TAL2_YEAST
ID TAL2_YEAST Reviewed; 333 AA.
AC P53228; D6VUI1; Q6Q5P8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Transaldolase NQM1;
DE EC=2.2.1.2;
DE AltName: Full=Non-quiescent mutant protein 1;
GN Name=NQM1; OrderedLocusNames=YGR043C;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [5]
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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=18831051; DOI=10.1002/prot.22237;
RA Huang H., Rong H., Li X., Tong S., Zhu Z., Niu L., Teng M.;
RT "The crystal structure and identification of NQM1/YGR043C, a transaldolase
RT from Saccharomyces cerevisiae.";
RL Proteins 73:1076-1081(2008).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC beta-D-fructose 6-phosphate + D-erythrose 4-phosphate;
CC Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10019,
CC ECO:0000269|PubMed:18831051};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage):
CC step 2/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18831051}.
CC -!- MISCELLANEOUS: Present with 1920 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z72828; CAA97042.1; -; Genomic_DNA.
DR EMBL; AY557832; AAS56158.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08142.1; -; Genomic_DNA.
DR PIR; S64337; S64337.
DR RefSeq; NP_011557.1; NM_001181172.1.
DR PDB; 3CQ0; X-ray; 1.90 A; A/B=1-333.
DR PDBsum; 3CQ0; -.
DR AlphaFoldDB; P53228; -.
DR SMR; P53228; -.
DR BioGRID; 33290; 56.
DR MINT; P53228; -.
DR STRING; 4932.YGR043C; -.
DR iPTMnet; P53228; -.
DR MaxQB; P53228; -.
DR PaxDb; P53228; -.
DR PRIDE; P53228; -.
DR EnsemblFungi; YGR043C_mRNA; YGR043C; YGR043C.
DR GeneID; 852934; -.
DR KEGG; sce:YGR043C; -.
DR SGD; S000003275; NQM1.
DR VEuPathDB; FungiDB:YGR043C; -.
DR eggNOG; KOG2772; Eukaryota.
DR GeneTree; ENSGT00390000017361; -.
DR HOGENOM; CLU_047470_0_1_1; -.
DR InParanoid; P53228; -.
DR OMA; DTGDFKQ; -.
DR BioCyc; YEAST:YGR043C-MON; -.
DR BRENDA; 2.2.1.2; 984.
DR UniPathway; UPA00115; UER00414.
DR EvolutionaryTrace; P53228; -.
DR PRO; PR:P53228; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53228; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004801; F:transaldolase activity; IDA:SGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR CDD; cd00957; Transaldolase_TalAB; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004730; Transaldolase_1.
DR InterPro; IPR018225; Transaldolase_AS.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR PANTHER; PTHR10683:SF18; PTHR10683:SF18; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR TIGRFAMs; TIGR00874; talAB; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT CHAIN 1..333
FT /note="Transaldolase NQM1"
FT /id="PRO_0000173575"
FT ACT_SITE 144
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10019"
FT CONFLICT 290
FT /note="F -> S (in Ref. 3; AAS56158)"
FT /evidence="ECO:0000305"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:3CQ0"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3CQ0"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 78..98
FT /evidence="ECO:0007829|PDB:3CQ0"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3CQ0"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:3CQ0"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:3CQ0"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:3CQ0"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 213..228
FT /evidence="ECO:0007829|PDB:3CQ0"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:3CQ0"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:3CQ0"
FT HELIX 305..333
FT /evidence="ECO:0007829|PDB:3CQ0"
SQ SEQUENCE 333 AA; 37254 MW; 6492030A7DA3D343 CRC64;
MSEPSEKKQK VATSSLEQLK KAGTHVVADS GDFEAISKYE PQDSTTNPSL ILAASKLEKY
ARFIDAAVEY GRKHGKTDHE KIENAMDKIL VEFGTQILKV VPGRVSTEVD ARLSFDKKAT
VKKALHIIKL YKDAGVPKER VLIKIASTWE GIQAARELEV KHGIHCNMTL LFSFTQAVAC
AEANVTLISP FVGRIMDFYK ALSGKDYTAE TDPGVLSVKK IYSYYKRHGY ATEVMAASFR
NLDELKALAG IDNMTLPLNL LEQLYESTDP IENKLNSESA KEEGVEKVSF INDEPHFRYV
LNEDQMATEK LSDGIRKFSA DIEALYKLVE EKM
