ID TAL_CLOK5 Reviewed; 215 AA.
AC A5N6V9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 01-MAY-2013, entry version 48.
DE RecName: Full=Probable transaldolase;
DE EC=2.2.1.2;
GN Name=tal; OrderedLocusNames=CKL_0998;
OS Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=431943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA Hagemeier C., Thauer R.K., Gottschalk G.;
RT "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT metabolic features.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
CC -!- FUNCTION: Transaldolase is important for the balance of
CC metabolites in the pentose-phosphate pathway (By similarity).
CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
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
CC stage): step 2/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3B
CC subfamily.
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DR EMBL; CP000673; EDK33040.1; -; Genomic_DNA.
DR RefSeq; YP_001394388.1; NC_009706.1.
DR ProteinModelPortal; A5N6V9; -.
DR SMR; A5N6V9; 1-210.
DR STRING; 431943.CKL_0998; -.
DR EnsemblBacteria; EDK33040; EDK33040; CKL_0998.
DR GeneID; 5390942; -.
DR KEGG; ckl:CKL_0998; -.
DR PATRIC; 19463439; VBICloKlu111549_1054.
DR eggNOG; COG0176; -.
DR HOGENOM; HOG000226073; -.
DR KO; K00616; -.
DR OMA; DNYGFET; -.
DR ProtClustDB; CLSK2474777; -.
DR BioCyc; CKLU431943:GJF1-998-MONOMER; -.
DR UniPathway; UPA00115; UER00414.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; IEA:HAMAP.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:HAMAP.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00494; Transaldolase_3b; 1; -.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; Transaldolase.
DR InterPro; IPR004731; Transaldolase_3A/3B.
DR InterPro; IPR022999; Transaldolase_3B.
DR InterPro; IPR018225; Transaldolase_AS.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; Transaldolase; 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 Complete proteome; Cytoplasm; Pentose shunt; Transferase.
FT CHAIN 1 215 Probable transaldolase.
FT /FTId=PRO_1000081408.
FT ACT_SITE 83 83 By similarity.
SQ SEQUENCE 215 AA; 23644 MW; 1BA8FC7F1442A001 CRC64;
MKLFIDTANV DEIRKANDMG IICGVTTNPS LIAKEGRNFK EVVKEITDIV DGPISAEVIS
LEWKEMVKEA RELVKIHKNI VIKIPMTQEG LKAVKVLSQE EIKTNVTLIF SAAQALLAAK
AGASYVSPFL GRLDDVGMDG IKLIEEIVTI FKVQNIVTEI IAASIRGPIH VVKCAALGSH
IATVPYKVLV QMCKHPLTDI GIERFLKDWE SVPDK
//
