TAL_CHLPD
ID TAL_CHLPD Reviewed; 226 AA.
AC A1BJV5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=Cpha266_2698;
OS Chlorobium phaeobacteroides (strain DSM 266).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266;
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., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-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}.
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DR EMBL; CP000492; ABL66682.1; -; Genomic_DNA.
DR RefSeq; WP_015961209.1; NC_008639.1.
DR AlphaFoldDB; A1BJV5; -.
DR SMR; A1BJV5; -.
DR STRING; 290317.Cpha266_2698; -.
DR EnsemblBacteria; ABL66682; ABL66682; Cpha266_2698.
DR KEGG; cph:Cpha266_2698; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_079764_0_0_10; -.
DR OMA; VRHPMHV; -.
DR OrthoDB; 784333at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000008701; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Pentose shunt; Reference proteome; Schiff base; Transferase.
FT CHAIN 1..226
FT /note="Probable transaldolase"
FT /id="PRO_1000126290"
FT ACT_SITE 91
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00494"
SQ SEQUENCE 226 AA; 24497 MW; C614187E39CE3E15 CRC64;
MKFFIDTASL EEIQAAKDLG MLDGVTTNPS LIARIVGDAS SFSYQDFREH IRRIAEIADG
PVSAEVTTTD AEEMIHEGEA LAAIHENVVV KCPLTIDGLK AIRHLSEKGI RTNATLVFSP
NQALLAAKAG ASYVSPFVGR LDDISTEGMA LVEQIITIYD NYGYLTEVIV ASIRHPRHVV
ESAMMGADIA TIPFSVIRQL ANHPLTDAGL KKFMEDAAIL KKESDA
