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Database: UniProt
Entry: A0A090ZIZ1_PAEMA
LinkDB: A0A090ZIZ1_PAEMA
Original site: A0A090ZIZ1_PAEMA 
ID   A0A090ZIZ1_PAEMA        Unreviewed;       288 AA.
AC   A0A090ZIZ1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Ketose-bisphosphate aldolase {ECO:0000313|EMBL:KFN10562.1, ECO:0000313|EMBL:MUG22029.1};
GN   ORFNames=DJ90_1010 {ECO:0000313|EMBL:KFN10562.1}, GNQ08_06250
GN   {ECO:0000313|EMBL:MUG22029.1};
OS   Paenibacillus macerans (Bacillus macerans).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=44252 {ECO:0000313|EMBL:KFN10562.1, ECO:0000313|Proteomes:UP000029278};
RN   [1] {ECO:0000313|EMBL:KFN10562.1, ECO:0000313|Proteomes:UP000029278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8244 {ECO:0000313|EMBL:KFN10562.1,
RC   ECO:0000313|Proteomes:UP000029278};
RA   Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA   Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA   Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MUG22029.1, ECO:0000313|Proteomes:UP000442469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3CT49 {ECO:0000313|EMBL:MUG22029.1,
RC   ECO:0000313|Proteomes:UP000442469};
RA   Olajide A.M., Chen S., Lapointe G.;
RT   "Draft genome sequences of five Paenibacillus species of dairy origin.";
RL   Submitted (NOV-2019) 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:KFN10562.1}.
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DR   EMBL; JMQA01000018; KFN10562.1; -; Genomic_DNA.
DR   EMBL; WNZZ01000003; MUG22029.1; -; Genomic_DNA.
DR   RefSeq; WP_036620166.1; NZ_WNZZ01000003.1.
DR   AlphaFoldDB; A0A090ZIZ1; -.
DR   STRING; 44252.DJ90_1010; -.
DR   GeneID; 77011756; -.
DR   PATRIC; fig|44252.3.peg.1475; -.
DR   HOGENOM; CLU_040088_0_1_9; -.
DR   OrthoDB; 9803995at2; -.
DR   Proteomes; UP000029278; Unassembled WGS sequence.
DR   Proteomes; UP000442469; 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:UP000029278};
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         180
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
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"
FT   BINDING         208..210
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         229..232
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ   SEQUENCE   288 AA;  31996 MW;  19E16A5300F6BCA1 CRC64;
     MYITLKEATR RAEALNYTVG AFNAHNLEML PDMIRAAKEQ GAPIIIQTSI DTAKYVGHEN
     FVAVCKSMAT TEMVDVVLHL DHARDFNDIK EAIDKGYTSV MYDGSHLPFK ENIMKTRAVV
     DYAHRYGVSV EGELGTIGGT EEGIHVDEDK QIYTDPKDAA EFVKATGVDA LAIAIGTNHG
     QYKSKTEVNI PLLKEIHAAV DVPLVIHGGT GVDEKDIHEL IDNGIRKFNV GTELLVTWTQ
     TAKETFRDTK VNKSLRHNII PCNQAVKEIV KHKIGIFMNK EGHLNTMR
//
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