ID E6U9V9_ETHHY Unreviewed; 215 AA.
AC E6U9V9;
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=Ethha_0655 {ECO:0000313|EMBL:ADU26225.1};
OS Ethanoligenens harbinense (strain DSM 18485 / JCM 12961 / CGMCC 1.5033 /
OS YUAN-3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ethanoligenens.
OX NCBI_TaxID=663278 {ECO:0000313|EMBL:ADU26225.1, ECO:0000313|Proteomes:UP000001551};
RN [1] {ECO:0000313|EMBL:ADU26225.1, ECO:0000313|Proteomes:UP000001551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18485 / JCM 12961 / CGMCC 1.5033 / YUAN-3
RC {ECO:0000313|Proteomes:UP000001551};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Wang A.,
RA Mouttaki H., He Z., Zhou J., Hemme C.L., Woyke T.;
RT "Complete sequence of Ethanoligenens harbinense YUAN-3.";
RL Submitted (DEC-2010) 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; CP002400; ADU26225.1; -; Genomic_DNA.
DR RefSeq; WP_013484595.1; NZ_CP025286.1.
DR AlphaFoldDB; E6U9V9; -.
DR STRING; 663278.Ethha_0655; -.
DR KEGG; eha:Ethha_0655; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_079764_0_0_9; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000001551; 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; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF36; TRANSALDOLASE-RELATED; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001551};
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; 23204 MW; 0B11B493FFE4EA1C CRC64;
MKLFVDTANV DEIRWANDLG VICGVTTNPS LIAKSGRIFE EVVREITTIV DGPISAEVVS
LEAEKMVEEA LPLAAIHPNI VIKLPLCAEG LKATKRLAAK GIHTNVTLVF SAAQALLAAR
AGATYVSPFL GRVDDISWEG MTLVRDIAEI FKVHGIPTEI IAASIRSPLH VTEAAKAGAH
IATVPYKVIL QMIEHPLTKI GVERFLKDWE SVPKA
//
