ID A0A2A7MEN4_9CLOT Unreviewed; 215 AA.
AC A0A2A7MEN4;
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=Probable transaldolase {ECO:0000256|HAMAP-Rule:MF_00494};
DE EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00494};
GN Name=fsa {ECO:0000313|EMBL:PEG30312.1};
GN Synonyms=tal {ECO:0000256|HAMAP-Rule:MF_00494,
GN ECO:0000313|EMBL:CAG9709685.1}, tal_2 {ECO:0000313|EMBL:VCT83677.1};
GN ORFNames=CNEO_44333 {ECO:0000313|EMBL:CAG9709685.1},
GN CNEONATNEC25_01274 {ECO:0000313|EMBL:VCT83677.1}, CQ394_00860
GN {ECO:0000313|EMBL:PEG30312.1};
OS Clostridium neonatale.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=137838 {ECO:0000313|EMBL:PEG30312.1, ECO:0000313|Proteomes:UP000220840};
RN [1] {ECO:0000313|EMBL:PEG30312.1, ECO:0000313|Proteomes:UP000220840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCDC99A005 {ECO:0000313|EMBL:PEG30312.1,
RC ECO:0000313|Proteomes:UP000220840};
RA Bernard K., Burdz T., Wiebe D., Balcewich B., Alfa M., Bernier A.-M.;
RT "Effective Description of Clostridium neonatale sp. nov. linked to
RT necrotizing enterocolitis in neonates and a clarification of species
RT assignable to the genus Clostridium (Prazmowski 1880) emend. Lawson and
RT Rainey 2016.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VCT83677.1, ECO:0000313|Proteomes:UP000431451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEC25 {ECO:0000313|EMBL:VCT83677.1,
RC ECO:0000313|Proteomes:UP000431451};
RG IHU Genomes;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CAG9709685.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CC3_PB {ECO:0000313|EMBL:CAG9709685.1};
RA Mesa V.;
RL Submitted (OCT-2021) 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}.
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; CAKJVE010000004; CAG9709685.1; -; Genomic_DNA.
DR EMBL; PDCJ01000001; PEG30312.1; -; Genomic_DNA.
DR EMBL; UWJD01000001; VCT83677.1; -; Genomic_DNA.
DR RefSeq; WP_058294483.1; NZ_UWJD01000001.1.
DR STRING; 137838.GCA_001458595_01610; -.
DR OrthoDB; 9807051at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000220840; Unassembled WGS sequence.
DR Proteomes; UP000431451; Unassembled WGS sequence.
DR Proteomes; UP000789738; Unassembled WGS sequence.
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:UP000220840};
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; 23318 MW; C0663B1A5E70A215 CRC64;
MKLFIDTANV ADIKMANDMG IICGVTTNPS LIAKEGRDFN EVIKEITSIV DGPISGEVIS
LDADGMIKEG REIAKIHKNM VVKIPMTEEG LKAVKVLSKE NIKTNVTLIF TPAQALLAAR
AGASYVSPFL GRLDDIATNS LELIKTIVDI FKIHDITTEI ITASIRSPLH VVDAARAGAH
IATVPANVIK AMLKHPLTDS GIERFMKDWN DAFNK
//