F16A3_CUPNH
ID F16A3_CUPNH Reviewed; 364 AA.
AC P19912;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Fructose-1,6-bisphosphatase class 1 3 {ECO:0000255|HAMAP-Rule:MF_01855};
DE Short=FBPase class 1 3 {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 3 {ECO:0000255|HAMAP-Rule:MF_01855};
GN Name=fbp3 {ECO:0000255|HAMAP-Rule:MF_01855}; Synonyms=cbbFP, cfxF;
GN OrderedLocusNames=PHG422;
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=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=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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 159-364.
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; U16792; AAA69974.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP86171.1; -; Genomic_DNA.
DR EMBL; M33562; AAA21956.1; -; Genomic_DNA.
DR PIR; I39525; I39525.
DR RefSeq; WP_011154334.1; NZ_CP039289.1.
DR AlphaFoldDB; P19912; -.
DR SMR; P19912; -.
DR STRING; 381666.PHG422; -.
DR PRIDE; P19912; -.
DR EnsemblBacteria; AAP86171; AAP86171; PHG422.
DR GeneID; 39976732; -.
DR KEGG; reh:PHG422; -.
DR PATRIC; fig|381666.6.peg.350; -.
DR eggNOG; COG0158; Bacteria.
DR HOGENOM; CLU_039977_0_0_4; -.
DR OMA; HEKSECY; -.
DR OrthoDB; 945770at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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 Plasmid; Reference proteome.
FT CHAIN 1..364
FT /note="Fructose-1,6-bisphosphatase class 1 3"
FT /id="PRO_0000200480"
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; 39777 MW; D0F8DB93A6DD0FF1 CRC64;
MPEVQRMTLT QFLIEERRRY PDASGGFNGL ILNVAMACKE IARAVAFGAL GGLHGKASTQ
AGEEGAVNVQ GEIQQKLDVL SNTTFLRVNE WGGYLAGMAS EEMEAPYQIP ENYPRGKYLL
VFDPLDGSSN IDVNVSVGSI FSVLRAPEGA DTVTEQDFLQ PGSAQVAAGY ALYGPTTMLV
LTVGNGVNGF TLDPNLGEFF LTHPHLRVPP DTQEFAINAS NSRFWEAPVQ RYIGECMAGK
SGPRGKDFNM RWIASMVAEA HRILMRGGVF MYPRDTKDPA KPGRLRLLYE ANPIAFLMEQ
AGGRASTGRQ TLMSVAPGAL HQRIGVIFGS RNEVERIEGY HTNQTDPDLP SPLFNERSLF
RASA
