TAL_KOCRD
ID TAL_KOCRD Reviewed; 368 AA.
AC B2GH92;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=KRH_12180;
OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX NCBI_TaxID=378753;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX PubMed=18408034; DOI=10.1128/jb.01853-07;
RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL J. Bacteriol. 190:4139-4146(2008).
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; AP009152; BAG29565.1; -; Genomic_DNA.
DR RefSeq; WP_012398286.1; NC_010617.1.
DR AlphaFoldDB; B2GH92; -.
DR SMR; B2GH92; -.
DR STRING; 378753.KRH_12180; -.
DR EnsemblBacteria; BAG29565; BAG29565; KRH_12180.
DR KEGG; krh:KRH_12180; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_050771_1_0_11; -.
DR OMA; RMMTTAD; -.
DR OrthoDB; 417261at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000008838; 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..368
FT /note="Transaldolase"
FT /id="PRO_1000126267"
FT ACT_SITE 140
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00493"
SQ SEQUENCE 368 AA; 39513 MW; FE62F2CD9962AE5C CRC64;
MTTPTQKLSD AGVSIWLDDL SRQRLTSGNL QKLIDTENVV GVTTNPTIFA AALADGESYR
EQVAELAAAD TSVDDAVFRI TTDDVRDACD LFAPIAEATQ GVDGRVSIEV DPRLAQDADA
TSAMAQKLSQ TIDRPNALIK IPATEKGLPS IAATVAEGIS VNVTLIFSLE RYRGVINAYM
EGLERALENG KDLSTIHSVA SFFVSRVDTE IDKRLDAVGS SEATALKGKA GLANARLAYQ
VYEQSLDTER WKRLAAAGAN PQRPLWASTG VKDPSLPDTL YVTELVAPNT VNTMPEKTLD
ATFDHAEVTG DTVTGTYEQS AEVLDAIAEQ GVSYQEVVAQ LETEGLQKFD ASWEELLSTV
RAALDAAR
