(data stored in SCRATCH zone)

SWISSPROT: C8VVF5_DESAS

ID   C8VVF5_DESAS            Unreviewed;       219 AA.
AC   C8VVF5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Probable transaldolase {ECO:0000256|HAMAP-Rule:MF_00494};
DE            EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00494};
GN   Name=tal {ECO:0000256|HAMAP-Rule:MF_00494};
GN   OrderedLocusNames=Dtox_0058 {ECO:0000313|EMBL:ACV61021.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61021.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61021.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Transaldolase is important for the balance of
CC       metabolites in the pentose-phosphate pathway. {ECO:0000256|HAMAP-
CC       Rule:MF_00494, ECO:0000256|SAAS:SAAS00709741}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-
CC         phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-
CC         phosphate; Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897,
CC         ChEBI:CHEBI:57483, ChEBI:CHEBI:57634, ChEBI:CHEBI:59776;
CC         EC=2.2.1.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00494,
CC         ECO:0000256|SAAS:SAAS01126537};
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_00494,
CC       ECO:0000256|SAAS:SAAS00118684}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00494,
CC       ECO:0000256|SAAS:SAAS00118691}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 3B
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00494,
CC       ECO:0000256|SAAS:SAAS00709782}.
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DR   EMBL; CP001720; ACV61021.1; -; Genomic_DNA.
DR   STRING; 485916.Dtox_0058; -.
DR   EnsemblBacteria; ACV61021; ACV61021; Dtox_0058.
DR   KEGG; dae:Dtox_0058; -.
DR   eggNOG; ENOG4105CW3; Bacteria.
DR   eggNOG; COG0176; LUCA.
DR   HOGENOM; HOG000226073; -.
DR   KO; K00616; -.
DR   OMA; VRHPMHV; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR   GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR   CDD; cd00956; Transaldolase_FSA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00494; Transaldolase_3b; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR022999; Transaldolase_3B.
DR   InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   InterPro; IPR033919; TSA/FSA_arc/bac.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   Pfam; PF00923; TAL_FSA; 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;
DR   PRODOM; C8VVF5.
DR   SWISS-2DPAGE; C8VVF5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00494,
KW   ECO:0000256|SAAS:SAAS00476608};
KW   Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00494,
KW   ECO:0000256|SAAS:SAAS00118654};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00494,
KW   ECO:0000256|SAAS:SAAS00118695};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00494,
KW   ECO:0000256|SAAS:SAAS00118651, ECO:0000313|EMBL:ACV61021.1}.
FT   ACT_SITE     87     87       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00494}.
SQ   SEQUENCE   219 AA;  23702 MW;  B121DEC91D2AFCE9 CRC64;
     MVLEIKLFLD TANVEEIRDA YSLGVISGVT TNPSLIALEG RDFVQVVREI ASIVDGPISA
     EAVSLEAAPM IEEARQLSSI HPNIVVKIPM TAEGLKAVKE LSSQGIKTNV TLIFSANQAL
     LAALAGASYV SPFVGRLDDI GYNGMQLIEE IMAIFNQYGL IAEVIAASVR HPMHVIDAAK
     SGADIATIPY KVLYQMIKHP LTDSGIERFL KDWEKVPVK
//

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