ID   ALF_STRGB               Reviewed;         340 AA.
AC   Q9ZEM7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Fructose-bisphosphate aldolase;
DE            Short=FBP aldolase;
DE            Short=FBPA;
DE            EC=4.1.2.13;
DE   AltName: Full=Fructose-1,6-bisphosphate aldolase;
GN   Name=fba; Synonyms=fda;
OS   Streptomyces galbus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=33898;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 14077 / CBS 700.72 / DSM 40480 / NBRC 13399 / VKM Ac-160;
RX   PubMed=11287146; DOI=10.1111/j.1574-6968.2001.tb10582.x;
RA   Wehmeier U.F.;
RT   "Molecular cloning, nucleotide sequence and structural analysis of the
RT   Streptomyces galbus DSM40480 fda gene: the S. galbus fructose-1,6-
RT   bisphosphate aldolase is a member of the class II aldolases.";
RL   FEMS Microbiol. Lett. 197:53-58(2001).
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.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC       provides a structural contribution. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5.;
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; AJ131707; CAA10483.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZEM7; -.
DR   SMR; Q9ZEM7; -.
DR   STRING; 33898.JRHJ01000001_gene613; -.
DR   PRIDE; Q9ZEM7; -.
DR   UniPathway; UPA00109; UER00183.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   InterPro; IPR006411; Fruct_bisP_bact.
DR   PANTHER; PTHR30559; PTHR30559; 1.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   TIGRFAMs; TIGR00167; cbbA; 1.
DR   TIGRFAMs; TIGR01520; FruBisAldo_II_A; 1.
DR   PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
PE   1: Evidence at protein level;
KW   Glycolysis; Lyase; Metal-binding; Zinc.
FT   CHAIN           1..340
FT                   /note="Fructose-bisphosphate aldolase"
FT                   /id="PRO_0000178744"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         250..252
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
FT   BINDING         271..274
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   340 AA;  36550 MW;  8DB47E14F8B8E9F7 CRC64;
     MPIATPEVYN EMLDRAKAGK FAYPAINVTS SQTLNAALRG FAEAESDGIV QISTGGAEFL
     GGQYSKDMVT GAVALAEFAH IIAEKYPVNI ALHTDHCPKD KLDGYVRPLL ALSKKRVEAG
     LGPLFQSHMW DGSAEPLADN LAIAQELLET ARAAQIILEV EITPTGGEED GVSHEINDSL
     YTTVDDAIRT AEALGLGEKG RYLLAASFGN VHGVYKPGNV VLRPELLKEL NEGVAARFGK
     ESPFDFVFHG GSGSSEEEIR TALENGVVKM NLDTDTQYAF TRPVAGHMFA NYDGVLKVDG
     EVGNKKAYDP RTWGKLAEAS MAARVVEATQ HLRSAGNKIK