ALF_CAMJE
ID ALF_CAMJE Reviewed; 354 AA.
AC Q0PAS0; P53818;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=fda, fdaC; OrderedLocusNames=Cj0597;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL34743.1; -; Genomic_DNA.
DR PIR; S52413; S52413.
DR RefSeq; WP_002852272.1; NC_002163.1.
DR RefSeq; YP_002344027.1; NC_002163.1.
DR PDB; 3QM3; X-ray; 1.85 A; A/B/C/D/E/F/G/H=1-354.
DR PDBsum; 3QM3; -.
DR AlphaFoldDB; Q0PAS0; -.
DR SMR; Q0PAS0; -.
DR IntAct; Q0PAS0; 9.
DR STRING; 192222.Cj0597; -.
DR PaxDb; Q0PAS0; -.
DR PRIDE; Q0PAS0; -.
DR EnsemblBacteria; CAL34743; CAL34743; Cj0597.
DR GeneID; 904922; -.
DR KEGG; cje:Cj0597; -.
DR PATRIC; fig|192222.6.peg.589; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_036923_0_0_7; -.
DR OMA; QAYCAEK; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000000799; 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 1: Evidence at protein level;
KW 3D-structure; Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..354
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000178711"
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 HELIX 3..5
FT /evidence="ECO:0007829|PDB:3QM3"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:3QM3"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:3QM3"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 76..95
FT /evidence="ECO:0007829|PDB:3QM3"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 111..128
FT /evidence="ECO:0007829|PDB:3QM3"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:3QM3"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:3QM3"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:3QM3"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:3QM3"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:3QM3"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 267..275
FT /evidence="ECO:0007829|PDB:3QM3"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 285..302
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:3QM3"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:3QM3"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:3QM3"
FT HELIX 326..347
FT /evidence="ECO:0007829|PDB:3QM3"
SQ SEQUENCE 354 AA; 38730 MW; E4ACB44EA1860135 CRC64;
MGVLDIVKAG VISGDELNKI 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
