GenomeNet

Database: UniProt
Entry: B9EM17_SALSA
LinkDB: B9EM17_SALSA
Original site: B9EM17_SALSA 
ID   B9EM17_SALSA            Unreviewed;       327 AA.
AC   B9EM17;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00018292, ECO:0000256|RuleBase:RU000501};
DE            EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|RuleBase:RU000501};
GN   Name=TALDO {ECO:0000313|EMBL:ACM08564.1};
GN   Synonyms=taldo {ECO:0000313|RefSeq:NP_001139898.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|EMBL:ACM08564.1};
RN   [1] {ECO:0000313|EMBL:ACM08564.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACM09807.1}, and Head kidney
RC   {ECO:0000313|EMBL:ACM08564.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RA   Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA   Koop B.F.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACM08564.1, ECO:0000313|RefSeq:NP_001139898.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACM09807.1}, and Head kidney
RC   {ECO:0000313|EMBL:ACM08564.1};
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
RN   [3] {ECO:0000313|EMBL:ACM08564.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACM09807.1}, and Head kidney
RC   {ECO:0000313|EMBL:ACM08564.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|RefSeq:NP_001139898.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BT056692; ACM08564.1; -; mRNA.
DR   EMBL; BT057935; ACM09807.1; -; mRNA.
DR   RefSeq; NP_001139898.1; NM_001146426.1.
DR   GeneID; 100286487; -.
DR   KEGG; sasa:100286487; -.
DR   CTD; 37804; -.
DR   OrthoDB; 1972468at2759; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000087266; Unplaced.
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   2: Evidence at transcript level;
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW   ECO:0000256|RuleBase:RU000501};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transferase {ECO:0000256|RuleBase:RU000501}.
SQ   SEQUENCE   327 AA;  36550 MW;  6EADEEC681718C26 CRC64;
     MESALEQLKK HTVVVADTGD FNAIEEYKPQ DATTNPSLIL AAAKMAAYQH LVDQAIKYGI
     AKGGPEEEQV TNTMDKLFVS FGLEILKKIP GRVSTEVDAR LSYDKDEMVA RALRIIALYE
     EAGIKKDRVL IKLSSTWEGI QAGRELEEKH GVHCNMTLLF SFAQAVACAE AKVTLISPFV
     GRIMDWYKEN TAQKSYEAHE DPGVISVTKI YNHYKKYDYT TVVMGASFRN TGEVKALAGC
     DLLTISPSLL GELSKDHSTV TPMLTVQKAK ACDLEKVHLD EKEFRWQHNE DRMAVEKLSD
     GIRKFAADAI KLETMIKEKM LNVKNGQ
//
DBGET integrated database retrieval system