TAL_RHILO
ID TAL_RHILO Reviewed; 218 AA.
AC Q98EV0;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Probable transaldolase;
DE EC=2.2.1.2;
GN Name=tal; OrderedLocusNames=mlr4072;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3B subfamily.
CC {ECO:0000305}.
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DR EMBL; BA000012; BAB50817.1; -; Genomic_DNA.
DR RefSeq; WP_010912160.1; NC_002678.2.
DR AlphaFoldDB; Q98EV0; -.
DR SMR; Q98EV0; -.
DR STRING; 266835.14024213; -.
DR EnsemblBacteria; BAB50817; BAB50817; BAB50817.
DR GeneID; 66681422; -.
DR KEGG; mlo:mlr4072; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_079764_0_0_5; -.
DR OMA; VRHPMHV; -.
DR OrthoDB; 784333at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
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; cd00956; Transaldolase_FSA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00494; Transaldolase_3b; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR022999; Transaldolase_3B.
DR InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR InterPro; IPR018225; Transaldolase_AS.
DR InterPro; IPR033919; TSA/FSA_arc/bac.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR TIGRFAMs; TIGR00875; fsa_talC_mipB; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Pentose shunt; Schiff base; Transferase.
FT CHAIN 1..218
FT /note="Probable transaldolase"
FT /id="PRO_0000173679"
FT ACT_SITE 83
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 218 AA; 23408 MW; 6462C0FB45588A64 CRC64;
MKFFVDTADI KDIRELNDLG LLDGVTTNPS LILKSGGKIA DVTKQICDIV QGPVSAEVVA
TEYKDMMAEA EVLAKIAPNV CIKVPLTLDG LKACKTIRTQ MNRMVNVTLC FSANQALLAA
KAGASFISPF VGRIDDTGSD GMELIQEIRQ IYDNYDYQTE ILTASVRTVN HVKQAALIGA
DVITAPPATL KALVNHPLTD KGLAAFLADW AKTGQKIG
