ID A0A0D1V2R6_ANEMI Unreviewed; 287 AA.
AC A0A0D1V2R6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Fructose-bisphosphate aldolase {ECO:0000313|EMBL:KON94479.1, ECO:0000313|EMBL:SDI43758.1};
DE EC=4.1.2.13 {ECO:0000313|EMBL:KON94479.1};
GN ORFNames=AF333_02215 {ECO:0000313|EMBL:KON94479.1}, SAMN04487909_10412
GN {ECO:0000313|EMBL:SDI43758.1};
OS Aneurinibacillus migulanus (Bacillus migulanus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=47500 {ECO:0000313|EMBL:KON94479.1, ECO:0000313|Proteomes:UP000037269};
RN [1] {ECO:0000313|EMBL:KON94479.1, ECO:0000313|Proteomes:UP000037269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2895 {ECO:0000313|EMBL:KON94479.1,
RC ECO:0000313|Proteomes:UP000037269};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14205 dsm 2895.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SDI43758.1, ECO:0000313|Proteomes:UP000182836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2895 {ECO:0000313|EMBL:SDI43758.1,
RC ECO:0000313|Proteomes:UP000182836};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; LGUG01000004; KON94479.1; -; Genomic_DNA.
DR EMBL; FNED01000004; SDI43758.1; -; Genomic_DNA.
DR RefSeq; WP_043067529.1; NZ_LIXL01000010.1.
DR AlphaFoldDB; A0A0D1V2R6; -.
DR STRING; 47500.AF333_02215; -.
DR PATRIC; fig|47500.12.peg.335; -.
DR OrthoDB; 9803995at2; -.
DR Proteomes; UP000037269; Unassembled WGS sequence.
DR Proteomes; UP000182836; 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; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:KON94479.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000037269};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 86
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 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 183
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 184
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 211
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 212..214
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 233..236
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 287 AA; 30897 MW; 815D958E8F3E519A CRC64;
MPLVSMTDML NKAVEGKYAV GQFNLNNLEF TQAILQAAEE EKSPVILGVS EGAARYMGGF
KLVVAIVQAL MEEYKITVPV AIHLDHGSSF EKCVEAIHAG FTSVMIDGSH HPLEENIALT
KRVVDVAHAL GVSVEAELGR IGGQEDDLIV QDAEAAYAIP AECDKLVRET GVDCFAPALG
SVHGPYKGEP NLGFDRMEEV MKLTGVPLVL HGGTGIPTKD IQRAISLGTA KINVNTENQI
ASAKTVREVL DAKPELYDPR KYLGPARDTI KETVKGKMRE FGSSNKA
//
