ALF1_CUPNH
ID ALF1_CUPNH Reviewed; 345 AA.
AC Q59100; Q0K1F1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Fructose-bisphosphate aldolase, chromosomal;
DE Short=FBP aldolase;
DE Short=FBPA;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase;
GN Name=cbbAC; Synonyms=cbbA2; OrderedLocusNames=H16_B1384;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7763137; DOI=10.1007/bf00393383;
RA Schaeferfohann J., Yoo J.-G., Bowien B.;
RT "Analysis of the genes forming the distal parts of the two cbb CO2 fixation
RT operons from Alcaligenes eutrophus.";
RL Arch. Microbiol. 163:291-299(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; U12422; AAC43445.1; -; Genomic_DNA.
DR EMBL; AM260480; CAJ96173.1; -; Genomic_DNA.
DR PIR; I39552; I39552.
DR RefSeq; WP_010809300.1; NZ_CP039288.1.
DR AlphaFoldDB; Q59100; -.
DR SMR; Q59100; -.
DR STRING; 381666.H16_B1384; -.
DR PRIDE; Q59100; -.
DR EnsemblBacteria; CAJ96173; CAJ96173; H16_B1384.
DR GeneID; 57647282; -.
DR KEGG; reh:H16_B1384; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_040088_0_0_4; -.
DR OMA; TVGGMED; -.
DR OrthoDB; 827430at2; -.
DR UniPathway; UPA00109; UER00183.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000008210; Chromosome 2.
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; Reference proteome; Zinc.
FT CHAIN 1..345
FT /note="Fructose-bisphosphate aldolase, chromosomal"
FT /id="PRO_0000178727"
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"
FT CONFLICT 19
FT /note="G -> D (in Ref. 1; AAC43445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 37397 MW; DABCBE4C408F2B4B CRC64;
MALISLRQLL DHAGEFGYGV PAFNVNNLEQ IHAIMEAAQE TDSPVILQAS AGARKYAGEA
YLRHMVLAAA ETHPDIPIVL HQDHGSSPAI CQASIRSGFT SVMMDGSLRE DMKTPSDYDY
NVEVTRRVCE MAHAIGVSVE GELGCLGSLE TGQAGEEDGV GAAGTLSHDM MLTDPAQARD
FVARTGVDAL AIAIGTSHGA YKFSRKPTGD ILAMDRIREI HEQIPDTHLV MHGSSSVPQE
WLEIIRQYGG DIKETYGVPV EEILRGIKMG VRKVNIDTDI RLAMTGAIRK SLSDDRSEFD
PRKALLAAKK GARSVVKLRF EAFGCAGQAS RIKPVPLERV AKLYS
