ID   TALDO_HUMAN             Reviewed;         337 AA.
AC   P37837; B2R8M2; O00751; Q8WV32; Q8WZ45;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   27-MAR-2024, entry version 228.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2 {ECO:0000269|PubMed:18687684, ECO:0000269|PubMed:8955144};
GN   Name=TALDO1 {ECO:0000312|HGNC:HGNC:11559};
GN   Synonyms=TAL, TALDO, TALDOR;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8300619; DOI=10.1016/s0021-9258(17)42020-5;
RA   Banki K., Halladay D.L., Perl A.;
RT   "Cloning and expression of the human gene for transaldolase. A novel highly
RT   repetitive element constitutes an integral part of the coding sequence.";
RL   J. Biol. Chem. 269:2847-2851(1994).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=9339383; DOI=10.1006/geno.1997.4932;
RA   Banki K., Eddy R.L., Shows T.B., Halladay D.L., Bullrich F., Croce C.M.,
RA   Jurecic V., Baldini A., Perl A.;
RT   "The human transaldolase gene (TALDO1) is located on chromosome 11 at
RT   p15.4-p15.5.";
RL   Genomics 45:233-238(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=9524206; DOI=10.1016/s0378-1119(97)00639-2;
RA   Kusuda J., Hirai M., Toyoda A., Tanuma R., Nomura-Kitabayashi A.,
RA   Hashimoto K.;
RT   "Cloning and chromosomal localization of a paralog and a mouse homolog of
RT   the human transaldolase gene.";
RL   Gene 209:13-21(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=10702296; DOI=10.1074/jbc.275.10.7261;
RA   Perl A., Colombo E., Samoilova E., Butler M.C., Banki K.;
RT   "Human transaldolase-associated repetitive elements are transcribed by RNA
RT   polymerase III.";
RL   J. Biol. Chem. 275:7261-7272(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung, and Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-110.
RA   Perl A.;
RT   "Family of active retrotransposons carry two exons of the transaldolase
RT   gene and shows evidence of reverse splicing in human DNA.";
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8955144; DOI=10.1074/jbc.271.51.32994;
RA   Banki K., Hutter E., Colombo E., Gonchoroff N.J., Perl A.;
RT   "Glutathione levels and sensitivity to apoptosis are regulated by changes
RT   in transaldolase expression.";
RL   J. Biol. Chem. 271:32994-33001(1996).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-189.
RX   PubMed=18687684; DOI=10.1074/jbc.m803184200;
RA   Schneider S., Sandalova T., Schneider G., Sprenger G.A., Samland A.K.;
RT   "Replacement of a phenylalanine by a tyrosine in the active site confers
RT   fructose-6-phosphate aldolase activity to the transaldolase of Escherichia
RT   coli and human origin.";
RL   J. Biol. Chem. 283:30064-30072(2008).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-219; LYS-269; LYS-286 AND
RP   LYS-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND SER-256, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX   PubMed=10869557; DOI=10.1016/s0014-5793(00)01658-6;
RA   Thorell S., Gergely P. Jr., Banki K., Perl A., Schneider G.;
RT   "The three-dimensional structure of human transaldolase.";
RL   FEBS Lett. 475:205-208(2000).
RN   [15]
RP   ALTERNATIVE INITIATION.
RX   PubMed=27703206; DOI=10.1038/srep34648;
RA   Moriyama T., Tanaka S., Nakayama Y., Fukumoto M., Tsujimura K., Yamada K.,
RA   Bamba T., Yoneda Y., Fukusaki E., Oka M.;
RT   "Two isoforms of TALDO1 generated by alternative translational initiation
RT   show differential nucleocytoplasmic distribution to regulate the global
RT   metabolic network.";
RL   Sci. Rep. 6:34648-34648(2016).
RN   [16]
RP   VARIANT TALDOD SER-171 DEL.
RX   PubMed=11283793; DOI=10.1086/320108;
RA   Verhoeven N.M., Huck J.H.J., Roos B., Struys E.A., Salomons G.S.,
RA   Douwes A.C., van der Knaap M.S., Jakobs C.;
RT   "Transaldolase deficiency: liver cirrhosis associated with a new inborn
RT   error in the pentose phosphate pathway.";
RL   Am. J. Hum. Genet. 68:1086-1092(2001).
RN   [17]
RP   VARIANT TALDOD CYS-192.
RX   PubMed=25388407; DOI=10.1007/s00431-014-2449-5;
RA   Al-Shamsi A.M., Ben-Salem S., Hertecant J., Al-Jasmi F.;
RT   "Transaldolase deficiency caused by the homozygous p.R192C mutation of the
RT   TALDO1 gene in four Emirati patients with considerable phenotypic
RT   variability.";
RL   Eur. J. Pediatr. 174:661-668(2015).
CC   -!- FUNCTION: Catalyzes the rate-limiting step of the non-oxidative phase
CC       in the pentose phosphate pathway. Catalyzes the reversible conversion
CC       of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into
CC       erythrose-4-phosphate and beta-D-fructose 6-phosphate (PubMed:8955144,
CC       PubMed:18687684). Not only acts as a pentose phosphate pathway enzyme,
CC       but also affects other metabolite pathways by altering its subcellular
CC       localization between the nucleus and the cytoplasm (By similarity).
CC       {ECO:0000250|UniProtKB:Q93092, ECO:0000269|PubMed:18687684,
CC       ECO:0000269|PubMed:8955144}.
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:0000269|PubMed:18687684, ECO:0000269|PubMed:8955144};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17054;
CC         Evidence={ECO:0000305|PubMed:8955144};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17055;
CC         Evidence={ECO:0000305|PubMed:8955144};
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. {ECO:0000250|UniProtKB:Q93092}.
CC   -!- SUBUNIT: Homodimer (PubMed:10869557). Heterodimer with isoform 2 (By
CC       similarity). Interacts with KPNA1 and KPNA4 (By similarity).
CC       {ECO:0000250|UniProtKB:Q93092, ECO:0000269|PubMed:10869557}.
CC   -!- INTERACTION:
CC       P37837; P42858: HTT; NbExp=3; IntAct=EBI-1056712, EBI-466029;
CC       P37837; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-1056712, EBI-750109;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC       {ECO:0000250|UniProtKB:Q93092}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q93092}. Note=Shuttles between the nucleus and
CC       the cytoplasm. Actively transported into the nucleus in an importin
CC       alpha/beta-dependent manner. Exported into the cytoplasm by CRM1.
CC       {ECO:0000250|UniProtKB:Q93092}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000250|UniProtKB:Q93092}. Note=Imported into the nucleus when
CC       incorporated in isoform 1/isoform 2 homodimer.
CC       {ECO:0000250|UniProtKB:Q93092}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1; Synonyms=TALDO1L {ECO:0000303|PubMed:27703206};
CC         IsoId=P37837-1; Sequence=Displayed;
CC       Name=2; Synonyms=TALDO1S {ECO:0000303|PubMed:27703206};
CC         IsoId=P37837-2; Sequence=VSP_061595;
CC   -!- DOMAIN: The first 10 amino acids are essential for nuclear
CC       localization. {ECO:0000250|UniProtKB:Q93092}.
CC   -!- DISEASE: Transaldolase deficiency (TALDOD) [MIM:606003]: An inborn
CC       error of the pentose phosphate pathway resulting in early-onset
CC       multisystem disease. Clinical features include growth retardation,
CC       dysmorphic features, cutis laxa, congenital heart disease,
CC       hepatosplenomegaly, telangiectases of the skin, pancytopenia, and
CC       bleeding tendency. {ECO:0000269|PubMed:11283793,
CC       ECO:0000269|PubMed:25388407}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L19437; AAB53943.1; -; mRNA.
DR   EMBL; AF010400; AAC52068.1; -; Genomic_DNA.
DR   EMBL; AF010398; AAC52068.1; JOINED; Genomic_DNA.
DR   EMBL; AF010399; AAC52068.1; JOINED; Genomic_DNA.
DR   EMBL; AF058913; AAF40478.1; -; Genomic_DNA.
DR   EMBL; AK313427; BAG36219.1; -; mRNA.
DR   EMBL; BC010103; AAH10103.1; -; mRNA.
DR   EMBL; BC018847; AAH18847.2; -; mRNA.
DR   EMBL; L27346; AAL31313.1; -; Genomic_DNA.
DR   CCDS; CCDS7712.1; -. [P37837-1]
DR   PIR; A49985; A49985.
DR   RefSeq; NP_006746.1; NM_006755.1. [P37837-1]
DR   PDB; 1F05; X-ray; 2.45 A; A/B=1-337.
DR   PDBsum; 1F05; -.
DR   AlphaFoldDB; P37837; -.
DR   SMR; P37837; -.
DR   BioGRID; 112751; 116.
DR   IntAct; P37837; 26.
DR   MINT; P37837; -.
DR   STRING; 9606.ENSP00000321259; -.
DR   Allergome; 9551; Hom s Transaldolase.
DR   GlyGen; P37837; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P37837; -.
DR   MetOSite; P37837; -.
DR   PhosphoSitePlus; P37837; -.
DR   SwissPalm; P37837; -.
DR   BioMuta; TALDO1; -.
DR   DMDM; 6648092; -.
DR   OGP; P37837; -.
DR   REPRODUCTION-2DPAGE; IPI00744692; -.
DR   CPTAC; CPTAC-2777; -.
DR   EPD; P37837; -.
DR   jPOST; P37837; -.
DR   MassIVE; P37837; -.
DR   MaxQB; P37837; -.
DR   PaxDb; 9606-ENSP00000321259; -.
DR   PeptideAtlas; P37837; -.
DR   PRIDE; P37837; -.
DR   ProteomicsDB; 55278; -.
DR   Pumba; P37837; -.
DR   Antibodypedia; 22640; 317 antibodies from 32 providers.
DR   DNASU; 6888; -.
DR   Ensembl; ENST00000319006.8; ENSP00000321259.3; ENSG00000177156.11. [P37837-1]
DR   GeneID; 6888; -.
DR   KEGG; hsa:6888; -.
DR   MANE-Select; ENST00000319006.8; ENSP00000321259.3; NM_006755.2; NP_006746.1.
DR   UCSC; uc001lqz.4; human. [P37837-1]
DR   AGR; HGNC:11559; -.
DR   CTD; 6888; -.
DR   DisGeNET; 6888; -.
DR   GeneCards; TALDO1; -.
DR   HGNC; HGNC:11559; TALDO1.
DR   HPA; ENSG00000177156; Low tissue specificity.
DR   MalaCards; TALDO1; -.
DR   MIM; 602063; gene.
DR   MIM; 606003; phenotype.
DR   neXtProt; NX_P37837; -.
DR   OpenTargets; ENSG00000177156; -.
DR   Orphanet; 101028; Transaldolase deficiency.
DR   PharmGKB; PA36328; -.
DR   VEuPathDB; HostDB:ENSG00000177156; -.
DR   eggNOG; KOG2772; Eukaryota.
DR   GeneTree; ENSGT00390000017361; -.
DR   HOGENOM; CLU_047470_0_1_1; -.
DR   InParanoid; P37837; -.
DR   OMA; THAEFLW; -.
DR   OrthoDB; 1972468at2759; -.
DR   PhylomeDB; P37837; -.
DR   TreeFam; TF300757; -.
DR   PathwayCommons; P37837; -.
DR   Reactome; R-HSA-163754; Insulin effects increased synthesis of Xylulose-5-Phosphate.
DR   Reactome; R-HSA-6791055; TALDO1 deficiency: failed conversion of SH7P, GA3P to Fru(6)P, E4P.
DR   Reactome; R-HSA-6791462; TALDO1 deficiency: failed conversion of Fru(6)P, E4P to SH7P, GA3P.
DR   Reactome; R-HSA-71336; Pentose phosphate pathway.
DR   Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR   Reactome; R-HSA-9818028; NFE2L2 regulates pentose phosphate pathway genes.
DR   SignaLink; P37837; -.
DR   SIGNOR; P37837; -.
DR   UniPathway; UPA00115; UER00414.
DR   BioGRID-ORCS; 6888; 22 hits in 1162 CRISPR screens.
DR   ChiTaRS; TALDO1; human.
DR   EvolutionaryTrace; P37837; -.
DR   GenomeRNAi; 6888; -.
DR   Pharos; P37837; Tbio.
DR   PRO; PR:P37837; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P37837; Protein.
DR   Bgee; ENSG00000177156; Expressed in trabecular bone tissue and 207 other cell types or tissues.
DR   ExpressionAtlas; P37837; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0048029; F:monosaccharide binding; IEA:Ensembl.
DR   GO; GO:0004801; F:transaldolase activity; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:Ensembl.
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; Aldolase class I; 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   NCBIfam; TIGR00874; talAB; 1.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   PANTHER; PTHR10683:SF18; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
DR   Genevisible; P37837; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative initiation; Cytoplasm;
KW   Disease variant; Nucleus; Pentose shunt; Phosphoprotein;
KW   Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..337
FT                   /note="Transaldolase"
FT                   /id="PRO_0000173564"
FT   MOTIF           1..10
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q93092"
FT   ACT_SITE        142
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000269|PubMed:10869557"
FT   MOD_RES         115
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q93092"
FT   MOD_RES         219
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         256
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         269
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         286
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         321
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1..10
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305|PubMed:27703206"
FT                   /id="VSP_061595"
FT   VARIANT         171
FT                   /note="Missing (in TALDOD)"
FT                   /evidence="ECO:0000269|PubMed:11283793"
FT                   /id="VAR_011511"
FT   VARIANT         192
FT                   /note="R -> C (in TALDOD)"
FT                   /evidence="ECO:0000269|PubMed:25388407"
FT                   /id="VAR_086514"
FT   MUTAGEN         189
FT                   /note="F->Y: Confers fructose-6-phosphate aldolase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:18687684"
FT   HELIX           14..21
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   STRAND          22..27
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   TURN            31..34
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   STRAND          40..43
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           46..53
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           59..72
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           76..98
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   STRAND          103..106
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           109..111
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           115..131
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           136..138
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   STRAND          139..144
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           147..160
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           172..180
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   STRAND          184..190
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           191..200
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           208..210
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           212..226
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   STRAND          232..236
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           241..245
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   TURN            246..249
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   STRAND          250..255
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           257..265
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           276..281
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           291..299
FT                   /evidence="ECO:0007829|PDB:1F05"
FT   HELIX           302..330
FT                   /evidence="ECO:0007829|PDB:1F05"
SQ   SEQUENCE   337 AA;  37540 MW;  8CB4992AEF364E64 CRC64;
     MSSSPVKRQR MESALDQLKQ FTTVVADTGD FHAIDEYKPQ DATTNPSLIL AAAQMPAYQE
     LVEEAIAYGR KLGGSQEDQI KNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA
     RARRLIELYK EAGISKDRIL IKLSSTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE
     AGVTLISPFV GRILDWHVAN TDKKSYEPLE DPGVKSVTKI YNYYKKFSYK TIVMGASFRN
     TGEIKALAGC DFLTISPKLL GELLQDNAKL VPVLSAKAAQ ASDLEKIHLD EKSFRWLHNE
     DQMAVEKLSD GIRKFAADAV KLERMLTERM FNAENGK
//