ID   TALB_PASMU              Reviewed;         316 AA.
AC   Q9CKH9;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Transaldolase B;
DE            EC=2.2.1.2;
GN   Name=talB; Synonyms=tal_2; OrderedLocusNames=PM1639;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000250}.
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   -!- 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.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004439; AAK03723.1; -; Genomic_DNA.
DR   RefSeq; WP_010907268.1; NC_002663.1.
DR   AlphaFoldDB; Q9CKH9; -.
DR   SMR; Q9CKH9; -.
DR   STRING; 747.DR93_723; -.
DR   PRIDE; Q9CKH9; -.
DR   EnsemblBacteria; AAK03723; AAK03723; PM1639.
DR   KEGG; pmu:PM1639; -.
DR   PATRIC; fig|272843.6.peg.1658; -.
DR   HOGENOM; CLU_047470_0_1_6; -.
DR   OMA; ICKFAED; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:transaldolase activity; ISS:UniProtKB.
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; -; 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   PANTHER; PTHR10683; PTHR10683; 1.
DR   PANTHER; PTHR10683:SF18; PTHR10683:SF18; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   TIGRFAMs; TIGR00874; talAB; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT   CHAIN           1..316
FT                   /note="Transaldolase B"
FT                   /id="PRO_0000173602"
FT   ACT_SITE        131
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   316 AA;  35254 MW;  24563CC37F37C853 CRC64;
     MTQLDSLRSM TVVVADTGDI EAIKQYQPQD ATTNPSLILS ASALPQYAPL IDDAIAYAKT
     KSDCPRQQLV DAEDKLAVNI GLEILKIIPG RISTEVDARL SYDTQATIEK ARKLIKLYNE
     AGIENHRILI KIASTWQGIR AAEVLEKEGI NCNLTLLFSE AQARACAEAG VYLISPFVGR
     ILDWHKANTG RQDYPAAEDP GVISVTQIYN YYKQHNYKTV VMGASFRNVD EIIELAGCDR
     LTISPTLLSH LQAREGELVR KLAFSGELKD RPQPLTESEF YWQHNSDPMA VAKLAEGICK
     FAEDQEKLEK MLLERL