F16A2_CUPNH
ID F16A2_CUPNH Reviewed; 364 AA.
AC P19911; Q0K1E5;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Fructose-1,6-bisphosphatase class 1 2 {ECO:0000255|HAMAP-Rule:MF_01855};
DE Short=FBPase class 1 2 {ECO:0000255|HAMAP-Rule:MF_01855};
DE EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01855};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 2 {ECO:0000255|HAMAP-Rule:MF_01855};
GN Name=fbp2 {ECO:0000255|HAMAP-Rule:MF_01855}; Synonyms=cbbF2, cbbFC, cfxF;
GN OrderedLocusNames=H16_B1390;
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=7767230; DOI=10.1007/bf00294635;
RA Yoo J.-G., Bowien B.;
RT "Analysis of the cbbF genes from Alcaligenes eutrophus that encode
RT fructose-1,6-/sedoheptulose-1,7-bisphosphatase.";
RL Curr. Microbiol. 31:55-61(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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-364.
RX PubMed=2559876; DOI=10.1016/0378-1119(89)90490-3;
RA Kossmann J., Klintworth R., Bowien B.;
RT "Sequence analysis of the chromosomal and plasmid genes encoding
RT phosphoribulokinase from Alcaligenes eutrophus.";
RL Gene 85:247-252(1989).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01855};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01855};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01855};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000255|HAMAP-
CC Rule:MF_01855}.
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DR EMBL; U16791; AAA69975.1; -; Genomic_DNA.
DR EMBL; AM260480; CAJ96179.1; -; Genomic_DNA.
DR EMBL; M33563; AAA21958.1; -; Genomic_DNA.
DR PIR; I39556; I39556.
DR RefSeq; WP_011617202.1; NZ_CP039288.1.
DR AlphaFoldDB; P19911; -.
DR SMR; P19911; -.
DR STRING; 381666.H16_B1390; -.
DR PRIDE; P19911; -.
DR EnsemblBacteria; CAJ96179; CAJ96179; H16_B1390.
DR GeneID; 57647288; -.
DR KEGG; reh:H16_B1390; -.
DR eggNOG; COG0158; Bacteria.
DR HOGENOM; CLU_039977_0_0_4; -.
DR OMA; NSRFWEP; -.
DR OrthoDB; 945770at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008210; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR CDD; cd00354; FBPase; 1.
DR HAMAP; MF_01855; FBPase_class1; 1.
DR InterPro; IPR044015; FBPase_C_dom.
DR InterPro; IPR000146; FBPase_class-1.
DR InterPro; IPR033391; FBPase_N.
DR InterPro; IPR028343; FBPtase.
DR InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR PANTHER; PTHR11556; PTHR11556; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00115; F16BPHPHTASE.
DR PROSITE; PS00124; FBPASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..364
FT /note="Fructose-1,6-bisphosphatase class 1 2"
FT /id="PRO_0000200479"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 125
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 126..129
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
SQ SEQUENCE 364 AA; 39607 MW; 0BD30D7CBBCDCC23 CRC64;
MPEVQRMTLT QFLIEERRRY PDASGGFNGL ILNVAMACKE IARAVAFGAL GGLHGKASNQ
AGEAGAVNVQ GEIQQKLDVL SNTTFLRVNE WGGYLAGMAS EEMEAPYQIP DHYPRGKYLL
VFDPLDGSSN IDVNVSVGSI FSVLRAPEGA SAVTEQDFLQ PGSAQVAAGY ALYGPTTMLV
LTVGNGVNGF TLDPNLGEFF LTHPNLQVPA DTQEFAINAS NSRFWEAPVQ RYIAECMAGK
SGPRGKDFNM RWIASMVAEA HRILMRGGVF MYPRDSKDPA KPGRLRLLYE ANPIAFLMEQ
AGGRASTGRQ TLMSVAPGAL HQRIGVIFGS RNEVERIEGY HTDQTDPDLP SPLFNERSLF
RASA
