ID PDXT_HAEIN Reviewed; 192 AA. AC P45294; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 2. DT 13-SEP-2023, entry version 118. DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000255|HAMAP-Rule:MF_01615}; DE EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01615}; DE AltName: Full=Pdx2 {ECO:0000255|HAMAP-Rule:MF_01615}; DE AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000255|HAMAP-Rule:MF_01615}; DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01615}; GN Name=pdxT {ECO:0000255|HAMAP-Rule:MF_01615}; GN OrderedLocusNames=HI_1648; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). 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:0000255|HAMAP-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:0000255|HAMAP- CC 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:0000255|HAMAP-Rule:MF_01615}; CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of heterodimers. CC Only shows activity in the heterodimer. {ECO:0000255|HAMAP- CC Rule:MF_01615}. CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family. CC {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC23295.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; L42023; AAC23295.1; ALT_INIT; Genomic_DNA. DR PIR; G64173; G64173. DR RefSeq; NP_439790.2; NC_000907.1. DR AlphaFoldDB; P45294; -. DR SMR; P45294; -. DR STRING; 71421.HI_1648; -. DR MEROPS; C26.A32; -. DR EnsemblBacteria; AAC23295; AAC23295; HI_1648. DR KEGG; hin:HI_1648; -. DR PATRIC; fig|71421.8.peg.1724; -. DR eggNOG; COG0311; Bacteria. DR HOGENOM; CLU_069674_2_0_6; -. DR OrthoDB; 9810320at2; -. DR PhylomeDB; P45294; -. DR BioCyc; HINF71421:G1GJ1-1665-MONOMER; -. DR UniPathway; UPA00245; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:1903600; C:glutaminase complex; IBA:GO_Central. 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:0006543; P:glutamine catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0008614; P:pyridoxine metabolic process; IBA:GO_Central. 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 NCBIfam; TIGR03800; PLP_synth_Pdx2; 1. 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 PROSITE; PS01236; PDXT_SNO_1; 1. DR PROSITE; PS51130; PDXT_SNO_2; 1. PE 3: Inferred from homology; KW Glutamine amidotransferase; Hydrolase; Lyase; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1..192 FT /note="Pyridoxal 5'-phosphate synthase subunit PdxT" FT /id="PRO_0000135641" FT ACT_SITE 82 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615" FT ACT_SITE 172 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615" FT ACT_SITE 174 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615" FT BINDING 50..52 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615" FT BINDING 109 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615" FT BINDING 136..137 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01615" SQ SEQUENCE 192 AA; 21070 MW; 52297D26C0EE5579 CRC64; MKIGILALQG AFAEHARMLE KLGIESVELR NLKNFQQHYS DLSGLILPGG ESTAIGKLLR ELYMLEPIKQ AISSGFPVFG TCAGLILLAK EITSQKESHF GTMDIVVERN AYGRQLGSFY TEADCKGVGK IPMTFIRGPI ISSVGKKVNI LATVNNKIVA AQEKNMLVTS FHPELTNNLS LHKYFIDICK VA //