ID A0A1G7UD73_9LACT Unreviewed; 277 AA.
AC A0A1G7UD73;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013779};
GN ORFNames=SAMN05421791_10937 {ECO:0000313|EMBL:SDG44989.1};
OS Facklamia miroungae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX NCBI_TaxID=120956 {ECO:0000313|EMBL:SDG44989.1, ECO:0000313|Proteomes:UP000199708};
RN [1] {ECO:0000313|EMBL:SDG44989.1, ECO:0000313|Proteomes:UP000199708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-466 {ECO:0000313|EMBL:SDG44989.1,
RC ECO:0000313|Proteomes:UP000199708};
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; FNCK01000009; SDG44989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7UD73; -.
DR STRING; 120956.SAMN05421791_10937; -.
DR OrthoDB; 9803995at2; -.
DR Proteomes; UP000199708; Unassembled WGS sequence.
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 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.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000199708};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 81
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 82
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 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 179
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 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"
SQ SEQUENCE 277 AA; 30939 MW; 72392718C70BB676 CRC64;
MRVSSSQLLK KAQNNHYAVP AVNFIDGLTA NAYLAVAEKL NMPMILAFAQ AHNEWLSLEE
AAWIGTHIQE KATVPIVLHL DHGQDIHFIQ RAIDLGFNSV MIDASTETFA NNVKRTKEVV
NYAHDHGVDV EAEIGFVGAN ENLENHELVE SIYTEVEDAI EFVNQTKVDS LAISIGTAHG
IYKGTPKINF KRLSQIRERI DIPLVLHGGS STGYENLNRC AREGITKINL FSDMINAGFN
AINMPSVKDY PSLIIQMKKS IEKQLEEYYA VFGLIER
//
