ID   E6VZD4_PSEA9            Unreviewed;       215 AA.
AC   E6VZD4;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Probable transaldolase {ECO:0000256|HAMAP-Rule:MF_00494};
DE            EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00494};
GN   Name=tal {ECO:0000256|HAMAP-Rule:MF_00494};
GN   OrderedLocusNames=Daes_3013 {ECO:0000313|EMBL:ADU64006.1};
OS   Pseudodesulfovibrio aespoeensis (strain ATCC 700646 / DSM 10631 / Aspo-2)
OS   (Desulfovibrio aespoeensis).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae.
OX   NCBI_TaxID=643562 {ECO:0000313|EMBL:ADU64006.1, ECO:0000313|Proteomes:UP000002191};
RN   [1] {ECO:0000313|Proteomes:UP000002191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC   {ECO:0000313|Proteomes:UP000002191};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pedersen K., Jagevall S.,
RA   Hazen T., Woyke T.;
RT   "Complete sequence of Desulfovibrio aespoeensis Aspo-2.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU64006.1, ECO:0000313|Proteomes:UP000002191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700646 / DSM 10631 / Aspo-2
RC   {ECO:0000313|Proteomes:UP000002191};
RX   PubMed=24874683;
RA   Pedersen K., Bengtsson A., Edlund J., Rabe L., Hazen T., Chakraborty R.,
RA   Goodwin L., Shapiro N.;
RT   "Complete Genome Sequence of the Subsurface, Mesophilic Sulfate-Reducing
RT   Bacterium Desulfovibrio aespoeensis Aspo-2.";
RL   Genome Announc. 2:e00509-14(2014).
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000256|HAMAP-Rule:MF_00494}.
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_00494};
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_00494}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00494}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 3B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005740, ECO:0000256|HAMAP-Rule:MF_00494}.
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DR   EMBL; CP002431; ADU64006.1; -; Genomic_DNA.
DR   RefSeq; WP_013515907.1; NC_014844.1.
DR   AlphaFoldDB; E6VZD4; -.
DR   STRING; 643562.Daes_3013; -.
DR   KEGG; das:Daes_3013; -.
DR   eggNOG; COG0176; Bacteria.
DR   HOGENOM; CLU_079764_0_0_7; -.
DR   OrthoDB; 9807051at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000002191; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
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; cd00956; Transaldolase_FSA; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00494; Transaldolase_3b; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR022999; Transaldolase_3B.
DR   InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   InterPro; IPR033919; TSA/FSA_arc/bac.
DR   NCBIfam; TIGR00875; fsa_talC_mipB; 1.
DR   PANTHER; PTHR10683:SF40; FRUCTOSE-6-PHOSPHATE ALDOLASE 1-RELATED; 1.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00494};
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126, ECO:0000256|HAMAP-
KW   Rule:MF_00494};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW   Rule:MF_00494};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00494}.
FT   ACT_SITE        83
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
SQ   SEQUENCE   215 AA;  23369 MW;  1B12F0EAF5B2B149 CRC64;
     MQFFLDTANV DQIREVQGLG LLDGVTTNPT LLARQGGDWR EQASLICSMV DGPVSLEVIA
     TTHEEMIKEA KDLVSFGENV VVKIPMIAEG LRAMRELGER GIRVNATLVF SPAQALLAAK
     LGATYVSPFV GRLDGLSQSG MECVEQIRTI FDNYDFKTQI LVASVRHPMH VLDAALIGAD
     VVTLPYATLA QLIRHPLTDS GLAAFLADWE AFQKG
//