TAL_ACIC1
ID TAL_ACIC1 Reviewed; 372 AA.
AC A0LTY8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00493};
DE EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00493};
GN Name=tal {ECO:0000255|HAMAP-Rule:MF_00493}; OrderedLocusNames=Acel_1126;
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX NCBI_TaxID=351607;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00493}.
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|HAMAP-Rule:MF_00493};
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:0000255|HAMAP-Rule:MF_00493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00493}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00493}.
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DR EMBL; CP000481; ABK52898.1; -; Genomic_DNA.
DR RefSeq; WP_011719961.1; NC_008578.1.
DR AlphaFoldDB; A0LTY8; -.
DR SMR; A0LTY8; -.
DR STRING; 351607.Acel_1126; -.
DR EnsemblBacteria; ABK52898; ABK52898; Acel_1126.
DR KEGG; ace:Acel_1126; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_050771_1_0_11; -.
DR OMA; EGVYSAI; -.
DR OrthoDB; 417261at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000008221; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR CDD; cd00955; Transaldolase_like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00493; Transaldolase_2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004732; Transaldolase_2.
DR InterPro; IPR018225; Transaldolase_AS.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1.
DR TIGRFAMs; TIGR00876; tal_mycobact; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT CHAIN 1..372
FT /note="Transaldolase"
FT /id="PRO_1000026519"
FT ACT_SITE 140
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
SQ SEQUENCE 372 AA; 40947 MW; 9212E2A9C38C83AA CRC64;
MTDPLAELSA AGVSIWIDDI SRDRLQTGNL AALIRDRHVV GVTTNPTIFG KAIEGSARYQ
DQLRDLAVRG VDVNEALRAL TAYDVRWACD VTRPVFDATD GVDGRVSIEV DPRLAHDTEA
TIAEARALWW LVDRPNLFIK IPATVEGLPA IAQCLAEGIS VNVTLIFSVK RYEQVIDAFF
DGVERAIEAG HDLSRLASVA SFFVSRVDTE VDKRLEKIGG EALQWKAKAA VANARLAYRT
YEEKFATPRW QALAAKGARP QRPLWASTST KDPSLPDTLY VTELVAPGTV NTMPESTLQA
VYDHGVIRGD TIRGYYADAQ ATLDALATLG IDYDDVTDTL EREGVEKFEA SWTELAAAVT
RSLERARRER GR