ID A0A0G0SIM5_9BACT Unreviewed; 295 AA.
AC A0A0G0SIM5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE SubName: Full=Ketose-bisphosphate aldolase, class-II {ECO:0000313|EMBL:KKR25577.1};
GN ORFNames=UT58_C0042G0003 {ECO:0000313|EMBL:KKR25577.1};
OS Microgenomates group bacterium GW2011_GWC1_39_7b.
OC Bacteria.
OX NCBI_TaxID=1618516 {ECO:0000313|EMBL:KKR25577.1, ECO:0000313|Proteomes:UP000034178};
RN [1] {ECO:0000313|EMBL:KKR25577.1, ECO:0000313|Proteomes:UP000034178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKR25577.1}.
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DR EMBL; LBXI01000042; KKR25577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0SIM5; -.
DR Proteomes; UP000034178; 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 83
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 84
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 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 189
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 217
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 295 AA; 32807 MW; 13580042B4F11CB4 CRC64;
MINQEKARKL WERTKREKFA VGAFNIDNQE TLIAIARAAR AKNSPVLVEL SQGEVDLIGL
ANTRDLVDNY KAEYGIEMYI NLDHCPSVEQ ARAGIDQGFE FIHIDVSQAN HNATDEEIIA
ATREVVAYAG KTGALVESEP HYFGGSSNVH QENIDYEEIK KTFSTPEGAK VFVEATGIDT
FAAAIGNLHG RYPIPKQLDI ELLKRTRAAI RCAISLHGGS DTPAHFFKEA VQVGISKVNI
NSDMRYAFRT ELENQLRDHP DEYAVVKLEP PVIEAVQKVV EEHIDMFGSA NKAQL
//
