TAL_PELPD
ID TAL_PELPD Reviewed; 214 AA.
AC A1AKQ8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Probable transaldolase {ECO:0000255|HAMAP-Rule:MF_00494};
DE EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00494};
GN Name=tal {ECO:0000255|HAMAP-Rule:MF_00494}; OrderedLocusNames=Ppro_0294;
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00494}.
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:0000255|HAMAP-Rule:MF_00494};
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:0000255|HAMAP-Rule:MF_00494}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00494}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3B subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00494}.
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; CP000482; ABK97928.1; -; Genomic_DNA.
DR RefSeq; WP_011734242.1; NC_008609.1.
DR AlphaFoldDB; A1AKQ8; -.
DR SMR; A1AKQ8; -.
DR STRING; 338966.Ppro_0294; -.
DR EnsemblBacteria; ABK97928; ABK97928; Ppro_0294.
DR KEGG; ppd:Ppro_0294; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_079764_0_0_7; -.
DR OMA; VRHPMHV; -.
DR OrthoDB; 784333at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000006732; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
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; cd00956; Transaldolase_FSA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00494; Transaldolase_3b; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR022999; Transaldolase_3B.
DR InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR InterPro; IPR018225; Transaldolase_AS.
DR InterPro; IPR033919; TSA/FSA_arc/bac.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR TIGRFAMs; TIGR00875; fsa_talC_mipB; 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..214
FT /note="Probable transaldolase"
FT /id="PRO_1000060475"
FT ACT_SITE 83
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00494"
SQ SEQUENCE 214 AA; 23116 MW; C31597D83365BCF6 CRC64;
MKFFIDTADV REIREAHELG LVDGVTTNPS LIAKSGRKFQ EVIQEITSIV DGPISAEVIA
LDAPGMIREA EELVKIHANI VVKVPMTPEG LKATKALSAK GIKTNVTLIF SSLQALLAAK
AGATYVSPFV GRLDDISQDG MGIIEEIRTM FDNYGYTSEI IVASVRNPIH VLNSALIGAD
IATIPYSVML QLSKHPLTDA GIKKFLADWE SVPK
