F16A2_CERS4
ID F16A2_CERS4 Reviewed; 331 AA.
AC Q3IX60;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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}; OrderedLocusNames=RHOS4_33060;
GN ORFNames=RSP_3266;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; Calvin cycle. {ECO:0000255|HAMAP-
CC 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; CP000144; ABA80874.1; -; Genomic_DNA.
DR RefSeq; WP_011339166.1; NZ_CP030272.1.
DR RefSeq; YP_354775.1; NC_007494.2.
DR AlphaFoldDB; Q3IX60; -.
DR SMR; Q3IX60; -.
DR STRING; 272943.RSP_3266; -.
DR EnsemblBacteria; ABA80874; ABA80874; RSP_3266.
DR KEGG; rsp:RSP_3266; -.
DR PATRIC; fig|272943.9.peg.3693; -.
DR eggNOG; COG0158; Bacteria.
DR OMA; NSRFWEP; -.
DR PhylomeDB; Q3IX60; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000002703; 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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
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 Calvin cycle; Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..331
FT /note="Fructose-1,6-bisphosphatase class 1 2"
FT /id="PRO_0000364667"
FT BINDING 80
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 101..104
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 261
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
SQ SEQUENCE 331 AA; 35256 MW; 500EB63E9BBECD13 CRC64;
MAIELEDLGL SPDVADVMQR LARVGAGIAR IISRNGLERD LGAGVGTNAG GDGQKALDVI
ADDAFRAALE GSAVAYYASE EQDEVVTLGE GSLALAIDPL DGSSNIDVNV SIGTIFSIFP
AAAGPEASFL RPGTEQIAGG YIIYGPQCAL VCSFGQGVQH WVLDLDAGIF RRMPDIRPLP
AETSEFAINA SNYRHWPQPI RAFVDDLVAG AEGPRGKNFN MRWIASLVAE THRILMRGGV
FLYPGDERKG YERGRLRHVY ECAPIAFLIA NVGGGATDGC ADILTALPDR LHARTPFVFG
CASKVARVAA YHDLACEETS ALFGSRGLFR S
