ID E6U7S7_ETHHY Unreviewed; 288 AA.
AC E6U7S7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE SubName: Full=Fructose-1,6-bisphosphate aldolase, class II {ECO:0000313|EMBL:ADU28200.1};
DE EC=4.1.2.29 {ECO:0000313|EMBL:ADU28200.1};
GN OrderedLocusNames=Ethha_2707 {ECO:0000313|EMBL:ADU28200.1};
OS Ethanoligenens harbinense (strain DSM 18485 / JCM 12961 / CGMCC 1.5033 /
OS YUAN-3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ethanoligenens.
OX NCBI_TaxID=663278 {ECO:0000313|EMBL:ADU28200.1, ECO:0000313|Proteomes:UP000001551};
RN [1] {ECO:0000313|EMBL:ADU28200.1, ECO:0000313|Proteomes:UP000001551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18485 / JCM 12961 / CGMCC 1.5033 / YUAN-3
RC {ECO:0000313|Proteomes:UP000001551};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N., Wang A.,
RA Mouttaki H., He Z., Zhou J., Hemme C.L., Woyke T.;
RT "Complete sequence of Ethanoligenens harbinense YUAN-3.";
RL Submitted (DEC-2010) 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; CP002400; ADU28200.1; -; Genomic_DNA.
DR RefSeq; WP_013486543.1; NZ_CP025286.1.
DR AlphaFoldDB; E6U7S7; -.
DR STRING; 663278.Ethha_2707; -.
DR KEGG; eha:Ethha_2707; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_040088_0_1_9; -.
DR OMA; PRTWGKL; -.
DR Proteomes; UP000001551; Chromosome.
DR GO; GO:0047441; F:5-dehydro-2-deoxyphosphogluconate aldolase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ADU28200.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001359-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000001551};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 85
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 86
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 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 178
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 179
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 288 AA; 30514 MW; CD7953A04879F292 CRC64;
MSLVSAAEMT KKALAGKYAV GQFNINNLEW TKSILLTAQE LKSPVILGVS EGAGKYMTGY
KTVTAMVKAM IEELGITVPV ALHLDHGSYE GAYKAIEAGF SSIMFDGSHY PIEENVAKTK
ELVEKTHSMG LSLEAEVGAI GGEEDGVIGG GEVADPAECK RIADLGVDIL AAGIGNIHGV
YPANWQGLRF DVLAKIKEIV GDKPLVLHGG TGIPEDQIKK AISLGVSKIN VNTECQLSFA
AATRKYIEEG KDKQGKGFDP RKLLAPGAEA IKETVREKIA LFGSANKA
//