ID E1TC71_BURSG Unreviewed; 317 AA.
AC E1TC71;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 29-MAY-2013, entry version 22.
DE RecName: Full=Transaldolase;
DE EC=2.2.1.2;
GN Name=tal; OrderedLocusNames=BC1003_1011;
OS Burkholderia sp. (strain CCGE1003).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=640512;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCGE1003;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA Ovchinnikova G., Martinez-Romero E., Rogel M.A., Auchtung J.,
RA Tiedje J.M., Woyke T.;
RT "Complete sequence of chromosome 1 of Burkholderia sp. CCGE1003.";
RL Submitted (SEP-2010) 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 -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
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DR EMBL; CP002217; ADN56991.1; -; Genomic_DNA.
DR RefSeq; YP_003906282.1; NC_014539.1.
DR EnsemblBacteria; ADN56991; ADN56991; BC1003_1011.
DR GeneID; 9765880; -.
DR KEGG; bgf:BC1003_1011; -.
DR PATRIC; 42208079; VBIBurSp98639_1057.
DR HOGENOM; HOG000281234; -.
DR KO; K00616; -.
DR OMA; EGINCNM; -.
DR BioCyc; BSP640512:GBXV-1019-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_00492; Transaldolase_1; 1; -.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; Transaldolase.
DR InterPro; IPR004730; Transaldolase_1.
DR InterPro; IPR018225; Transaldolase_AS.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; Transaldolase; 1.
DR TIGRFAMs; TIGR00874; talAB; 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 ACT_SITE 126 126 By similarity.
SQ SEQUENCE 317 AA; 35044 MW; 4153C9882E7FB869 CRC64;
MTTALDQLKQ YTTVVADTGD FQQLAQYKPQ DATTNPSLIL KAVQKDDYRP LLEKTVKDHA
SKPMGAIIDQ LLIAFGTEIL KIIPGRVSTE VDARLSFDVQ GSIAKGRELI ALYKEHGIDR
ERVLIKLAST WEGVRAAEVL QKEGINCNMT LLFSLAQAAA CAEAGAKLIS PFVGRIYDWY
KKNAGSAWDE AKDGGANDPG VQSVRRIYAY YKKFGYKTEV MGASFRTTGQ ILELAGCDLL
TISPDLLQKL HESTEKVERK LSPESSHDAN MERVPVDEPS FRFLVNDEAM ATEKLAEGIR
AFAADAVKLE KLIEALR
//
