ID   ALF2_RHOCA              Reviewed;         114 AA.
AC   P50923;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Fructose-bisphosphate aldolase 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 II;
DE   Flags: Fragment;
GN   Name=cbbA; Synonyms=cfxB;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11166 / DSM 1710 / CCUG 31484 / JCM 21090 / LMG 2962 / NBRC
RC   16435 / NCIMB 8254 / ATH 2.3.1;
RA   Larimer F.W., Lu T.-Y.S., Buley D.M.;
RL   Submitted (APR-1995) 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: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 biosynthesis; Calvin cycle.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: This protein is encoded within the form II ribulose-
CC       bisphosphate carboxylase operon.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; U23145; AAB82047.1; -; Genomic_DNA.
DR   PIR; T10505; T10505.
DR   AlphaFoldDB; P50923; -.
DR   SMR; P50923; -.
DR   UniPathway; UPA00109; UER00183.
DR   UniPathway; UPA00116; -.
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   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   Pfam; PF01116; F_bP_aldolase; 1.
PE   3: Inferred from homology;
KW   Calvin cycle; Glycolysis; Lyase; Zinc.
FT   CHAIN           <1..114
FT                   /note="Fructose-bisphosphate aldolase 2"
FT                   /id="PRO_0000178732"
FT   BINDING         35..38
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   114 AA;  12747 MW;  18811FF5D217BD92 CRC64;
     LQDIINEFGG AMPQTFGVPV EEIVRGIKMG VRKVNIDTDC RMRMTGQFRR IAEQNKAEFD
     PRKFLKPAMD AMRDLCKARL EAFGTAGHAS KIKVIPMDDM AKRYASGSLA PKTN