TAL_CHLFF
ID TAL_CHLFF Reviewed; 327 AA.
AC Q255E4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Transaldolase {ECO:0000255|HAMAP-Rule:MF_00492};
DE EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00492};
GN Name=tal {ECO:0000255|HAMAP-Rule:MF_00492}; OrderedLocusNames=CF0322;
OS Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=264202;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fe/C-56;
RX PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA Hattori M., Kuhara S., Shirai M.;
RT "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL DNA Res. 13:15-23(2006).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000255|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:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00492}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00492}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00492}.
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DR EMBL; AP006861; BAE81094.1; -; Genomic_DNA.
DR RefSeq; WP_011457874.1; NC_007899.1.
DR AlphaFoldDB; Q255E4; -.
DR SMR; Q255E4; -.
DR STRING; 264202.CF0322; -.
DR KEGG; cfe:CF0322; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_047470_0_1_0; -.
DR OMA; KFGYKTL; -.
DR OrthoDB; 784333at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000001260; 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; Schiff base; Transferase.
FT CHAIN 1..327
FT /note="Transaldolase"
FT /id="PRO_1000014497"
FT ACT_SITE 132
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00492"
SQ SEQUENCE 327 AA; 35972 MW; 9D2DCD75E5354B28 CRC64;
MSSQFEQLKL LSVLVCDTGD PELVKSSGSQ DATTNPSLIL KVAQEPKYQE MLTEAIAWGI
RQNGDDVQTL TFVLDKIQVN FGLEILKCIP GRVSLEIDAR LSFNTEAMVQ RAIFLSELFV
ASGGDKKRLL VKIPGTWEGI QAVEILEKQG ISCNVTLIFN LIQAIAAAKA KATLISPFVG
RIYDWWIAAY GDEGYSIDTD PGVASVSNIY TYYKKFDIPT QIMAASFRSK EQVLALAGCD
LLTVSPKLLD ELKKDQSSVT KKLDVAEAKK LDVQPVELTE SVFRFLMNED AMATEKLAEG
IRIFSGDTQI LEAAVTEFIK QIAAQDA
