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Database: UniProt/SWISS-PROT
Entry: TAL_CLOK1
LinkDB: TAL_CLOK1
Original site: TAL_CLOK1 
ID   TAL_CLOK1               Reviewed;         215 AA.
AC   B9E0C8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   01-MAY-2013, entry version 31.
DE   RecName: Full=Probable transaldolase;
DE            EC=2.2.1.2;
GN   Name=tal; OrderedLocusNames=CKR_0902;
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016;
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Vertes A.A., Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative
RT   genomics of Clostridia species.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; AP009049; BAH05953.1; -; Genomic_DNA.
DR   RefSeq; YP_002471367.1; NC_011837.1.
DR   ProteinModelPortal; B9E0C8; -.
DR   SMR; B9E0C8; 1-210.
DR   STRING; 583346.CKR_0902; -.
DR   EnsemblBacteria; BAH05953; BAH05953; CKR_0902.
DR   GeneID; 7275742; -.
DR   KEGG; ckr:CKR_0902; -.
DR   PATRIC; 19471612; VBICloKlu118830_1053.
DR   eggNOG; COG0176; -.
DR   HOGENOM; HOG000226073; -.
DR   KO; K00616; -.
DR   ProtClustDB; CLSK2474777; -.
DR   BioCyc; CKLU583346:GJNQ-947-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_1000198471.
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
//
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