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Database: UniProt
Entry: A0A086AC40_9FLAO
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ID   A0A086AC40_9FLAO        Unreviewed;       356 AA.
AC   A0A086AC40;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU366023};
DE            Short=FBP aldolase {ECO:0000256|RuleBase:RU366023};
DE            EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU366023};
GN   ORFNames=IW15_02085 {ECO:0000313|EMBL:KFF14254.1};
OS   Chryseobacterium soli.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=445961 {ECO:0000313|EMBL:KFF14254.1, ECO:0000313|Proteomes:UP000028705};
RN   [1] {ECO:0000313|EMBL:KFF14254.1, ECO:0000313|Proteomes:UP000028705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19298 {ECO:0000313|EMBL:KFF14254.1,
RC   ECO:0000313|Proteomes:UP000028705};
RA   Stropko S.J., Pipes S.E., Newman J.;
RT   "Genome of Chryseobacterium soli DSM 19298.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC       phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate
CC       (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and
CC       the reverse reaction in glycolysis. {ECO:0000256|RuleBase:RU366023}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC         phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00000441,
CC         ECO:0000256|RuleBase:RU366023};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001359-3,
CC         ECO:0000256|RuleBase:RU366023};
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       ECO:0000256|RuleBase:RU366023};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00004714, ECO:0000256|RuleBase:RU366023}.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000256|ARBA:ARBA00005812, ECO:0000256|RuleBase:RU366023}.
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:KFF14254.1}.
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DR   EMBL; JPRH01000001; KFF14254.1; -; Genomic_DNA.
DR   RefSeq; WP_034708886.1; NZ_JPRH01000001.1.
DR   AlphaFoldDB; A0A086AC40; -.
DR   STRING; 445961.IW15_02085; -.
DR   eggNOG; COG0191; Bacteria.
DR   OrthoDB; 9803995at2; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000028705; Unassembled WGS sequence.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00946; FBP_aldolase_IIA; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   InterPro; IPR006411; Fruct_bisP_bact.
DR   NCBIfam; TIGR00167; cbbA; 1.
DR   NCBIfam; TIGR01520; FruBisAldo_II_A; 1.
DR   PANTHER; PTHR30559:SF0; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR30559; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2; 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   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU366023};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU366023};
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        106
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT   BINDING         107
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         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT   BINDING         223
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         224
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         261
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         262..264
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT   BINDING         283..286
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ   SEQUENCE   356 AA;  39183 MW;  92FA458E71769D6B CRC64;
     MSRIFPAGVA TGQLVTDIFQ YAKENKFALP AVNVIGSSNV NAVMETAAKL NSPVIIQFSN
     GGASFNAGKG LSNDGQKSAI LGAIAGAKHI HTLAEAYGAT VILHTDHCAK KLLPWIDGLM
     DANEEFFKQT GKSLYSSHML DLSEESLEEN LEVSAEYFER MAKMQMTLEV EIGVTGGEED
     GVDNSDVDNS KLYTQPEDVA YTYEKLKAIS DNFTIAAAFG NVHGVYKPGN VVLTPKILDN
     SQKFVQEKFG TAAKPINFVF HGGSGSTLEE IREAIDYGVI KMNIDTDLQF AYTEGIRDYM
     VNNIDYLRSQ IGNPEGEEKP NKKFYDPRNW VRKGEETFST RLVKAFEDLN NVNTLK
//
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