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Database: UniProt
Entry: D4G8X0_RIEPU
LinkDB: D4G8X0_RIEPU
Original site: D4G8X0_RIEPU 
ID   D4G8X0_RIEPU            Unreviewed;       322 AA.
AC   D4G8X0;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=transaldolase {ECO:0000256|ARBA:ARBA00013151};
DE            EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151};
GN   OrderedLocusNames=RIEPE_0546 {ECO:0000313|EMBL:ADD79526.1};
OS   Riesia pediculicola (strain USDA).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Candidatus Riesia.
OX   NCBI_TaxID=515618 {ECO:0000313|EMBL:ADD79526.1, ECO:0000313|Proteomes:UP000001700};
RN   [1] {ECO:0000313|EMBL:ADD79526.1, ECO:0000313|Proteomes:UP000001700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA {ECO:0000313|EMBL:ADD79526.1,
RC   ECO:0000313|Proteomes:UP000001700};
RA   Kirkness E.F.;
RT   "Genome sequence of Riesia pediculicola USDA.";
RL   Submitted (MAY-2008) 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   -!- 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};
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}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008012}.
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DR   EMBL; CP001085; ADD79526.1; -; Genomic_DNA.
DR   RefSeq; WP_013087516.1; NC_014109.1.
DR   AlphaFoldDB; D4G8X0; -.
DR   STRING; 515618.RIEPE_0546; -.
DR   KEGG; rip:RIEPE_0546; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_047470_0_1_6; -.
DR   OMA; KFGYKTL; -.
DR   OrthoDB; 9809101at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000001700; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   CDD; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004730; Transaldolase_1.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   PANTHER; PTHR10683:SF18; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW   Transferase {ECO:0000313|EMBL:ADD79526.1}.
SQ   SEQUENCE   322 AA;  37564 MW;  04B1E3091E5AE241 CRC64;
     MNKLISLKKI TNVMADTSDL DEIQKYRPND VTTNPSSILS FVENKKNDYF LKTIFHSFDF
     DNFSRETIGS KLYEIILIRL ASEIVKMIPG RVSIEMNSRF SYDEENCFEI SKKIIQSLEE
     EGIKKNRILI KIASTWQGIQ AAKRLEKIGI NCNLTLIFSF AQAIACADSK VHSISPFVGR
     ITDWYQNNEN KKKLDDQEDP GINFVKNIYK YYKSNGFNTN IIGASIRSTK HIFELSGCDY
     LTIPPQLLQK LSCSRGEIKR KIIKKTYLNK YQKNEKMTES DFYWKHCSDN MANFSLSNGI
     HKFFVDQEKL KRFILNRFYK NF
//
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