ID A0A1J5GX73_9BACT Unreviewed; 288 AA.
AC A0A1J5GX73;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Tagatose-bisphosphate aldolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUK09_00935 {ECO:0000313|EMBL:OIP76836.1};
OS Parcubacteria group bacterium CG2_30_36_38.
OC Bacteria.
OX NCBI_TaxID=1805316 {ECO:0000313|EMBL:OIP76836.1, ECO:0000313|Proteomes:UP000183308};
RN [1] {ECO:0000313|EMBL:OIP76836.1, ECO:0000313|Proteomes:UP000183308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_36_38 {ECO:0000313|EMBL:OIP76836.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIP76836.1}.
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DR EMBL; MNZE01000016; OIP76836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5GX73; -.
DR STRING; 1805316.AUK09_00935; -.
DR Proteomes; UP000183308; 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.
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 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 183
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 184
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 214
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 215..217
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 236..239
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 288 AA; 31896 MW; 2236E74A94BC889F CRC64;
MLIHISEIIK EGREKKFALG AFNTFNLEST LGIAGAAEEK KAAAILQVSE ATISYAGLKA
ITHIVKTVAK NQARKARIAL HLDHGKKFLS VVECIKAGFS SVMMDAADLP FDENVALTKK
AVDYAHKHKV WAQGELGKIV KEPLEIEELR RNPEKFLTDP DLAREFVRKT NVDTLAVSIG
NVHGFYKMKN GAPHLFLNHL KEIREKVNVP LVLHGASGIS VEETKKAREL GVQIVNIDTE
IRMTFRESLS RSLAEAGANG EFDPRKILEP SIKAIKELVK RKIGDFGQ
//
