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Database: UniProt
Entry: E6U7S7_ETHHY
LinkDB: E6U7S7_ETHHY
Original site: E6U7S7_ETHHY 
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
//
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