ID A0A1U6GMV4_9GAMM Unreviewed; 313 AA.
AC A0A1U6GMV4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=transaldolase {ECO:0000256|ARBA:ARBA00013151};
DE EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151};
GN Name=tal {ECO:0000313|EMBL:SLJ84816.1};
GN ORFNames=DABAL43B_1621 {ECO:0000313|EMBL:SLJ84816.1};
OS Psychrobacter sp. DAB_AL43B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1028416 {ECO:0000313|EMBL:SLJ84816.1, ECO:0000313|Proteomes:UP000190084};
RN [1] {ECO:0000313|EMBL:SLJ84816.1, ECO:0000313|Proteomes:UP000190084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAB_AL43B {ECO:0000313|EMBL:SLJ84816.1};
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 (MAR-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|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; LT799838; SLJ84816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U6GMV4; -.
DR STRING; 1028416.DABAL43B_1621; -.
DR KEGG; psyc:DABAL43B_1621; -.
DR OrthoDB; 9809101at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000190084; Chromosome i.
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; PS01054; TRANSALDOLASE_1; 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:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SLJ84816.1}.
SQ SEQUENCE 313 AA; 34456 MW; 1A900275A658F8F8 CRC64;
MSALQQLRTM TTIVADTGDL AAIARLKPID ATTNPSLITK ALINPDNEAM LSEAMSRHRD
DIDAVIDELT IQIGCDILAL IEGRVSTEVD ARLSYDTQAT IDKALEFMEA YQKAGIDSER
VLIKMAATWQ GIEAARYLET QNIHCNLTLL FGQHQAIACA DAGVTLISPF VGRILDWQKR
QQNRQNVPAS DDMGVQSVKL IYQYYKQHGY NTQVMGASFR STEQILALAG CDLLTIAPNL
IDELAAMDVE VTRQLSPSMS MDLADMTRVS LTSEEFSTAY QQDTVTQDLL PKGIDGFIGA
RDELAAMLAT MRD
//