SNZ2_YEAST
ID SNZ2_YEAST Reviewed; 298 AA.
AC P53824; D6W0L4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Probable pyridoxal 5'-phosphate synthase subunit SNZ2;
DE Short=PLP synthase subunit SNZ2;
DE EC=4.3.3.6;
DE AltName: Full=PDX1 homolog 2;
DE Short=Pdx1.2;
GN Name=SNZ2; OrderedLocusNames=YNL333W; ORFNames=N0290;
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=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 PROBABLE FUNCTION, INDUCTION, AND INTERACTION WITH THI11.
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; Z71608; CAA96266.1; -; Genomic_DNA.
DR EMBL; Z71609; CAA96267.1; -; Genomic_DNA.
DR EMBL; AY692873; AAT92892.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10230.1; -; Genomic_DNA.
DR RefSeq; NP_014066.1; NM_001183171.1.
DR AlphaFoldDB; P53824; -.
DR SMR; P53824; -.
DR BioGRID; 35508; 27.
DR DIP; DIP-1695N; -.
DR IntAct; P53824; 12.
DR MINT; P53824; -.
DR STRING; 4932.YNL333W; -.
DR MaxQB; P53824; -.
DR PaxDb; P53824; -.
DR PRIDE; P53824; -.
DR EnsemblFungi; YNL333W_mRNA; YNL333W; YNL333W.
DR GeneID; 855383; -.
DR KEGG; sce:YNL333W; -.
DR SGD; S000005277; SNZ2.
DR VEuPathDB; FungiDB:YNL333W; -.
DR eggNOG; KOG1606; Eukaryota.
DR GeneTree; ENSGT00390000018460; -.
DR HOGENOM; CLU_055352_1_0_1; -.
DR InParanoid; P53824; -.
DR OMA; FGEMASI; -.
DR BioCyc; YEAST:G3O-33316-MON; -.
DR UniPathway; UPA00245; -.
DR PRO; PR:P53824; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53824; protein.
DR GO; GO:0016843; F:amine-lyase activity; IBA:GO_Central.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; ISS:SGD.
DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-EC.
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 GO; GO:0042819; P:vitamin B6 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 1: Evidence at protein level;
KW Lyase; Pyridoxal phosphate; Reference proteome; Schiff base.
FT CHAIN 1..298
FT /note="Probable pyridoxal 5'-phosphate synthase subunit
FT SNZ2"
FT /id="PRO_0000109359"
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; 32033 MW; EE02E7C546C460AC 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 AKLLQISSDL GDLMGGISIQ SINEAGGKNG ARLSEIGW
