(data stored in SCRATCH zone)

SWISSPROT: C1AS73_RHOOB

ID   C1AS73_RHOOB            Unreviewed;       381 AA.
AC   C1AS73;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=Transaldolase {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000256|SAAS:SAAS00118670};
DE            EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000256|SAAS:SAAS00118670};
GN   Name=tal {ECO:0000256|HAMAP-Rule:MF_00493,
GN   ECO:0000313|EMBL:BAH48322.1};
GN   OrderedLocusNames=ROP_00750 {ECO:0000313|EMBL:BAH48322.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48322.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48322.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48322.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transaldolase is important for the balance of
CC       metabolites in the pentose-phosphate pathway. {ECO:0000256|HAMAP-
CC       Rule:MF_00493}.
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000256|SAAS:SAAS00118662}.
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:0000256|HAMAP-Rule:MF_00493,
CC       ECO:0000256|SAAS:SAAS00118684}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493,
CC       ECO:0000256|SAAS:SAAS00399167}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00493}.
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DR   EMBL; AP011115; BAH48322.1; -; Genomic_DNA.
DR   STRING; 632772.ROP_00750; -.
DR   EnsemblBacteria; BAH48322; BAH48322; ROP_00750.
DR   KEGG; rop:ROP_00750; -.
DR   PATRIC; fig|632772.20.peg.96; -.
DR   eggNOG; ENOG4107QQX; Bacteria.
DR   eggNOG; COG0176; LUCA.
DR   HOGENOM; HOG000226074; -.
DR   KO; K00616; -.
DR   OMA; TAFEDHG; -.
DR   OrthoDB; POG091H05PS; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000002212; Chromosome.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP.
DR   CDD; cd00955; Transaldolase_like; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00493; Transaldolase_2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004732; Transaldolase_2.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   PANTHER; PTHR10683:SF21; PTHR10683:SF21; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1.
DR   TIGRFAMs; TIGR00876; tal_mycobact; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1AS73.
DR   SWISS-2DPAGE; C1AS73.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493,
KW   ECO:0000256|SAAS:SAAS00118680};
KW   Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00493,
KW   ECO:0000256|SAAS:SAAS00118654};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00493,
KW   ECO:0000256|SAAS:SAAS00118695};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00493,
KW   ECO:0000256|SAAS:SAAS00118651, ECO:0000313|EMBL:BAH48322.1}.
FT   ACT_SITE    152    152       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00493}.
SQ   SEQUENCE   381 AA;  40971 MW;  05604838FA5B71F2 CRC64;
     MMTRFPPAPV GATVSRLHRL YREQGQSPWL DNLTRPYLRD GTLAEFVAAG IRGVTANPTI
     FARAIAGSDA YDAQFAALIA QGRAVEDAYW ELAAADVVDA AAVLRPVYDT SGGTDGFVSI
     EVAPELARDT DATIAAAGRL HERIARPNVF VKIPATAEGI PAIADMIGKG VSINITLIFS
     LARYEQVIEA YLQGLEARAA RGADLAAVRS VASFFVSRVD TEVDKRLEHS GDPEAPALRG
     RAAIAQARLA YRIFQDRFTG TRWETLAARG ARVQRPLWAS TSTKNPDYPD TRYVDSLIGP
     DTVNTLPEAT ITAFEDHGTL TRSIDTVPAG AAAVLDELAA AGIDMDDVGR TLEDQGVAAF
     HQSFADLLTE LRAKAHQLAQ R
//

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