ALF2_CERSP
ID ALF2_CERSP Reviewed; 354 AA.
AC P29271;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 90.
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;
GN Name=cfxB;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1939098; DOI=10.1016/s0021-9258(18)54944-9;
RA Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R.;
RT "Identification, expression, and deduced primary structure of transketolase
RT and other enzymes encoded within the form II CO2 fixation operon of
RT Rhodobacter sphaeroides.";
RL J. Biol. Chem. 266:20447-20452(1991).
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.
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; M68914; AAA26157.1; -; Genomic_DNA.
DR PIR; D41080; D41080.
DR RefSeq; WP_011339169.1; NZ_WSNV01000001.1.
DR AlphaFoldDB; P29271; -.
DR SMR; P29271; -.
DR OrthoDB; 827430at2; -.
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 CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR006412; Fruct_bisP_Calv.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01521; FruBisAldo_II_B; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 3: Inferred from homology;
KW Calvin cycle; Glycolysis; Lyase; Metal-binding; Zinc.
FT CHAIN 1..354
FT /note="Fructose-bisphosphate aldolase 2"
FT /id="PRO_0000178733"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 233..235
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 275..278
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
SQ SEQUENCE 354 AA; 38269 MW; 9F547E84FC72ACF5 CRC64;
MALITLRQLL DHAAEQGYGV PAFNINNMEQ GLAIMEAARA CDAPVIIQAS RGARSYANDI
MLAKMIEALA AIYPEIPLCM HQDHGNNEAT CMTAIRHGFT SVMMDGSLKA DAKTPADYDY
NVDITARVSH MAHWVGASVE GELGVLGSLE TGESEAEDGH GAEGKLDHSQ LLTDPDQAVD
FVKKTQVDAL AIACGTSHGA YKFSRKPDGE ILAMSVIEAI HKKLPDTHLV MHGSSSVPQE
LQDIINAFGG AMPQTFGVPV EEIVRGIKMG VRKVNIDTDC RMAMTGQFRR IAQQTPSEFD
PRKFLKPAMD AMRDLCKQRL EAFGTAGQAG KIRIIPMDDM AKRYASGALA PKTA
