TAL1_SCHPO
ID TAL1_SCHPO Reviewed; 322 AA.
AC O42700;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Transaldolase;
DE EC=2.2.1.2;
GN Name=tal1; ORFNames=SPCC1020.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 111-322.
RA Kawamukai M.;
RT "S.pombe transaldolase homolog.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268 AND SER-269, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000250}.
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 -!- 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:0000250}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329672; CAA18994.1; -; Genomic_DNA.
DR EMBL; AB010049; BAA24182.1; -; mRNA.
DR PIR; T40834; T40834.
DR PIR; T43308; T43308.
DR RefSeq; NP_587953.1; NM_001022944.2.
DR AlphaFoldDB; O42700; -.
DR SMR; O42700; -.
DR BioGRID; 275551; 39.
DR STRING; 4896.SPCC1020.06c.1; -.
DR iPTMnet; O42700; -.
DR MaxQB; O42700; -.
DR PaxDb; O42700; -.
DR PRIDE; O42700; -.
DR EnsemblFungi; SPCC1020.06c.1; SPCC1020.06c.1:pep; SPCC1020.06c.
DR PomBase; SPCC1020.06c; tal1.
DR VEuPathDB; FungiDB:SPCC1020.06c; -.
DR eggNOG; KOG2772; Eukaryota.
DR HOGENOM; CLU_047470_0_1_1; -.
DR InParanoid; O42700; -.
DR OMA; KFGYKTL; -.
DR PhylomeDB; O42700; -.
DR Reactome; R-SPO-163754; Insulin effects increased synthesis of Xylulose-5-Phosphate.
DR Reactome; R-SPO-71336; Pentose phosphate pathway.
DR UniPathway; UPA00115; UER00414.
DR PRO; PR:O42700; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004801; F:transaldolase activity; IDA:PomBase.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; EXP:PomBase.
DR CDD; cd00957; Transaldolase_TalAB; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00492; Transaldolase_1; 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 Pentose shunt; Phosphoprotein; Reference proteome; Schiff base;
KW Transferase.
FT CHAIN 1..322
FT /note="Transaldolase"
FT /id="PRO_0000173573"
FT ACT_SITE 132
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 322 AA; 35238 MW; 0807DC610EEB2E7E CRC64;
MSSLEQLKAT GTVVVSDTGD FESIAKYKPQ DATTNPSLIL AASKKPQYAA LVDAAVDYAK
AKGGSINSQI EIAFDRLLIE FGTKILAIVP GRVSTEVDAR YSFDTQTTIE KARHLIKLYE
AEGIGRERVL IKIASTYEGI QAAKQLEEEG IHCNLTLLFS FVQAVACAEA NVTLISPFVG
RILDFYKAKN NRDYTAQEDP GVVSVSNIFN YYKKFGYKTI VMGASFRNVG EIKELAGVDF
LTISPALLEQ LNNSTDAVPK KLDASKASSL NLEKVSYLTD EPKFRFDFNN DEMAVVKLST
GIAAFAKDAD TLRTILKAKL EA
