F16PA_SYNE7
ID F16PA_SYNE7 Reviewed; 344 AA.
AC Q59943; P96146; Q31KQ4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Fructose-1,6-bisphosphatase class 1;
DE Short=FBPase class 1;
DE EC=3.1.3.11;
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1;
DE AltName: Full=Fructose-1,6-bisphosphatase F-II;
GN Name=fbp; OrderedLocusNames=Synpcc7942_2335;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8566707; DOI=10.1111/j.1574-6968.1995.tb07882.x;
RA Newman J., Karakaya H., Scanlan D.J., Mann N.H.;
RT "A comparison of gene organization in the zwf region of the genomes of the
RT cyanobacteria Synechococcus sp. PCC 7942 and Anabaena sp. PCC 7120.";
RL FEMS Microbiol. Lett. 133:187-193(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, ACTIVITY REGULATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8837735; DOI=10.1006/abbi.1996.0425;
RA Tamoi M., Ishikawa T., Takeda T., Shigeoka S.;
RT "Molecular characterization and resistance to hydrogen peroxide of two
RT fructose-1,6-bisphosphatases from Synechococcus PCC 7942.";
RL Arch. Biochem. Biophys. 334:27-36(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes only the formation of fructose 6-phosphate by
CC hydrolysis of fructose 1,6-bisphosphate. {ECO:0000269|PubMed:8837735}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Not inhibited by AMP and slightly innibited by
CC hydrogen peroxyde. {ECO:0000269|PubMed:8837735}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for fructose 1,6-bisphosphate (at pH 8)
CC {ECO:0000269|PubMed:8837735};
CC pH dependence:
CC Optimum pH is 9. Activities at pH 8.0 and 9.5 were approx 67% and
CC 85%, respectively, of that at pH 9.0. {ECO:0000269|PubMed:8837735};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8837735}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
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DR EMBL; U33285; AAA98846.1; -; Genomic_DNA.
DR EMBL; D49680; BAA08536.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58365.1; -; Genomic_DNA.
DR RefSeq; WP_011378409.1; NC_007604.1.
DR AlphaFoldDB; Q59943; -.
DR SMR; Q59943; -.
DR STRING; 1140.Synpcc7942_2335; -.
DR PRIDE; Q59943; -.
DR EnsemblBacteria; ABB58365; ABB58365; Synpcc7942_2335.
DR KEGG; syf:Synpcc7942_2335; -.
DR eggNOG; COG0158; Bacteria.
DR HOGENOM; CLU_039977_2_2_3; -.
DR OMA; YIPENCP; -.
DR OrthoDB; 945770at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2335-MON; -.
DR BRENDA; 3.1.3.11; 325.
DR UniPathway; UPA00116; -.
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-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 1: Evidence at protein level;
KW Calvin cycle; Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding.
FT CHAIN 1..344
FT /note="Fructose-1,6-bisphosphatase class 1"
FT /id="PRO_0000200489"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 29
FT /note="L -> F (in Ref. 2; BAA08536)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="V -> S (in Ref. 2; BAA08536)"
FT /evidence="ECO:0000305"
FT CONFLICT 229..250
FT /note="WQWPEGYRQYIREMHRREGYSG -> CSGPKVSPVHPGNASPRRLQR (in
FT Ref. 2; BAA08536)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="G -> A (in Ref. 1; AAA98846)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="A -> P (in Ref. 2; BAA08536)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="E -> R (in Ref. 2; BAA08536)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..344
FT /note="EACLAESVP -> DSLLG (in Ref. 2; BAA08536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38172 MW; E4E6EEC414A6BA79 CRC64;
MAQSTTSETH TRDLDRDCTT LSRHVLEQLQ SFSPEAQDLA ALMQRIGLAA KLIARRLSHA
GLVDDALGFT GEINVQGEAV KRMDVYANQV FISVFRQSGL VCRLASEEME KPYYIPENCP
IGRYTLLYDP LDGSANVDVD LNVGSIFAVR RQEFYDESHE AKDLLQPGDR QIAAGYVLYG
ASTLLVYSMG QGVHVFVLDP SLGEFVLAQS DIQLPNSGQI YSVNEGNFWQ WPEGYRQYIR
EMHRREGYSG RYSGALVADF HRILMQGGVF LYPETVKNPT GKLRLLYEAA PMAFLAEQAG
GKASDGQKPI LLRQPQALHE RCPLIIGSAA DVDFVEACLA ESVP
