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Database: UniProt
Entry: A0A2A7MEN4_9CLOT
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Original site: A0A2A7MEN4_9CLOT 
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}.
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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
//
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