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FBSB_PROM9
ID   FBSB_PROM9              Reviewed;         333 AA.
AC   Q31BB0;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 80.
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;
GN   OrderedLocusNames=PMT9312_0775;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
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., Thiel J., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL   Submitted (JUL-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. {ECO:0000250}.
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   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FBPase class 2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB49835.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000111; ABB49835.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_025926367.1; NC_007577.1.
DR   AlphaFoldDB; Q31BB0; -.
DR   SMR; Q31BB0; -.
DR   STRING; 74546.PMT9312_0775; -.
DR   EnsemblBacteria; ABB49835; ABB49835; PMT9312_0775.
DR   KEGG; pmi:PMT9312_0775; -.
DR   eggNOG; COG1494; Bacteria.
DR   HOGENOM; CLU_054938_0_0_3; -.
DR   OrthoDB; 879338at2; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000002715; Chromosome.
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   3: Inferred from homology;
KW   Calvin cycle; Carbohydrate metabolism; Hydrolase; Manganese; Metal-binding.
FT   CHAIN           1..333
FT                   /note="D-fructose 1,6-bisphosphatase class 2/sedoheptulose
FT                   1,7-bisphosphatase"
FT                   /id="PRO_0000342718"
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         85
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         88..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164..166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         186..188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  35090 MW;  8EABBE4129802686 CRC64;
     MNQTLIQEIL EVVEQAAIAS AKLTGLGQKD EADAAAVEAM RLRMGKIEMK GKIVIGEGER
     DEAPMLYIGE EVGSGSGPGV DFAVDPCEGT NLCANNQRGS MAVLAASDTG GLFNAPDFYM
     NKLAAPPAAK GKVDIRNSAT ENLKILSDCL DLSIDELTVV VMDRTRHKDL IKEIRGCGAK
     VQPISDGDVQ AAIACGFAGT GTHCLMGIGA APEGVISAAA MRALGGHFQG QLVYDPAIAQ
     TSEWADYTKE GNIKRLNEMG ITDIDKIYEA NELASGENVV FAGSGITDGL LFDGVKFERD
     CVRTSSLVIS TLDSTARFTN TVHIKDGAKS ISL
 
 
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