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Database: UniProt
Entry: C5CGH2
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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-OCT-2014, entry version 34.
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};
GN   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. {ECO:0000255|HAMAP-
CC       Rule:MF_00494}.
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
CC       {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
CC       stage): 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
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00494}.
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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   OrthoDB; EOG6PS600; -.
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:UniProtKB-HAMAP.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-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; Reference proteome;
KW   Schiff base; Transferase.
FT   CHAIN         1    218       Probable transaldolase.
FT                                /FTId=PRO_1000206474.
FT   ACT_SITE     83     83       Schiff-base intermediate with substrate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00494}.
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
//
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