SNO1_YEAST
ID SNO1_YEAST Reviewed; 224 AA.
AC Q03144; D6VZR8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit SNO1;
DE EC=4.3.3.6;
DE AltName: Full=PDX2 homolog 1;
DE Short=Pdx2.1;
DE AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit;
DE EC=3.5.1.2 {ECO:0000269|PubMed:14764090};
GN Name=SNO1; OrderedLocusNames=YMR095C; ORFNames=YM6543.02C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP PROTEIN SEQUENCE OF 1-9, FUNCTION AS GLUTAMINASE, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14764090; DOI=10.1111/j.1432-1033.2003.03973.x;
RA Dong Y.X., Sueda S., Nikawa J., Kondo H.;
RT "Characterization of the products of the genes SNO1 and SNZ1 involved in
RT pyridoxine synthesis in Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 271:745-752(2004).
RN [5]
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).
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:0000305}.
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:0000305};
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:0000269|PubMed:14764090};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 mM for glutamine {ECO:0000269|PubMed:14764090};
CC Vmax=0.48 umol/min/mg enzyme with glutamine as substrate
CC {ECO:0000269|PubMed:14764090};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC {ECO:0000305}.
CC -!- INTERACTION:
CC Q03144; Q03148: SNZ1; NbExp=4; IntAct=EBI-28190, EBI-17618;
CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family. {ECO:0000305}.
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DR EMBL; Z49807; CAA89896.1; -; Genomic_DNA.
DR EMBL; AY692745; AAT92764.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09992.1; -; Genomic_DNA.
DR PIR; S55081; S55081.
DR RefSeq; NP_013813.1; NM_001182595.1.
DR AlphaFoldDB; Q03144; -.
DR SMR; Q03144; -.
DR BioGRID; 35270; 57.
DR ComplexPortal; CPX-1370; SNO1-SNZ1 pyridoxal 5'-phosphate synthase complex.
DR DIP; DIP-1642N; -.
DR IntAct; Q03144; 10.
DR MINT; Q03144; -.
DR STRING; 4932.YMR095C; -.
DR MEROPS; C26.A32; -.
DR MaxQB; Q03144; -.
DR PaxDb; Q03144; -.
DR PRIDE; Q03144; -.
DR EnsemblFungi; YMR095C_mRNA; YMR095C; YMR095C.
DR GeneID; 855120; -.
DR KEGG; sce:YMR095C; -.
DR SGD; S000004701; SNO1.
DR VEuPathDB; FungiDB:YMR095C; -.
DR eggNOG; KOG3210; Eukaryota.
DR GeneTree; ENSGT00390000011516; -.
DR HOGENOM; CLU_069674_0_1_1; -.
DR InParanoid; Q03144; -.
DR OMA; VFIRAPI; -.
DR BioCyc; MetaCyc:G3O-32795-MON; -.
DR BioCyc; YEAST:G3O-32795-MON; -.
DR SABIO-RK; Q03144; -.
DR UniPathway; UPA00245; -.
DR PRO; PR:Q03144; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03144; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1903600; C:glutaminase complex; IPI:SGD.
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:0036001; P:'de novo' pyridoxal 5'-phosphate biosynthetic process; IMP:SGD.
DR GO; GO:0006543; P:glutamine catabolic process; IDA:ComplexPortal.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:SGD.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IGI:SGD.
DR GO; GO:0008614; P:pyridoxine metabolic process; IBA:GO_Central.
DR GO; GO:0042819; P:vitamin B6 biosynthetic process; IMP: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 Direct protein sequencing; Glutamine amidotransferase; Hydrolase; Lyase;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..224
FT /note="Pyridoxal 5'-phosphate synthase subunit SNO1"
FT /id="PRO_0000135619"
FT ACT_SITE 100
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT BINDING 67..69
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT BINDING 129
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P37528"
FT BINDING 160..161
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P37528"
SQ SEQUENCE 224 AA; 24907 MW; C0EC1B2382581D40 CRC64;
MHKTHSTMSG KSMKVIGVLA LQGAFLEHTN HLKRCLAEND YGIKIEIKTV KTPEDLAQCD
ALIIPGGEST SMSLIAQRTG LYPCLYEFVH NPEKVVWGTC AGLIFLSAQL ENESALVKTL
GVLKVDVRRN AFGRQAQSFT QKCDFSNFIP GCDNFPATFI RAPVIERILD PIAVKSLYEL
PVNGKDVVVA ATQNHNILVT SFHPELADSD TRFHDWFIRQ FVSN
