TALDO_HUMAN
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 03-AUG-2022, entry version 219.
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}; 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; -.
DR PIR; A49985; A49985.
DR RefSeq; NP_006746.1; NM_006755.1.
DR PDB; 1F05; X-ray; 2.45 A; A/B=1-337.
DR PDBsum; 1F05; -.
DR AlphaFoldDB; P37837; -.
DR SMR; P37837; -.
DR BioGRID; 112751; 92.
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 EPD; P37837; -.
DR jPOST; P37837; -.
DR MassIVE; P37837; -.
DR MaxQB; P37837; -.
DR PaxDb; P37837; -.
DR PeptideAtlas; P37837; -.
DR PRIDE; P37837; -.
DR ProteomicsDB; 55278; -.
DR Antibodypedia; 22640; 278 antibodies from 32 providers.
DR DNASU; 6888; -.
DR Ensembl; ENST00000319006.8; ENSP00000321259.3; ENSG00000177156.11.
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.
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; KFGYKTL; -.
DR OrthoDB; 1402459at2759; -.
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-9759194; Nuclear events mediated by NFE2L2.
DR SignaLink; P37837; -.
DR SIGNOR; P37837; -.
DR UniPathway; UPA00115; UER00414.
DR BioGRID-ORCS; 6888; 22 hits in 1082 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 205 other tissues.
DR ExpressionAtlas; P37837; baseline and differential.
DR Genevisible; P37837; HS.
DR GO; GO:0005737; C:cytoplasm; IDA: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:0019682; P:glyceraldehyde-3-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; -; 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 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
