ID TAL_KOSOT Reviewed; 218 AA.
AC C5CGH2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 01-MAY-2013, entry version 28.
DE RecName: Full=Probable transaldolase;
DE EC=2.2.1.2;
GN Name=tal; OrderedLocusNames=Kole_1872;
OS Kosmotoga olearia (strain TBF 19.5.1).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Kosmotoga.
OX NCBI_TaxID=521045;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBF 19.5.1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinnikova G., Noll K.;
RT "Complete sequence of Thermotogales bacterium TBF 19.5.1.";
RL Submitted (JUN-2009) 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; CP001634; ACR80553.1; -; Genomic_DNA.
DR RefSeq; YP_002941557.1; NC_012785.1.
DR STRING; 521045.Kole_1872; -.
DR EnsemblBacteria; ACR80553; ACR80553; Kole_1872.
DR GeneID; 7967794; -.
DR KEGG; kol:Kole_1872; -.
DR PATRIC; 22189106; VBIKosOle109242_1963.
DR eggNOG; COG0176; -.
DR HOGENOM; HOG000226073; -.
DR KO; K00616; -.
DR ProtClustDB; PRK01362; -.
DR BioCyc; KOLE521045:GHRV-1923-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 1 218 Probable transaldolase.
FT /FTId=PRO_1000206474.
FT ACT_SITE 83 83 By similarity.
SQ SEQUENCE 218 AA; 23980 MW; 0D0BBF0DA104BEDA CRC64;
MRIFLDTANI EEIKKAVAWG VIDGVTTNPT LIAREKAPFT ERIKEICETV KGPVSAEVVA
LDYEGMVKEA RDLAMLDEHV VIKIPMTPEG IKAVKTLSSE GIKTNVTLVF SAVQALLAAK
AGATYVSPFI GRVDDISSDG LRLVEDIVAI FSNYGFQTNV LAASIRHPMH VLELATIGVD
IVTMPFNVLE KLFHHPLTDK GIERFLNDWE EYRKGTGL
//
