ID A0A1W1VWF2_9DEIO Unreviewed; 320 AA.
AC A0A1W1VWF2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00492};
DE EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00492};
GN Name=tal {ECO:0000256|HAMAP-Rule:MF_00492};
GN ORFNames=SAMN00790413_06132 {ECO:0000313|EMBL:SMB97695.1};
OS Deinococcus hopiensis KR-140.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=695939 {ECO:0000313|EMBL:SMB97695.1, ECO:0000313|Proteomes:UP000192582};
RN [1] {ECO:0000313|EMBL:SMB97695.1, ECO:0000313|Proteomes:UP000192582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KR-140 {ECO:0000313|EMBL:SMB97695.1,
RC ECO:0000313|Proteomes:UP000192582};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000256|HAMAP-Rule:MF_00492,
CC ECO:0000256|RuleBase:RU004155}.
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:0000256|HAMAP-Rule:MF_00492,
CC ECO:0000256|RuleBase:RU004155};
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:0000256|ARBA:ARBA00004857, ECO:0000256|HAMAP-
CC Rule:MF_00492, ECO:0000256|RuleBase:RU004155}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00492}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00008012, ECO:0000256|HAMAP-Rule:MF_00492,
CC ECO:0000256|RuleBase:RU004155}.
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DR EMBL; FWWU01000011; SMB97695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1VWF2; -.
DR STRING; 695939.SAMN00790413_06132; -.
DR OrthoDB; 9807051at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000192582; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00492};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126, ECO:0000256|HAMAP-
KW Rule:MF_00492}; Reference proteome {ECO:0000313|Proteomes:UP000192582};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00492};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00492}.
FT ACT_SITE 128
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00492"
SQ SEQUENCE 320 AA; 35412 MW; 4E458DBBF1B50D94 CRC64;
MPSKLEQLRK FSVVVADTGD FTAISQYRPR DCTTNPSLIL KAARQPESAE LVNEVVTDCA
RRGERTEEML DTLAVRFGVE LTKLVPGDVS TEVDAMLSFD VTAMVTKARA LIERYEKWGV
DRERVLIKLA ATWEGIRAAE VLEREGIRCN LTLVFSLEQA VACAQAGVFL ISPFVGRITD
WYKKAEGRNS YPVDDDPGVG SVRRIYTHFK SQGYATAVMG ASFRSAAQVE ALAGCDRLTV
SPTLLSDLDQ DQGMLTRRLG SAQAATPPTG PITEPAFRWS LLENQMAGEK LTEGLRVFHM
DYLSLKREIQ TKVQGQKVLT
//
