ID A0A172WD61_BUCSC Unreviewed; 317 AA.
AC A0A172WD61;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=XW81_00435 {ECO:0000313|EMBL:ANF16901.1};
OS Buchnera aphidicola subsp. Schlechtendalia chinensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=118110 {ECO:0000313|EMBL:ANF16901.1, ECO:0000313|Proteomes:UP000077654};
RN [1] {ECO:0000313|EMBL:ANF16901.1, ECO:0000313|Proteomes:UP000077654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC {ECO:0000313|EMBL:ANF16901.1,
RC ECO:0000313|Proteomes:UP000077654};
RA Zhang Y.;
RT "Buchnera aphidicola assembly.";
RL Submitted (APR-2015) 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_00492, 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|ARBA:ARBA00001469, ECO:0000256|HAMAP-
CC Rule:MF_00492, 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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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; CP011299; ANF16901.1; -; Genomic_DNA.
DR RefSeq; WP_075473867.1; NZ_CP011299.1.
DR AlphaFoldDB; A0A172WD61; -.
DR STRING; 118110.XW81_00435; -.
DR PATRIC; fig|118110.3.peg.81; -.
DR OrthoDB; 9809101at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000077654; 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; 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:SF16; TRANSALDOLASE A; 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:UP000077654};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00492};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00492}.
FT ACT_SITE 131
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00492"
SQ SEQUENCE 317 AA; 35964 MW; 2E97B6D2789D9C5C CRC64;
MNQLESLKKY SKVVVDSGDI NLIRKYLPED ATTNPSLVLK AIVSPENEII VRESITYAKK
KGGTYDFQLL NAVDKISVIL GKKILEVISG RVSTEIDAHL SFNTDLCIER SKKIISMYEE
EGIHRSKILI KLAATWECIK ASEELKNFDI DCNLTLLFSF AQARACAEAG VFLISPFVGR
IYDWYKSKLL IKEYLAQEDP GVQSVRNIYN YYKKHGYKTI IMGASFRNIE QVLELSGCDC
LTISPNLLEK LQCNESVVVQ KLYSSCNVAK KPISILSQSD FSWLHNTEPM AVEKLSEGIR
QFSHDQKELE AIIRNKM
//
