ID A0A1Q3NMW0_9BACT Unreviewed; 303 AA.
AC A0A1Q3NMW0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE SubName: Full=Ketose-bisphosphate aldolase {ECO:0000313|EMBL:OJU97137.1};
GN ORFNames=BGO18_03100 {ECO:0000313|EMBL:OJU97137.1};
OS Candidatus Saccharibacteria bacterium 47-87.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1895828 {ECO:0000313|EMBL:OJU97137.1, ECO:0000313|Proteomes:UP000185868};
RN [1] {ECO:0000313|EMBL:OJU97137.1, ECO:0000313|Proteomes:UP000185868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47-87 {ECO:0000313|EMBL:OJU97137.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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};
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:OJU97137.1}.
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DR EMBL; MKSO01000001; OJU97137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3NMW0; -.
DR STRING; 1895828.BGO18_03100; -.
DR Proteomes; UP000185868; 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 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.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 91
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 92
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 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 197
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 225
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 303 AA; 33477 MW; EADFCD6D8926348C CRC64;
MGLTIAEIRD NTLRARHLMQ RSRQQHFAVG AFNIDNQETL IAIARAAQKL NAPVLVEVSQ
GEVDAIGIDN LRDLVDNYKK EYGIEMYINL DHSPTVEACK AAIDAGYEFI HIDISQANHD
ASEEEIIEKT REVVEYAKFT GALVESEPHY FGGSSNVHTE TIDYQEIKKT FSTPESAKAF
VEATGVDTFA AAVGNLHGKY PVPKELDLEL LARIREAIPC QISLHGGSGT PLHYFEDAAK
IGVSKININS DMRYAFRTVM EEELKAHPDE FAVVKLMDKV KDAVQAVVEE KIQAFGSAGK
AVV
//
