ALF_CAMJJ
ID ALF_CAMJJ Reviewed; 354 AA.
AC A1VYV7; P53818;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
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=fbaA, fda, fdaC; OrderedLocusNames=CJJ81176_0625;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8525063; DOI=10.1016/0923-2508(96)80292-0;
RA Burucoa C., Fremaux C., Pei Z., Tummuru M., Blaser M.J., Cenatiempo Y.,
RA Fauchere J.L.;
RT "Nucleotide sequence and characterization of peb4A encoding an antigenic
RT protein in Campylobacter jejuni.";
RL Res. Microbiol. 146:467-476(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) 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 degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; X84703; CAA59176.1; -; Genomic_DNA.
DR EMBL; CP000538; EAQ73283.1; -; Genomic_DNA.
DR PIR; S52413; S52413.
DR RefSeq; WP_002856965.1; NC_008787.1.
DR AlphaFoldDB; A1VYV7; -.
DR SMR; A1VYV7; -.
DR STRING; 354242.CJJ81176_0625; -.
DR EnsemblBacteria; EAQ73283; EAQ73283; CJJ81176_0625.
DR KEGG; cjj:CJJ81176_0625; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_036923_0_0_7; -.
DR OMA; QAYCAEK; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000000646; 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; -; 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.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 3: Inferred from homology;
KW Glycolysis; Lyase; Metal-binding; Zinc.
FT CHAIN 1..354
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000281895"
FT ACT_SITE 104
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 261..263
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 282..285
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT CONFLICT 20
FT /note="V -> I (in Ref. 1; CAA59176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 38716 MW; 3F42FDE4782192C3 CRC64;
MGVLDIVKAG VISGDELNKV YDYAKAEGFA IPAVNVVGTD SINAVLEAAK KVNSPVIIQF
SNGGAKFYAG KNCPNGEVLG AISGAKHVHL LAKAYGVPVI LHTDHAARKL LPWIDGLIEA
NAQYKKTHGQ ALFSSHMLDL SEESLEENLS TCEVYLQKLD ALGVALEIEL GCTGGEEDGV
DNTGIDNSKL YTQPEDVALA YERLGKISDK FSIAASFGNV HGVYKPGNVS LQPEILKNSQ
KFVKDKFALN SDKPINFVFH GGSGSELKDI KNAVSYGVIK MNIDTDTQWA FWDGVREYEL
KNRAYLQGQI GNPEGDDKPN KKYYDPRVWL RSGEESMIKR LEIAFEDLNC INKN
