT_SITE 81 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01615, FT ECO:0000256|PIRSR:PIRSR005639-1" FT ACT_SITE 177 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 177 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01615, FT ECO:0000256|PIRSR:PIRSR005639-1" FT ACT_SITE 179 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 179 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01615, FT ECO:0000256|PIRSR:PIRSR005639-1" FT BINDING 49..51 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 113 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 141..142 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 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 //