ID   SNZ3_YEAST              Reviewed;         298 AA.
AC   P43545; D6VTH1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 169.
DE   RecName: Full=Probable pyridoxal 5'-phosphate synthase subunit SNZ3;
DE            Short=PLP synthase subunit SNZ3;
DE            EC=4.3.3.6;
DE   AltName: Full=PDX1 homolog 3;
DE            Short=Pdx1.3;
GN   Name=SNZ3; OrderedLocusNames=YFL059W;
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   PROBABLE FUNCTION, AND INDUCTION.
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 formation of pyridoxal 5'-phosphate from ribose
CC       5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The
CC       ammonia is provided by a SNO isoform. Can also use ribulose 5-phosphate
CC       and dihydroxyacetone phosphate as substrates, resulting from enzyme-
CC       catalyzed isomerization of RBP and G3P, respectively.
CC       {ECO:0000250|UniProtKB:Q03148}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate +
CC         L-glutamine = pyridoxal 5'-phosphate + L-glutamate + phosphate + 3
CC         H2O + H(+); 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:Q03148};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC   -!- SUBUNIT: Homohexamer (By similarity). Interacts with THI11
CC       (PubMed:12271461). {ECO:0000250|UniProtKB:Q03148,
CC       ECO:0000269|PubMed:12271461}.
CC   -!- INDUCTION: By the absence of external thiamine.
CC       {ECO:0000269|PubMed:12271461}.
CC   -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000305}.
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DR   EMBL; D50617; BAA09182.1; -; Genomic_DNA.
DR   EMBL; BK006940; DAA12381.1; -; Genomic_DNA.
DR   PIR; S56196; S56196.
DR   RefSeq; NP_116596.1; NM_001179908.1.
DR   AlphaFoldDB; P43545; -.
DR   SMR; P43545; -.
DR   BioGRID; 31088; 14.
DR   DIP; DIP-1644N; -.
DR   FunCoup; P43545; 257.
DR   IntAct; P43545; 12.
DR   MINT; P43545; -.
DR   STRING; 4932.YFL059W; -.
DR   iPTMnet; P43545; -.
DR   PaxDb; 4932-YFL059W; -.
DR   PeptideAtlas; P43545; -.
DR   EnsemblFungi; YFL059W_mRNA; YFL059W; YFL059W.
DR   GeneID; 850485; -.
DR   KEGG; sce:YFL059W; -.
DR   AGR; SGD:S000001835; -.
DR   SGD; S000001835; SNZ3.
DR   VEuPathDB; FungiDB:YFL059W; -.
DR   eggNOG; KOG1606; Eukaryota.
DR   HOGENOM; CLU_055352_1_0_1; -.
DR   InParanoid; P43545; -.
DR   OMA; RYANRGW; -.
DR   OrthoDB; 1660966at2759; -.
DR   BioCyc; YEAST:G3O-30408-MONOMER; -.
DR   UniPathway; UPA00245; -.
DR   BioGRID-ORCS; 850485; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P43545; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P43545; protein.
DR   GO; GO:0016843; F:amine-lyase activity; IBA:GO_Central.
DR   GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IDA:SGD.
DR   GO; GO:0042823; P:pyridoxal 5'-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IGI:SGD.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IGI:SGD.
DR   CDD; cd04727; pdxS; 1.
DR   FunFam; 3.20.20.70:FF:000001; Pyridoxine biosynthesis protein PDX1; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01824; PdxS; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001852; PdxS/SNZ.
DR   InterPro; IPR033755; PdxS/SNZ_N.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; NF003215; PRK04180.1; 1.
DR   NCBIfam; TIGR00343; pyridoxal 5'-phosphate synthase lyase subunit PdxS; 1.
DR   PANTHER; PTHR31829; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNZ1-RELATED; 1.
DR   PANTHER; PTHR31829:SF0; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNZ1-RELATED; 1.
DR   Pfam; PF01680; SOR_SNZ; 1.
DR   PIRSF; PIRSF029271; Pdx1; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS01235; PDXS_SNZ_1; 1.
DR   PROSITE; PS51129; PDXS_SNZ_2; 1.
PE   2: Evidence at transcript level;
KW   Lyase; Pyridoxal phosphate; Reference proteome; Schiff base.
FT   CHAIN           1..298
FT                   /note="Probable pyridoxal 5'-phosphate synthase subunit
FT                   SNZ3"
FT                   /id="PRO_0000109360"
FT   ACT_SITE        78
FT                   /note="Schiff-base intermediate with D-ribose 5-phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         21
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         150
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         213
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         234..235
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
SQ   SEQUENCE   298 AA;  32019 MW;  FDBADC5546C460AC CRC64;
     MSEFKVKTGL AQMLKGGVIM DVVTPEQAII AERAGACAVM ALERIPADMR KSGQVCRMSD
     PRMIKEIMEA VSIPVMAKVR IGHFVEAQIL EELQVDYIDE SEVLTPADWT HHIEKHNFKV
     PFVCGAKDLG EALRRINEGA AMIRTKGEAG TGDVSEAVKH ITKIKAEIQQ YKENLKTESD
     FAAKATELRV PVDLLKTTLS EGKLPVVNFA AGGVATPADA ALLMQLGCEG VFVGSGIFKS
     SDPEKLACAI VEATTHYDNP AKLLQVSSDL GDLMGGISIQ SINEAGGKNG ARLSEIGW
//