ID   ALF_BUCBP               Reviewed;         359 AA.
AC   Q89AB6;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Fructose-bisphosphate aldolase class 2;
DE            Short=FBP aldolase;
DE            Short=FBPA;
DE            EC=4.1.2.13;
DE   AltName: Full=Fructose-1,6-bisphosphate aldolase;
DE   AltName: Full=Fructose-bisphosphate aldolase class II;
GN   Name=fbaA; Synonyms=fba; OrderedLocusNames=bbp_401;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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:0000250}.
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   -!- 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; AE016826; AAO27113.1; -; Genomic_DNA.
DR   RefSeq; WP_011091514.1; NC_004545.1.
DR   AlphaFoldDB; Q89AB6; -.
DR   SMR; Q89AB6; -.
DR   STRING; 224915.bbp_401; -.
DR   KEGG; bab:bbp_401; -.
DR   eggNOG; COG0191; Bacteria.
DR   HOGENOM; CLU_036923_0_0_6; -.
DR   OrthoDB; 9803995at2; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000000601; Chromosome.
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   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; PS00602; ALDOLASE_CLASS_II_1; 1.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..359
FT                   /note="Fructose-bisphosphate aldolase class 2"
FT                   /id="PRO_0000178710"
FT   ACT_SITE        110
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         266..268
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
FT   BINDING         287..290
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   359 AA;  40487 MW;  49DE95BCADB14B5B CRC64;
     MCNILNKIKP GVITGNEALK LFKIAKKNHF AIPAINCINT DSINIVLETA KKAKSPVIIQ
     FSYGGSNFIS GPGLTTNILH KKAIIGALSG ANHVHIMAKH YNVPVILHTD HCNKNMLPWI
     DELINVGTKH FKTYNKPLFT SHMIDLSNEK LDYNINICSK YLEKMRKINM LLEIELGCTG
     GEEDGINNTK INKSLLYTQP NEVNYAYERL SSVGPEFIIA ASFGNVHGVY KSGNVRLTPD
     ILKKSQNYVS KKHNLSCNPL CFVFHGGSGS SEKDIKKSIK YGVIKMNIDT DIQWATWQGI
     LNFYNKNNKY LHNQIGNLDN ENKPNKKYYD PRTWIRSSQI SVSNHLTKIF RILNSCNTL
//