ID SNO3_YEAST Reviewed; 222 AA. AC P43544; D6VTH0; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 162. DE RecName: Full=Probable pyridoxal 5'-phosphate synthase subunit SNO3; DE EC=4.3.3.6; DE AltName: Full=PDX2 homolog 3; DE Short=Pdx2.3; DE AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit; DE EC=3.5.1.2; GN Name=SNO3; OrderedLocusNames=YFL060C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., RA Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces RT cerevisiae."; RL Nat. Genet. 10:261-268(1995). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP FUNCTION. RX PubMed=12271461; DOI=10.1002/yea.916; RA Rodriguez-Navarro S., Llorente B., Rodriguez-Manzaneque M.T., Ramne A., RA Uber G., Marchesan D., Dujon B., Herrero E., Sunnerhagen P., RA Perez-Ortin J.E.; RT "Functional analysis of yeast gene families involved in metabolism of RT vitamins B1 and B6."; RL Yeast 19:1261-1276(2002). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). 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 a SNZ CC isoform. {ECO:0000250|UniProtKB:Q03144, ECO:0000269|PubMed:12271461}. 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; CC Evidence={ECO:0000250|UniProtKB:Q03144}; 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:0000250|UniProtKB:Q03144}; CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis. CC {ECO:0000250|UniProtKB:Q03144}. CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family. {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; D50617; BAA09181.1; -; Genomic_DNA. DR EMBL; BK006940; DAA12380.1; -; Genomic_DNA. DR PIR; S56195; S56195. DR RefSeq; NP_116595.1; NM_001179907.1. DR AlphaFoldDB; P43544; -. DR SMR; P43544; -. DR BioGRID; 31087; 9. DR DIP; DIP-1645N; -. DR IntAct; P43544; 5. DR MINT; P43544; -. DR STRING; 4932.YFL060C; -. DR MEROPS; C26.A32; -. DR MaxQB; P43544; -. DR PaxDb; 4932-YFL060C; -. DR PeptideAtlas; P43544; -. DR EnsemblFungi; YFL060C_mRNA; YFL060C; YFL060C. DR GeneID; 850484; -. DR KEGG; sce:YFL060C; -. DR AGR; SGD:S000001834; -. DR SGD; S000001834; SNO3. DR VEuPathDB; FungiDB:YFL060C; -. DR eggNOG; KOG3210; Eukaryota. DR GeneTree; ENSGT00390000011516; -. DR HOGENOM; CLU_069674_0_1_1; -. DR InParanoid; P43544; -. DR OMA; ENIEMYS; -. DR OrthoDB; 842at2759; -. DR BioCyc; YEAST:G3O-30407-MONOMER; -. DR UniPathway; UPA00245; -. DR PRO; PR:P43544; -. DR Proteomes; UP000002311; Chromosome VI. DR RNAct; P43544; Protein. 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-EC. DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-EC. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0008614; P:pyridoxine metabolic process; IDA:SGD. DR CDD; cd01749; GATase1_PB; 1. DR Gene3D; 3.40.50.880; -; 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 1: Evidence at protein level; KW Glutamine amidotransferase; Hydrolase; Lyase; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1..222 FT /note="Probable pyridoxal 5'-phosphate synthase subunit FT SNO3" FT /id="PRO_0000135621" FT ACT_SITE 91 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P37528" FT ACT_SITE 197 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P37528" FT ACT_SITE 199 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P37528" FT BINDING 58..60 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P37528" FT BINDING 120 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P37528" FT BINDING 151..152 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P37528" SQ SEQUENCE 222 AA; 25132 MW; C7A0EFA9826FB77C CRC64; MTVVIGVLAL QGAFIEHVRH VEKCIVENRD FYEKKLSVMT VKDKNQLAQC DALIIPGGES TAMSLIAERT GFYDDLYAFV HNPSKVTWGT CAGLIYISQQ LSNEAKLVKT LNLLKVKVKR NAFGRQAQSS TRICDFSNFI PHCNDFPATF IRAPVIEEVL DPEHVQVLYK LDGKDNGGQE LIVAAKQKNN ILATSFHPEL AENDIRFHDW FIREFVLKNY SK //