ID A0A0F0CAZ7_9CLOT Unreviewed; 287 AA.
AC A0A0F0CAZ7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Fructose-bisphosphate aldolase {ECO:0000313|EMBL:KJJ68530.1};
DE EC=4.1.2.13 {ECO:0000313|EMBL:KJJ68530.1};
GN Name=fba_1 {ECO:0000313|EMBL:KJJ68530.1};
GN ORFNames=CLFS41_45950 {ECO:0000313|EMBL:KJJ68530.1};
OS Clostridium sp. FS41.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ68530.1, ECO:0000313|Proteomes:UP000033604};
RN [1] {ECO:0000313|EMBL:KJJ68530.1, ECO:0000313|Proteomes:UP000033604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS41 {ECO:0000313|EMBL:KJJ68530.1,
RC ECO:0000313|Proteomes:UP000033604};
RA Poehlein A., Daniel R.;
RT "Genome sequencing of Clostridium sp. FS41.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001359-3};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000256|PIRSR:PIRSR001359-3};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJJ68530.1}.
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DR EMBL; JYHN01000069; KJJ68530.1; -; Genomic_DNA.
DR RefSeq; WP_007866016.1; NZ_JYHN01000069.1.
DR AlphaFoldDB; A0A0F0CAZ7; -.
DR GeneID; 77445794; -.
DR PATRIC; fig|1609975.3.peg.4912; -.
DR Proteomes; UP000033604; Unassembled WGS sequence.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR011289; Fruc_bis_ald_class-2.
DR NCBIfam; TIGR00167; cbbA; 1.
DR NCBIfam; TIGR01859; fruc_bis_ald; 1.
DR PANTHER; PTHR30304; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR30304:SF0; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE SUBUNIT GATY-RELATED; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:KJJ68530.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000033604};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 84
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 178
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 208..210
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 229..232
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 287 AA; 30652 MW; D476CA252538F916 CRC64;
MLVSAKEMLD KAREGKYAVG QFNINNLEWT KSVLLTAEEL KSPVILGVSE GAGKYMTGFK
TVAAMVEAMM EELNITVPVA LHLDHGSYEG CYKCIKAGFS SIMFDGSHYP IEENIEKTKE
LVKIAHAMGL SLEAEVGSIG GEEDGVVGLG ECADPNECKA IADLGIDFLA AGIGNIHGKY
PANWPGLRFD VLESVKEKVG DMPLVLHGGT GIPEDMIKKA ISLGVAKINV NTECQLTFAA
ATREYIEAGK DQQGKGFDPR KLLAPGADAI KATVKEKMEL FGSVGKA
//
