ALF2_CUPNH
ID ALF2_CUPNH Reviewed; 345 AA.
AC Q59101; Q7WWS6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Fructose-bisphosphate aldolase, plasmid;
DE Short=FBP aldolase;
DE Short=FBPA;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase;
GN Name=cbbAP; OrderedLocusNames=PHG416;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
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=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
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; U12423; AAC43448.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP86165.1; -; Genomic_DNA.
DR PIR; I39555; I39555.
DR RefSeq; WP_011154328.1; NZ_CP039289.1.
DR AlphaFoldDB; Q59101; -.
DR SMR; Q59101; -.
DR STRING; 381666.PHG416; -.
DR EnsemblBacteria; AAP86165; AAP86165; PHG416.
DR GeneID; 39976443; -.
DR KEGG; reh:PHG416; -.
DR PATRIC; fig|381666.6.peg.344; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_040088_0_0_4; -.
DR OMA; EWQMDVC; -.
DR OrthoDB; 827430at2; -.
DR UniPathway; UPA00109; UER00183.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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; Plasmid;
KW Reference proteome; Zinc.
FT CHAIN 1..345
FT /note="Fructose-bisphosphate aldolase, plasmid"
FT /id="PRO_0000178728"
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 285
FT /note="T -> I (in Ref. 1; AAC43448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 37412 MW; B5E2CBB6200388B7 CRC64;
MALISLRQLL DHAGEFGYGV PAFNVNNLEQ IHAIMEAAEE TDSPVILQAS AGARKYAGEA
YLRHMVLAAA ETHPDIPIVL HQDHGSSPAV CQASIRSGFT SVMMDGSLRE DMKTPSDYDY
NVDVTRRVCE MAHAVGVSVE GELGCLGSLE TGQAGEEDGV GAAGTLSHDM MLTDPAQARD
FVARTGVDAL AIAIGTSHGA YKFSRKPTGD ILAIDRIREI HEQIPDTHLV MHGSSSVPQE
WLEIIRQYGG DIKETYGVPV EEILRGIKTG VRKVNIDTDI RLAMTGAIRK SLAEDRSEFD
PRKALLAAKK GARSVVKLRF EAFGCAGQAS KIKPIAMEQL AQWYR
