ID A0A1I5DPR3_9MICO Unreviewed; 370 AA.
AC A0A1I5DPR3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 {ECO:0000256|HAMAP-Rule:MF_00493};
GN ORFNames=SAMN05216219_3031 {ECO:0000313|EMBL:SFO01204.1};
OS Mycetocola miduiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Mycetocola.
OX NCBI_TaxID=995034 {ECO:0000313|EMBL:SFO01204.1, ECO:0000313|Proteomes:UP000198867};
RN [1] {ECO:0000313|Proteomes:UP000198867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11101 {ECO:0000313|Proteomes:UP000198867};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FOVM01000010; SFO01204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5DPR3; -.
DR STRING; 995034.SAMN05216219_3031; -.
DR OrthoDB; 9809101at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000198867; 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:UP000198867};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00493};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00493}.
FT ACT_SITE 142
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 370 AA; 39174 MW; 06305FED712391D5 CRC64;
MTENTPTAQL SAAGVSIWLD DLSRGRMDSG SLQELIDTRN VVGVTTNPTI FAGALSNGES
YAEQVSELAA AGKDVTEAVF EITTADVARA ADVFRPIYDA SNGFDGRVSI EVEPRLAHDA
AATIAEAKEL WAKIDKPNVM IKIPATVEGL EAITAAIGAG ISVNVTLIFS LQRYREVMNA
YLTGLEQAKA AGIDLSTIHS VASFFVSRVD TEIDKRLVAV GTDEALALKS KAGVANAQLA
YEVFEQTFAS ERAAGLLAAG ANKQRPLWAS TGVKDPSLPD TLYVTQLVAD GVVNTMPEKT
LEATFDHGQI DGDTVTGSYD EANKVLDAIA GLGISYDEVT ALLEKEGVEK FIVSWNELLD
TVTEALAAAK
//
