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Database: UniProt
Entry: C5LZ11_PERM5
LinkDB: C5LZ11_PERM5
Original site: C5LZ11_PERM5 
ID   C5LZ11_PERM5            Unreviewed;       350 AA.
AC   C5LZ11;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|RuleBase:RU000501};
DE            EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|RuleBase:RU000501};
GN   ORFNames=Pmar_PMAR016097 {ECO:0000313|EMBL:EEQ98020.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EEQ98020.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the rate-limiting step of the non-oxidative phase
CC       in the pentose phosphate pathway. Catalyzes the reversible conversion
CC       of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into
CC       erythrose-4-phosphate and beta-D-fructose 6-phosphate.
CC       {ECO:0000256|RuleBase:RU000501}.
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:0000256|RuleBase:RU000501};
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. {ECO:0000256|ARBA:ARBA00004857,
CC       ECO:0000256|RuleBase:RU000501}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008012}.
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DR   EMBL; GG686838; EEQ98020.1; -; Genomic_DNA.
DR   RefSeq; XP_002765303.1; XM_002765257.1.
DR   AlphaFoldDB; C5LZ11; -.
DR   EnsemblProtists; EEQ98020; EEQ98020; Pmar_PMAR016097.
DR   GeneID; 9037930; -.
DR   InParanoid; C5LZ11; -.
DR   OMA; ICKFAED; -.
DR   OrthoDB; 1972468at2759; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000007800; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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   CDD; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00492; Transaldolase_1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004730; Transaldolase_1.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   NCBIfam; TIGR00874; talAB; 1.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   PANTHER; PTHR10683:SF18; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW   ECO:0000256|RuleBase:RU000501};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800};
KW   Transferase {ECO:0000256|RuleBase:RU000501}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   350 AA;  38815 MW;  AF9AFAA079F40899 CRC64;
     MPSPKNLAGA HPAASSPKKA KTLDASNQLE ALKNMTSVVA DTGDFDKIKQ FRPDDATTNP
     TLLYQAAQMP EYAHVMTKAI KNAKAQNLTG DALVDEVCDQ LAVSFGFEIL QIVDGYVSTE
     CDANLSFDRQ ASLNKARKII SMYESMGISR DRILIKMAST WECIQACKEL EKEGIHCNMT
     LLFSFAQAVG AAQAGATLIS PFVGRILDWY KKSTGKASYP MDEDPGVQSV RKIYNYYKKY
     GYNTIVMGAS FRNTDEIRGL AGCDKLTISP KLLKELQDNT DVSGMKRYLD PERAVADTDK
     LADLTEPEFR WMLNEDACAT EKLAEGLRNF NKDLQKLKEV VRAKLAEAEK
//
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