ID L7ETD3_9ACTN Unreviewed; 382 AA.
AC L7ETD3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00493};
DE EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00493};
GN Name=tal_2 {ECO:0000313|EMBL:ELP61976.1};
GN Synonyms=tal {ECO:0000256|HAMAP-Rule:MF_00493};
GN ORFNames=STRTUCAR8_07658 {ECO:0000313|EMBL:ELP61976.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP61976.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP61976.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP61976.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000256|ARBA:ARBA00003518,
CC ECO:0000256|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:0000256|ARBA:ARBA00001469, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00004857, ECO:0000256|HAMAP-
CC Rule:MF_00493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008426, ECO:0000256|HAMAP-Rule:MF_00493}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELP61976.1}.
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DR EMBL; AEJB01000642; ELP61976.1; -; Genomic_DNA.
DR RefSeq; WP_006383114.1; NZ_AEJB01000642.1.
DR AlphaFoldDB; L7ETD3; -.
DR STRING; 85558.T45_05954; -.
DR PATRIC; fig|698760.3.peg.9054; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000010931; 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; cd00955; Transaldolase_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR00876; tal_mycobact; 1.
DR PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF31; TRANSALDOLASE; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00493};
KW Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00493};
KW Reference proteome {ECO:0000313|Proteomes:UP000010931};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00493};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000313|EMBL:ELP61976.1}.
FT ACT_SITE 141
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 382 AA; 41530 MW; F1E48CE0E74286BF CRC64;
MTDDVLKRLS DEGVAIWLDD LSRKRITSGN LAELIERRHV VGVTTNPTIF EQAVGRGDDY
ADQLRELALR GVTVSEAVRM ITTADVRDAA DILRPVFDAT GGRDGWVSIE VDPRLAHGTA
ATVAEAKQLA WLVDRPNTLI KIPATNAGLL AITEVVGLGI SVNVTLIFSL ERHREVMDAY
LSGLEKAKER GLDLSKIHSV ASFFVSRVDA EIDKRLDAID TPEAEEARGK AALANARLAY
QAFEEVFGSA DGSTQPSGRW AALDRTRANR QRPLWASTGV KDPSYPDTLY VTELVAPGTV
NTMPEATLDA TADHGEITGN TIAGTYKQAR SDLDALAGMG ISFRYVAQVL ETEGLQKFQQ
SWDSLLNAVR HARPPKARVI AD
//
