ID A0A0G0VJU8_9BACT Unreviewed; 310 AA.
AC A0A0G0VJU8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE SubName: Full=Ketose-bisphosphate aldolase, class-II {ECO:0000313|EMBL:KKS01290.1};
GN ORFNames=UU54_C0007G0009 {ECO:0000313|EMBL:KKS01290.1};
OS Candidatus Yanofskybacteria bacterium GW2011_GWA2_41_22.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1619023 {ECO:0000313|EMBL:KKS01290.1, ECO:0000313|Proteomes:UP000033903};
RN [1] {ECO:0000313|EMBL:KKS01290.1, ECO:0000313|Proteomes:UP000033903}
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:KKS01290.1}.
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DR EMBL; LCBA01000007; KKS01290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0VJU8; -.
DR PATRIC; fig|1619023.3.peg.180; -.
DR Proteomes; UP000033903; 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 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 Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 107
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 108
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 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 208
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 238
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 310 AA; 33979 MW; 4536A57B72D3239F CRC64;
MRGEIPAGIY AVPEKFTCQP VSRFKNMLNL NSHLQKAKEG HYAIGHFNFA TADVLRGIIE
AAKEAGVPAV MVGTSEGEAG FIGMKEAVAL VAALRGEYDF PVFLNADHFK SFEKCKEAID
AGYDSVIIDA SRLPYHENVA ITKKVVDYAR SVNSDISVES ELGYLRGKSE LQTKIEISPD
DYTKPEEAAR FIAETGVARL AIVFGNIHGI VTEQIEKLDI KHLRKITAAV PETFLVLHGA
SGLKDEDIAT SIKAGIVNVH FNTELRVAYR EGIDKALHAK PDESAPYKYL ALAVEDVKKV
VAEKVKLFMS
//
