SNZ3_YEAST
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 03-AUG-2022, entry version 158.
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 = 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: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 IntAct; P43545; 12.
DR MINT; P43545; -.
DR STRING; 4932.YFL059W; -.
DR iPTMnet; P43545; -.
DR MaxQB; P43545; -.
DR PaxDb; P43545; -.
DR PRIDE; P43545; -.
DR EnsemblFungi; YFL059W_mRNA; YFL059W; YFL059W.
DR GeneID; 850485; -.
DR KEGG; sce:YFL059W; -.
DR SGD; S000001835; SNZ3.
DR VEuPathDB; FungiDB:YFL059W; -.
DR eggNOG; KOG1606; Eukaryota.
DR GeneTree; ENSGT00390000018460; -.
DR HOGENOM; CLU_055352_1_0_1; -.
DR InParanoid; P43545; -.
DR OMA; RYANRGW; -.
DR BioCyc; YEAST:G3O-30408-MON; -.
DR UniPathway; UPA00245; -.
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:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0042823; P:pyridoxal 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 Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR31829; PTHR31829; 1.
DR Pfam; PF01680; SOR_SNZ; 1.
DR PIRSF; PIRSF029271; Pdx1; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00343; TIGR00343; 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
