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Database: UniProt
Entry: W0EC12_9FIRM
LinkDB: W0EC12_9FIRM
Original site: W0EC12_9FIRM 
ID   W0EC12_9FIRM            Unreviewed;       284 AA.
AC   W0EC12;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Fructose-bisphosphate aldolase {ECO:0000313|EMBL:AHF08292.1};
GN   ORFNames=DESME_15575 {ECO:0000313|EMBL:AHF08292.1};
OS   Desulfitobacterium metallireducens DSM 15288.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=871968 {ECO:0000313|EMBL:AHF08292.1, ECO:0000313|Proteomes:UP000010847};
RN   [1] {ECO:0000313|EMBL:AHF08292.1, ECO:0000313|Proteomes:UP000010847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15288 {ECO:0000313|Proteomes:UP000010847};
RG   DOE Joint Genome Institute;
RA   Smidt H., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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};
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DR   EMBL; CP007032; AHF08292.1; -; Genomic_DNA.
DR   RefSeq; WP_006716783.1; NZ_CP007032.1.
DR   AlphaFoldDB; W0EC12; -.
DR   STRING; 871968.DESME_15575; -.
DR   KEGG; dmt:DESME_15575; -.
DR   eggNOG; COG0191; Bacteria.
DR   HOGENOM; CLU_040088_0_1_9; -.
DR   OrthoDB; 9803995at2; -.
DR   Proteomes; UP000010847; Chromosome.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic 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   InterPro; IPR011289; Fruc_bis_ald_class-2.
DR   NCBIfam; TIGR00167; cbbA; 1.
DR   NCBIfam; TIGR01859; fruc_bis_ald; 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   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001359-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010847};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001359-3}.
FT   ACT_SITE        82
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT   BINDING         83
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         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         180
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         181
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
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         209..211
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         230..233
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ   SEQUENCE   284 AA;  30427 MW;  172DCF72DC19B2F6 CRC64;
     MSLVPMTELL KKAQQGHYAV GAFNCNNMEI VQAIVAAAEA EKSPVIIQAS QGAIKYAGIE
     YISTLTQLAA EKASVPVALH LDHGTSFAQV VQCVRNGFSS VMIDGSKLPL EENIALTNKV
     IEVAHSIGVS VEAELGKIGG TEDDISVSER DTLFTDPSDA ERFVREAKVD ALAIAIGTAH
     GQYKGVPKLD FERLKEIRKR VDTPIVLHGS SGVPEEAIRE AISLGVCKVN IDTNIREAFV
     AAARQVMEQN PNEIDPRKML GPAREATIAI IRGKIQIFGS SGKA
//
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