ID H9UEJ5_FERPD Unreviewed; 217 AA.
AC H9UEJ5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=Ferpe_1889 {ECO:0000313|EMBL:AFG35938.1};
OS Fervidobacterium pennivorans (strain DSM 9078 / Ven5).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=771875 {ECO:0000313|EMBL:AFG35938.1, ECO:0000313|Proteomes:UP000007384};
RN [1] {ECO:0000313|Proteomes:UP000007384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9078 / Ven5 {ECO:0000313|Proteomes:UP000007384};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Noll K.M., Woyke T.;
RT "Complete sequence of Fervidobacterium pennivorans DSM 9078.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003260; AFG35938.1; -; Genomic_DNA.
DR RefSeq; WP_014452365.1; NC_017095.1.
DR AlphaFoldDB; H9UEJ5; -.
DR STRING; 771875.Ferpe_1889; -.
DR KEGG; fpe:Ferpe_1889; -.
DR PATRIC; fig|771875.3.peg.1914; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_079764_0_0_0; -.
DR OrthoDB; 9807051at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000007384; 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.
DR PROSITE; PS00958; TRANSALDOLASE_2; 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 217 AA; 23896 MW; 4FA5DD8E03908783 CRC64;
MKIFLDTANL EEIRQGVEWG IVDGVTTNPT LIAKEGADFE KRIKEICELV QGPVSAEVIS
LNWEGMVEEA RKLAAIDEHV VIKIPMTPDG IKAVKILSAE GIRTNVTLVF SANQALLAAK
AGATYVSPFV GRIDDNGNDG LKLLEEIMQI FANYGFETEV IAASIRHPMH VVEAALIGVD
IATVPFDVLK KMFMHPLTDV GIKRFLQDWE SYKSSKK
//
