ID F8TQC3_9SYNE Unreviewed; 204 AA.
AC F8TQC3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 28-JUN-2023, entry version 30.
DE SubName: Full=Fructose-1,6-bisphosphate aldolase {ECO:0000313|EMBL:AEJ33850.1};
DE Flags: Fragment;
OS Synechococcus sp. A15-48A3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1050653 {ECO:0000313|EMBL:AEJ33850.1};
RN [1] {ECO:0000313|EMBL:AEJ33850.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A15-48A3 {ECO:0000313|EMBL:AEJ33850.1};
RA Mazard S.L., Ostrowski M., Partensky F., Scanlan D.J.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEJ33850.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A15-48A3 {ECO:0000313|EMBL:AEJ33850.1};
RX PubMed=21651684; DOI=10.1111/j.1462-2920.2011.02514.x;
RA Mazard S., Ostrowski M., Partensky F., Scanlan D.J.;
RT "Multi-locus sequence analysis, taxonomic resolution and biogeography of
RT marine Synechococcus.";
RL Environ. Microbiol. 14:372-386(2012).
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; JF307282; AEJ33850.1; -; Genomic_DNA.
DR AlphaFoldDB; F8TQC3; -.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
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 Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 93
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 94
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 127
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 128..130
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 170..173
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEJ33850.1"
FT NON_TER 204
FT /evidence="ECO:0000313|EMBL:AEJ33850.1"
SQ SEQUENCE 204 AA; 21798 MW; F01B8D190B78EFBE CRC64;
GSLEADAKTP ASYEYNVAVT KQVVDFAHSV GVSVEGELGC LGSLETGKGE AEDGHGFEGE
LSKDMLLTDP AEAADFVAKT KCDALAIAIG TSHGAYKFTR KPTGEVLAIS RIAEIHKAIP
NTHLVMHGSS SVPQEWLEMI NKHGGSIPET YGVPVEEIQE GIRNGVRKVN IDTDNRLAFT
AAVREAAMAD PANFDPRHFN KPAR
//
