SNO3_YEAST
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 03-AUG-2022, entry version 155.
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}.
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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; P43544; -.
DR PRIDE; P43544; -.
DR EnsemblFungi; YFL060C_mRNA; YFL060C; YFL060C.
DR GeneID; 850484; -.
DR KEGG; sce:YFL060C; -.
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 BioCyc; YEAST:G3O-30407-MON; -.
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 PANTHER; PTHR31559; PTHR31559; 1.
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 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
