ALF_XANFL
ID ALF_XANFL Reviewed; 354 AA.
AC Q56815;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000303|PubMed:8550527};
DE Short=FBP aldolase;
DE Short=FBPA;
DE EC=4.1.2.13 {ECO:0000269|PubMed:8550527};
DE AltName: Full=Fructose-1,6-bisphosphate aldolase;
GN Name=cbbA {ECO:0000303|PubMed:8550527};
OS Xanthobacter flavus.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Xanthobacter.
OX NCBI_TaxID=281;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RC STRAIN=H4-14;
RX PubMed=8550527; DOI=10.1128/jb.178.3.888-893.1996;
RA van den Bergh E.R., Baker S.C., Raggers R.J., Terpstra P., Woudstra E.C.,
RA Dijkhuizen L., Meijer W.G.;
RT "Primary structure and phylogeny of the Calvin cycle enzymes transketolase
RT and fructosebisphosphate aldolase of Xanthobacter flavus.";
RL J. Bacteriol. 178:888-893(1996).
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:0000269|PubMed:8550527}.
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:0000269|PubMed:8550527};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0AB71};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000250|UniProtKB:P0AB71};
CC -!- ACTIVITY REGULATION: Activity is stimulated by Fe(2+) in
CC autotrophically grown cells. {ECO:0000269|PubMed:8550527}.
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 {ECO:0000250|UniProtKB:P0AB71}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0AB71}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; U29134; AAA96742.1; -; Genomic_DNA.
DR AlphaFoldDB; Q56815; -.
DR SMR; Q56815; -.
DR PRIDE; Q56815; -.
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 1: Evidence at protein level;
KW Calvin cycle; Glycolysis; Lyase; Metal-binding; Zinc.
FT CHAIN 1..354
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000178755"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0AB71"
FT BINDING 50
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P0AB71"
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|UniProtKB:P0AB71"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AB71"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AB71"
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|UniProtKB:P0AB71"
FT BINDING 199
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:P0AB71"
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|UniProtKB:P0AB71"
FT BINDING 233..235
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:P0AB71"
FT BINDING 275..278
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:P0AB71"
SQ SEQUENCE 354 AA; 37982 MW; DDF44661B527E4B7 CRC64;
MALVSMRQLL DHAADDSYGL PAFNVNNMEQ VKAIMDAARA TSSPVILQGS AGARKYAGEP
FLRHLIAAAV EAYPEIPVVM HQDHGASPAV CMGAIKSGFS SVMMDGSLKE DGKTPADYDY
NVSVTAKVVE LAHAVGVSVE GELGCLGSLE TGKGEAEDGH GAEEALDHSK LLTDPDEAAQ
FVKATQCDAL AIAIGTSHGA YKFTRKPTGD ILAIDRIKAI HQRIPTTHLV MHGSSSVPQE
LLEEIRTYGG DIKETYGVPV EEIQEGIRYG VRKVNIDTDI RLAMTAAIRR VGAKNKSEFD
PRKFMAAAME EAKKVCIARF EAFGSAGKAE KIRAIELDEM AKRYASGELA QVVH
