ID A0A259F0S1_9PROT Unreviewed; 988 AA.
AC A0A259F0S1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ORFNames=B7X82_14395 {ECO:0000313|EMBL:OZA32115.1};
OS Hydrogenophilales bacterium 17-64-65.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970528 {ECO:0000313|EMBL:OZA32115.1, ECO:0000313|Proteomes:UP000216509};
RN [1] {ECO:0000313|EMBL:OZA32115.1, ECO:0000313|Proteomes:UP000216509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17-64-65 {ECO:0000313|EMBL:OZA32115.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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|HAMAP-Rule:MF_00493}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008426, ECO:0000256|HAMAP-Rule:MF_00493}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZA32115.1}.
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; NCIQ01000025; OZA32115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259F0S1; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000216509; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR CDD; cd00955; Transaldolase_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00493; Transaldolase_2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR004732; Transaldolase_2.
DR InterPro; IPR018225; Transaldolase_AS.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00876; tal_mycobact; 1.
DR PANTHER; PTHR43195:SF1; FI06132P-RELATED; 1.
DR PANTHER; PTHR43195; TRANSKETOLASE; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493};
KW Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00493};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00493}; Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00493}.
FT DOMAIN 676..840
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT ACT_SITE 141
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 988 AA; 106730 MW; AB81D0BEEA0A2ECA CRC64;
MEADSLRQLV AHGQSYWLDN LTRHKIASGE LERRVREHGL RGVTSNPAIF HQAISSSRDY
DDEIRDAFAA GRTAAEVHEA VMVSDVRDAC DVLRPVYDES GGVDGYVSLE VSPHLAHDTQ
ASIEEARRLH AAVNRPNLFI KIPGTLAGLP AIEQCLFEGI NINITLLFSV PRYEAVAEAW
LRALERRLEA GKPVAGIASV ASFFLSRIDI LADSLLAHRF GTAHEAQARS LLGKVAVANA
KLAYQRFKHM VASERWQKLA AQGAQVQRLL WASTSTKNPD YRDVMYVEPL IGPHTVNTLP
DKTITAFADR GQVATTLEDS VDDARQTMAA LDALGIDFAQ LATQLENEGV QKFIEPYDAL
TQLIEDKGRL LQRREGAEML PEATRLLRRQ VLRMTTEAGS GHPTSCLSCA EIVAALFFHE
MRWDPADPQA RNVDRFVLSK GHAAPILWAA LAAAGAIEED PMSLRRIDST LEGHPTPNNP
WIKVATGSLG QGLSAANGMA LANRLDGIDA RVFCLLGDGE CSEGSVWEAA QFASLNKLAN
LVAIVDVNGL GQSGPAPYGH DTAVLARRFE SFGWRAIEIH GHDMDAVLDA LERAREGGPT
AILACTVKGR GVSFLEGAGG WHGKPVERER LQQALDEVGD VQSQPRVEPR RSGAFETAIA
GTPGSIDVNY ASGAEVATRE AYGHALAKLG ALNPDIVALD GDVKNSTRSE FFAEAFPERF
FECWIAEQNM VGAALGLAAC GKIPFVSTFA CFLSRAYDFI RMAGHSRPQH LVFCGSHAGV
SIGEDGPSQM GLEDLAMFRA LAHSTVLYPC DAVSAERLTE QAARSEGIVY LRTTRGKTPV
IYGNDERFPV GGSKVLRASG DDQCTVVAAG VTVHEALAAH DSLKQQGIAL RVIDAYSVKP
LDVATLIQAA GETRGLVVVE DHWADGGLGD AVARAHDWLV PLRFLAVGSE PRSGTPHALL
ERHGISRHVI VQQVLALVNH PDAGRLRA
//
