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Database: UniProt
Entry: H1PPL8_9FUSO
LinkDB: H1PPL8_9FUSO
Original site: H1PPL8_9FUSO 
ID   H1PPL8_9FUSO            Unreviewed;       325 AA.
AC   H1PPL8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Fructose-1,6-bisphosphate aldolase, class II {ECO:0000313|EMBL:EHO84065.1};
GN   ORFNames=HMPREF0402_00361 {ECO:0000313|EMBL:EHO84065.1};
OS   Fusobacterium ulcerans 12-1B.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=457404 {ECO:0000313|EMBL:EHO84065.1, ECO:0000313|Proteomes:UP000003233};
RN   [1] {ECO:0000313|EMBL:EHO84065.1, ECO:0000313|Proteomes:UP000003233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12_1B {ECO:0000313|EMBL:EHO84065.1,
RC   ECO:0000313|Proteomes:UP000003233};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Ambrose C.E.,
RA   Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusobacterium ulcerans 12_1B.";
RL   Submitted (JUL-2012) 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:EHO84065.1}.
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DR   EMBL; AGWJ02000003; EHO84065.1; -; Genomic_DNA.
DR   RefSeq; WP_005982212.1; NZ_KE161007.1.
DR   AlphaFoldDB; H1PPL8; -.
DR   GeneID; 78453175; -.
DR   PATRIC; fig|457404.5.peg.891; -.
DR   HOGENOM; CLU_040088_0_0_0; -.
DR   BioCyc; FSP457404-HMP:GTSQ-362-MONOMER; -.
DR   Proteomes; UP000003233; Unassembled WGS sequence.
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; PS00602; ALDOLASE_CLASS_II_1; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001359-3};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001359-3}.
FT   ACT_SITE        93
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT   BINDING         94
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         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         189
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         190
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         222
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         223..225
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         265..268
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ   SEQUENCE   325 AA;  35288 MW;  5085AA562BCD5CE8 CRC64;
     MYNYKDLGLS NTKEMFAKAN KEGYAVPAFN FNNMEMALAI VEACAEMGSP VILQCSKGAL
     SYMGADVVPL LGKAAVDRAR NMGSDIPVAL HLDHGPDIAT VKTCIESGFS SVMIDGSHYD
     FAKNIEVSKE VVEYAHKFDV TVEAELGVLA GIEDDVKAES HTYTNPDEVE EFVNKTGVDS
     LAIAIGTSHG AHKFKPGEDP KLRLDILEEI ERRIPGFPIV LHGSSAVPKQ YTDMIKEFGG
     EVKDAIGIPN AELRKASKSA VAKINVDTDG RLAFTAAIRR VLGTNPKEFD PRKYLGAAKD
     EMKAYYKTKI VDVFGSEGAY KKGTK
//
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