ID A0A1D8FYU4_9ACTN Unreviewed; 372 AA.
AC A0A1D8FYU4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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_1 {ECO:0000313|EMBL:AOT58336.1};
GN Synonyms=tal {ECO:0000256|HAMAP-Rule:MF_00493};
GN ORFNames=A4G23_01145 {ECO:0000313|EMBL:AOT58336.1};
OS Streptomyces rubrolavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT58336.1, ECO:0000313|Proteomes:UP000095349};
RN [1] {ECO:0000313|EMBL:AOT58336.1, ECO:0000313|Proteomes:UP000095349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJM4426 {ECO:0000313|EMBL:AOT58336.1,
RC ECO:0000313|Proteomes:UP000095349};
RA Kim J.-G.;
RT "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL Submitted (SEP-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; CP017316; AOT58336.1; -; Genomic_DNA.
DR RefSeq; WP_069975921.1; NZ_CP017316.1.
DR AlphaFoldDB; A0A1D8FYU4; -.
DR STRING; 285473.A4G23_01145; -.
DR KEGG; srn:A4G23_01145; -.
DR PATRIC; fig|285473.5.peg.1193; -.
DR OrthoDB; 9809101at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000095349; 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; 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:UP000095349};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00493};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000313|EMBL:AOT58336.1}.
FT ACT_SITE 140
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 372 AA; 40590 MW; 95CEB679E85DA79F CRC64;
MTDALKRLSD EGVAIWLDDL SRKRITSGNL AELMDEQHVV GVTTNPSIFQ KAISEGHGYD
VQLTDLAARK VTVEEAIRMI TTADVRDAAD ILRPVFDATQ GQDGRVSIEV DPRLAHDTRA
TVAEAKQLAW LVDRPNTLIK IPATQAGLPA ITEAIGLGIS VNVTLIFSLE RYRLVMDAYL
AGLEKAKERG LDLSKIHSVA SFFVSRVDTE IDKRLDAIGT PEAKELRGKA ALANARLAYE
AYEEVFGSER WAALDRAQAN RQRPLWASTG VKDPAYKNTL YVDELVAPGT VNTMPEATLE
ATAARGEIRG DTITGTYDQA RADLEAIGKL GISYDEVVQL LEDEGVAKFE AAWNDLLAST
EAELKRLAPS EA
//
