ID A0A0E3U492_9ENTR Unreviewed; 317 AA.
AC A0A0E3U492;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, 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=talA {ECO:0000313|EMBL:AKC60662.1};
GN Synonyms=tal {ECO:0000256|HAMAP-Rule:MF_00492};
GN ORFNames=BOBLI757_519 {ECO:0000313|EMBL:AKC60662.1};
OS Blochmannia endosymbiont of Camponotus (Colobopsis) obliquus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=1505597 {ECO:0000313|EMBL:AKC60662.1, ECO:0000313|Proteomes:UP000033104};
RN [1] {ECO:0000313|EMBL:AKC60662.1, ECO:0000313|Proteomes:UP000033104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=757 {ECO:0000313|EMBL:AKC60662.1,
RC ECO:0000313|Proteomes:UP000033104};
RX PubMed=25861561;
RA Williams L.E., Wernegreen J.J.;
RT "Genome evolution in an ancient bacteria-ant symbiosis: parallel gene loss
RT among Blochmannia spanning the origin of the ant tribe Camponotini.";
RL PeerJ 3:E881-E881(2015).
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}.
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};
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}.
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}.
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DR EMBL; CP010049; AKC60662.1; -; Genomic_DNA.
DR RefSeq; WP_046305186.1; NZ_CP010049.1.
DR AlphaFoldDB; A0A0E3U492; -.
DR STRING; 1505597.BOBLI757_519; -.
DR KEGG; ben:BOBLI757_519; -.
DR PATRIC; fig|1505597.4.peg.510; -.
DR HOGENOM; CLU_047470_0_1_6; -.
DR OrthoDB; 9809101at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000033104; 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.
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:UP000033104};
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; 36501 MW; DC4047AE5DA39F00 CRC64;
MNQLDSLKKI SNIVVDSGNI EYIKQYQLQD VTTNPSLILQ AINNKSYQSL FKNALIYAQK
QGGNKDLQIT NAIDKLTVNI GICILQYISG SISIEIDPRF SFNHKMSIIQ AKKIINLYKE
QNIDKSRILI KLAATWEGIK AAAQLEKENI HCNLTLVFSF AQARACAEAK VFLISPFVGR
IYDWYHQKKP LIPYFVDEDP GIKSVKKIYR YYKKHCYKTI IMSASFRKIE QILALAGCDC
LTISPNFLNK LLNTHQNVEQ QLFPMNNKTF KQPIPISEPD FHWEHNKNAM AVEKLSEGIR
LFALDQQKLK QILKREL
//
