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Database: UniProt
Entry: A0A026WTU3_OOCBI
LinkDB: A0A026WTU3_OOCBI
Original site: A0A026WTU3_OOCBI 
ID   A0A026WTU3_OOCBI        Unreviewed;       332 AA.
AC   A0A026WTU3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
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=DMN91_008469 {ECO:0000313|EMBL:RLU19910.1}, X777_15717
GN   {ECO:0000313|EMBL:EZA59076.1};
OS   Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Dorylinae; Ooceraea.
OX   NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA59076.1, ECO:0000313|Proteomes:UP000053097};
RN   [1] {ECO:0000313|EMBL:EZA59076.1, ECO:0000313|Proteomes:UP000053097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA   Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA   Zhang G., Kronauer D.J.;
RT   "The genome of the clonal raider ant Cerapachys biroi.";
RL   Curr. Biol. 24:451-458(2014).
RN   [2] {ECO:0000313|EMBL:RLU19910.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU19910.1};
RX   PubMed=30249741; DOI=10.1101/gr.237123.118;
RA   McKenzie S.K., Kronauer D.J.C.;
RT   "The genomic architecture and molecular evolution of ant odorant
RT   receptors.";
RL   Genome Res. 28:1757-1765(2018).
RN   [3] {ECO:0000313|EMBL:RLU19910.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Clonal line C1 {ECO:0000313|EMBL:RLU19910.1};
RA   Mckenzie S.K., Kronauer D.J.C.;
RL   Submitted (JUL-2018) 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; KK107109; EZA59076.1; -; Genomic_DNA.
DR   EMBL; QOIP01000008; RLU19910.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A026WTU3; -.
DR   STRING; 2015173.A0A026WTU3; -.
DR   EnsemblMetazoa; XM_011332328.3; XP_011330630.1; LOC105275476.
DR   OMA; THAEFLW; -.
DR   OrthoDB; 1972468at2759; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000053097; Unassembled WGS sequence.
DR   Proteomes; UP000279307; Chromosome 8.
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:UP000053097};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000501}.
SQ   SEQUENCE   332 AA;  36768 MW;  175E304B240B84A4 CRC64;
     MTEPQSKKTK MMSSLSQLKD LTTVVADTGD FQAMEQFKPT DATTNPSLIL AAANQKKYAH
     LMEKAAECGK KSGSTLAEQV EAALDITCVL FGKEILNIIP GRVSTEVDAR LSFNKEASIE
     KAKRLVALYE GLGISKERVL IKLASTWEGI QAAKELEEKY GIHCNLTLLF SFAQAVACAE
     AGVTLISPFV GRILDWYVAN TDKKSYEGKE DPGVISVTKI YNYYKKFGYK TVVMGASFRN
     VGEIKELAGC DLLTISPKLL EELEKSNEAV GKVLSMESAK KCDLQKISLD EAEFRWLMNE
     DQMATDKLCE GIRKFAVDVR KLEKLMQDKI QG
//
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