ID A0A0X8F7L3_9LACT Unreviewed; 302 AA.
AC A0A0X8F7L3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013779};
GN ORFNames=CYJ27_00600 {ECO:0000313|EMBL:PKY91973.1}, HMPREF3187_00274
GN {ECO:0000313|EMBL:KXB37880.1};
OS Aerococcus christensenii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX NCBI_TaxID=87541 {ECO:0000313|EMBL:PKY91973.1, ECO:0000313|Proteomes:UP000234775};
RN [1] {ECO:0000313|EMBL:KXB37880.1, ECO:0000313|Proteomes:UP000070422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00635 {ECO:0000313|EMBL:KXB37880.1,
RC ECO:0000313|Proteomes:UP000070422};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PKY91973.1, ECO:0000313|Proteomes:UP000234775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0844 {ECO:0000313|EMBL:PKY91973.1,
RC ECO:0000313|Proteomes:UP000234775};
RA Thomas-White K., Wolfe A.J.;
RT "Phylogenetic diversity of female urinary microbiome.";
RL Submitted (DEC-2017) 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:PKY91973.1}.
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DR EMBL; LSCQ01000017; KXB37880.1; -; Genomic_DNA.
DR EMBL; PKGZ01000001; PKY91973.1; -; Genomic_DNA.
DR RefSeq; WP_060776554.1; NZ_PKGZ01000001.1.
DR AlphaFoldDB; A0A0X8F7L3; -.
DR STRING; 87541.AWM71_02725; -.
DR KEGG; acg:AWM71_02725; -.
DR PATRIC; fig|87541.4.peg.275; -.
DR OrthoDB; 9803995at2; -.
DR Proteomes; UP000070422; Unassembled WGS sequence.
DR Proteomes; UP000234775; 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:0005975; P:carbohydrate metabolic 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 NCBIfam; TIGR00167; cbbA; 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.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:PKY91973.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000234775};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 86
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 87
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 175
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 176
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 204
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 205..207
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 226..229
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 302 AA; 32935 MW; 8F99A9A409C900B6 CRC64;
MAFLVNGNEI FKDARKNHYA VGAYNTNNLE WTRALITGAK ETRTPLLIQV STGAAKYMGG
YKLVRDLILN EMDSMDVDIP VILNLDHGTF EAAKECIALG YSSVMFDGHA LPVEENLAKT
KEIVKLAHER GISVEAEIGK IGENQGGGEL ASVEDAIRFA EAGVDKLACG IGNIHGVYPE
GWEGLNFERL KEIADAVDTP LVLHGGSGIP QDQIKKAISL GISKININTE FQLAFQKATR
EYIEAGKDLD KSSKGYDPRK LLRAGTDAIT ASMKEMISWM GTRSVDDKIS KVVFDEASLN
EE
//
