ALF_HELPY
ID ALF_HELPY Reviewed; 307 AA.
AC P56109;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
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; OrderedLocusNames=HP_0176;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000511; AAD07246.1; -; Genomic_DNA.
DR PIR; H64541; H64541.
DR RefSeq; NP_206975.1; NC_000915.1.
DR RefSeq; WP_000960471.1; NC_018939.1.
DR PDB; 3C4U; X-ray; 1.83 A; A/B=1-307.
DR PDB; 3C52; X-ray; 2.30 A; A/B=1-307.
DR PDB; 3C56; X-ray; 2.30 A; A/B=1-307.
DR PDB; 5UCK; X-ray; 1.78 A; A/B=1-307.
DR PDB; 5UCN; X-ray; 1.67 A; A/B=1-307.
DR PDB; 5UCP; X-ray; 1.44 A; A/B=1-307.
DR PDB; 5UCS; X-ray; 1.41 A; A/B=1-307.
DR PDB; 5UCZ; X-ray; 1.78 A; A/B=1-307.
DR PDB; 5UD0; X-ray; 1.65 A; A/B=1-307.
DR PDB; 5UD1; X-ray; 1.79 A; A/B=1-307.
DR PDB; 5UD2; X-ray; 1.77 A; A/B=1-307.
DR PDB; 5UD3; X-ray; 1.44 A; A/B=1-307.
DR PDB; 5UD4; X-ray; 1.50 A; A/B=1-307.
DR PDB; 5VJF; X-ray; 1.85 A; A/B=1-307.
DR PDBsum; 3C4U; -.
DR PDBsum; 3C52; -.
DR PDBsum; 3C56; -.
DR PDBsum; 5UCK; -.
DR PDBsum; 5UCN; -.
DR PDBsum; 5UCP; -.
DR PDBsum; 5UCS; -.
DR PDBsum; 5UCZ; -.
DR PDBsum; 5UD0; -.
DR PDBsum; 5UD1; -.
DR PDBsum; 5UD2; -.
DR PDBsum; 5UD3; -.
DR PDBsum; 5UD4; -.
DR PDBsum; 5VJF; -.
DR AlphaFoldDB; P56109; -.
DR SMR; P56109; -.
DR STRING; 85962.C694_00875; -.
DR BindingDB; P56109; -.
DR ChEMBL; CHEMBL1287618; -.
DR PaxDb; P56109; -.
DR EnsemblBacteria; AAD07246; AAD07246; HP_0176.
DR KEGG; hpy:HP_0176; -.
DR PATRIC; fig|85962.47.peg.190; -.
DR eggNOG; COG0191; Bacteria.
DR OMA; PRTWGKL; -.
DR PhylomeDB; P56109; -.
DR BRENDA; 4.1.2.13; 2604.
DR UniPathway; UPA00109; UER00183.
DR EvolutionaryTrace; P56109; -.
DR PRO; PR:P56109; -.
DR Proteomes; UP000000429; 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:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; 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; IPR011289; Fruc_bis_ald_class-2.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01859; fruc_bis_ald; 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..307
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000178717"
FT ACT_SITE 82
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 211..213
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 253..256
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:5UCS"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:5UCS"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:5UCS"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:5UCS"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:5UCS"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:5UCS"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:5UCS"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:5UCS"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:5UCS"
FT HELIX 110..126
FT /evidence="ECO:0007829|PDB:5UCS"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:5UCS"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:5UCS"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:5UCS"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:5UCS"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:5UD3"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:5UCS"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:5UCS"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:5UCS"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:5UCS"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:5UCS"
FT HELIX 256..272
FT /evidence="ECO:0007829|PDB:5UCS"
FT HELIX 279..301
FT /evidence="ECO:0007829|PDB:5UCS"
SQ SEQUENCE 307 AA; 33773 MW; ADC5696C67C69A45 CRC64;
MLVKGNEILL KAHKEGYGVG AFNFVNFEML NAIFEAGNEE NSPLFIQTSE GAIKYMGIDM
AVGMVKTMCE RYPHIPVALH LDHGTTFESC EKAVKAGFTS VMIDASHHAF EENLELTSKV
VKMAHNAGVS VEAELGRLMG IEDNISVDEK DAVLVNPKEA EQFVKESQVD YLAPAIGTSH
GAFKFKGEPK LDFERLQEVK RLTNIPLVLH GASAIPDNVR KSYLDAGGDL KGSKGVPFEF
LQESVKGGIN KVNTDTDLRI AFIAEVRKVA NEDKSQFDLR KFFSPAQLAL KNVVKERMKL
LGSANKI
