FBSB_SYNE7
ID FBSB_SYNE7 Reviewed; 345 AA.
AC Q31QY2; P96145;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase;
DE Short=FBPase class 2/SBPase;
DE EC=3.1.3.11;
DE EC=3.1.3.37;
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 2;
DE AltName: Full=Fructose-1,6-bisphosphatase F-I;
GN OrderedLocusNames=Synpcc7942_0505;
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], PROTEIN SEQUENCE OF 1-24, FUNCTION,
RP SUBUNIT, ACTIVITY REGULATION, 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 [2]
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 the hydrolysis of fructose 1,6-bisphosphate (Fru
CC 1,6-P2) and sedoheptulose 1,7-bisphosphate (Sed 1,7-P2) to fructose 6-
CC phosphate and sedoheptulose 7-phosphate, respectively.
CC {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 -!- CATALYTIC ACTIVITY:
CC Reaction=D-sedoheptulose 1,7-bisphosphate + H2O = D-sedoheptulose 7-
CC phosphate + phosphate; Xref=Rhea:RHEA:17461, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57483, ChEBI:CHEBI:58335; EC=3.1.3.37;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by AMP and slightly innibited by
CC hydrogen peroxyde. {ECO:0000269|PubMed:8837735}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=52 uM for fructose-1,6-bisphosphate (at pH 8)
CC {ECO:0000269|PubMed:8837735};
CC KM=118 uM for sedoheptulose 1,7-bisphosphate (at pH 8)
CC {ECO:0000269|PubMed:8837735};
CC Vmax=11.7 umol/min/mg enzyme with fructose 1,6-bisphosphate as
CC substrate (at pH 8) {ECO:0000269|PubMed:8837735};
CC Vmax=12.1 umol/min/mg enzyme with sedoheptulose 1,7-bisphosphate as
CC substrate (at pH 8) {ECO:0000269|PubMed:8837735};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8837735}.
CC -!- SIMILARITY: Belongs to the FBPase class 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11934.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA11934.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D83512; BAA11934.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP000100; ABB56537.1; -; Genomic_DNA.
DR RefSeq; WP_011243327.1; NC_007604.1.
DR AlphaFoldDB; Q31QY2; -.
DR SMR; Q31QY2; -.
DR STRING; 1140.Synpcc7942_0505; -.
DR PRIDE; Q31QY2; -.
DR EnsemblBacteria; ABB56537; ABB56537; Synpcc7942_0505.
DR KEGG; syf:Synpcc7942_0505; -.
DR eggNOG; COG1494; Bacteria.
DR HOGENOM; CLU_054938_0_0_3; -.
DR OMA; AVFYMDK; -.
DR OrthoDB; 879338at2; -.
DR BioCyc; SYNEL:SYNPCC7942_0505-MON; -.
DR BRENDA; 3.1.3.11; 7781.
DR BRENDA; 3.1.3.37; 7781.
DR UniPathway; UPA00116; -.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050278; F:sedoheptulose-bisphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01516; FBPase_glpX; 1.
DR InterPro; IPR004464; FBPase_class-2/SBPase.
DR PANTHER; PTHR30447; PTHR30447; 1.
DR Pfam; PF03320; FBPase_glpX; 1.
DR PIRSF; PIRSF004532; GlpX; 1.
DR TIGRFAMs; TIGR00330; glpX; 1.
PE 1: Evidence at protein level;
KW Calvin cycle; Carbohydrate metabolism; Direct protein sequencing;
KW Hydrolase; Manganese; Metal-binding.
FT CHAIN 1..345
FT /note="D-fructose 1,6-bisphosphatase class 2/sedoheptulose
FT 1,7-bisphosphatase"
FT /id="PRO_0000342732"
FT BINDING 33
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 100..102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176..178
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198..200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 345 AA; 36966 MW; 51985911DE01A5E8 CRC64;
MEKTIGLEII EVVEQAAIAS ARLMGKGEKN EADRVAVEAM RVRMNQVEML GRIVIGEGER
DEAPMLYIGE EVGIYRDADK RAGVPAGKLV EIDIAVDPCE GTNLCAYGQP GSMAVLAISE
KGGLFAAPDF YMKKLAAPPA AKGKVDINKS ATENLKILSE CLDRAIDELV VVVMDRPRHK
ELIQEIRQAG ARVRLISDGD VSAAISCGFA GTNTHALMGI GAAPEGVISA AAMRCLGGHF
QGQLIYDPEV VKTGLIGESR ESNIARLQEM GITDPDRVYD ANELASGQEV LFAACGITPG
LLMEGVRFFK GGARTQSLVI SSQSRTARFV DTVHMFDDVK TVSLR
