ID   TALDO_CARMA             Reviewed;          75 AA.
AC   P80427;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2;
DE   Flags: Fragments;
OS   Carcinus maenas (Common shore crab) (Green crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Portunoidea; Carcinidae; Carcinus.
OX   NCBI_TaxID=6759;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Lachaise F., Somme G., Carpentier G., Granjeon E., Webster S.,
RA   Baghdassarian D.;
RT   "A transaldolase. An enzyme implicated in crab steroidogenesis.";
RL   Endocrine 5:23-32(1996).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. May play a role in the conversion of
CC       sterols into ecdysteroids via NADPH.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         beta-D-fructose 6-phosphate + D-erythrose 4-phosphate;
CC         Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10019};
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 stage):
CC       step 2/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in Y-organs.
CC   -!- PTM: Phosphorylated.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 6.8,
CC       its MW is: 36.2 kDa.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P80427; -.
DR   SMR; P80427; -.
DR   UniPathway; UPA00115; UER00414.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Pentose shunt; Phosphoprotein;
KW   Schiff base; Transferase.
FT   CHAIN           <1..>75
FT                   /note="Transaldolase"
FT                   /id="PRO_0000173568"
FT   NON_CONS        17..18
FT                   /evidence="ECO:0000305"
FT   NON_CONS        27..28
FT                   /evidence="ECO:0000305"
FT   NON_CONS        34..35
FT                   /evidence="ECO:0000305"
FT   NON_CONS        48..49
FT                   /evidence="ECO:0000305"
FT   NON_CONS        64..65
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         75
SQ   SEQUENCE   75 AA;  8818 MW;  BD844CEF4EB50559 CRC64;
     KYKPTDATTN PSLILQAKFL EELQNSKKIY NYYKKESVVE HLSESSAKKL EMTEANFRWE
     MNEDKFAVDA VKLEK