ID   Q1IMT9_KORVE            Unreviewed;       958 AA.
AC   Q1IMT9;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Transaldolase {ECO:0000256|HAMAP-Rule:MF_00493};
DE            EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00493};
GN   Name=tal {ECO:0000256|HAMAP-Rule:MF_00493};
GN   OrderedLocusNames=Acid345_2810 {ECO:0000313|EMBL:ABF41811.1};
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Koribacter.
OX   NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF41811.1, ECO:0000313|Proteomes:UP000002432};
RN   [1] {ECO:0000313|EMBL:ABF41811.1, ECO:0000313|Proteomes:UP000002432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345 {ECO:0000313|EMBL:ABF41811.1,
RC   ECO:0000313|Proteomes:UP000002432};
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000256|ARBA:ARBA00003518,
CC       ECO:0000256|HAMAP-Rule:MF_00493}.
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|ARBA:ARBA00001469, ECO:0000256|HAMAP-
CC         Rule:MF_00493};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC         Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC         EC=5.3.1.9; Evidence={ECO:0000256|RuleBase:RU000612};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000256|RuleBase:RU000612}.
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, ECO:0000256|HAMAP-
CC       Rule:MF_00493}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|RuleBase:RU000612}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008426, ECO:0000256|HAMAP-Rule:MF_00493}.
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; CP000360; ABF41811.1; -; Genomic_DNA.
DR   RefSeq; WP_011523612.1; NC_008009.1.
DR   AlphaFoldDB; Q1IMT9; -.
DR   STRING; 204669.Acid345_2810; -.
DR   EnsemblBacteria; ABF41811; ABF41811; Acid345_2810.
DR   KEGG; aba:Acid345_2810; -.
DR   eggNOG; COG0166; Bacteria.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_013922_0_0_0; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000002432; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR   CDD; cd05798; SIS_TAL_PGI; 1.
DR   CDD; cd00955; Transaldolase_like; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00493; Transaldolase_2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004732; Transaldolase_2.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   NCBIfam; TIGR00876; tal_mycobact; 1.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   PANTHER; PTHR10683:SF31; TRANSALDOLASE; 1.
DR   Pfam; PF00342; PGI; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00493};
KW   Gluconeogenesis {ECO:0000256|RuleBase:RU000612};
KW   Glycolysis {ECO:0000256|RuleBase:RU000612};
KW   Isomerase {ECO:0000256|RuleBase:RU000612, ECO:0000313|EMBL:ABF41811.1};
KW   Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00493};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002432};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00493};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00493}.
FT   ACT_SITE        140
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ   SEQUENCE   958 AA;  104177 MW;  A17A238812913F38 CRC64;
     MSNPLIELHS FGQSVWLDQI ERALFKTGKL AKLIKEDGLR GMTSNPTIFE KAITGSSDYQ
     EQIDRAARDG KTGNEIYEEV VIDDIAHAAD LFRPLYDSTN GEDGFVSLEV SPLLAKNTDG
     TIREAKTLFS RLNRPNVMIK VPATEEGLPA IEELIASGLN INVTLIFSVH RYEEVAEAYI
     RGLERRAQAG QPIDRIGSVA SFFVSRIDSA VDKQLEALEK EATDPAKKQE IHALRGKAAI
     ANAKLAYASF KRIFESPRFE ALKRKGARVQ RPLWASTSTK DPSYPDVLYV TELIGPHTVN
     TLPPATVDAW RDHGVAGAHL EKDMDKAPDV FAKLKALGID FNKVTDKLTT DGVRSFSASF
     VDLMRAIEQR REMSLPGIKE RHVSALGKYE GDVQAALQEL GSKNVIQRFW NKEAAVWSAD
     AGDQKIINNA LGWLTVTDLM QGKVKELKAF AAEVQAAGFK HAVVLGMGGS SLCPEVLRQT
     FGKQLDYPEL LVLDSTVPAA VLAIDKQIDP AKTLFIVASK SGSTTEPQMF YRYYFEKTKQ
     VLGDKAGQNF VAITDPNTQL ESEAKRDGFR KVFTNMADIG GRYSALSYFG MVPFTVMGGD
     VDSLLRRAKA AMDACAAGVE PANNAGAKIG AILGALARKG RDKVTFVTPP PISSLGLWIE
     QLIAESTGKH GKGIVPISGE SLGDPKVYGD DRVFVYIGVS GTNGANYEAQ LQALEQAGHP
     VLHHVLNSPI DLGEEFFLWE FATPIAGELI GINPFDQPNV QESKDNTKRI LKEYTDTGKI
     TQLPEVAEGD GLTVLTDENN RKALNGVSTP DSAITAHLGR VQKGDYFAIT QYIEETPEIE
     SLVQQIRTAV RDKACVATTT GYGPRFLHST GQLHKGGPDS GVFLQLISND AQDVPLPGEK
     FTFGVLKDAQ ALGDFESLSS RGRRAIRVNL GNNIVGGLKK ILAAVQQFEG ATAGAARK
//