FBSB_PROMA
ID FBSB_PROMA Reviewed; 334 AA.
AC Q7TVA4;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Pro_0840;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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}.
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DR EMBL; AE017126; AAP99884.1; -; Genomic_DNA.
DR RefSeq; NP_875232.1; NC_005042.1.
DR RefSeq; WP_011124992.1; NC_005042.1.
DR AlphaFoldDB; Q7TVA4; -.
DR SMR; Q7TVA4; -.
DR STRING; 167539.Pro_0840; -.
DR EnsemblBacteria; AAP99884; AAP99884; Pro_0840.
DR GeneID; 54200186; -.
DR KEGG; pma:Pro_0840; -.
DR PATRIC; fig|167539.5.peg.888; -.
DR eggNOG; COG1494; Bacteria.
DR HOGENOM; CLU_054938_0_0_3; -.
DR OMA; AVFYMDK; -.
DR OrthoDB; 879338at2; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000001420; 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;
KW Reference proteome.
FT CHAIN 1..334
FT /note="D-fructose 1,6-bisphosphatase class 2/sedoheptulose
FT 1,7-bisphosphatase"
FT /id="PRO_0000342713"
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 334 AA; 35039 MW; 476812AD22A15F0C CRC64;
MDRTLIQEIL EVVEQAAIAS AELTGLGQKD EADAAAVEAM RKRMGSIQMQ GRIVIGEGER
DEAPMLYIGE EVGSGSGPGV DFAVDPCEGT NLCANNQRGS MAVLAASDRG GLFNAPDFYM
KKLAAPPAAK GKVDIRKSAT ENINILSSCL GMAVSELTIV VMDRARHKDL IAEIRSTGAR
VQPISDGDVQ AAIACGFAGT GTHCLMGIGA APEGVISAAA MRALGGHFQG QLVYDPAIAM
TKEWADYTKE GNIARLNEMG ITDGDKIYEA DELASGENVV FAGSGITDGL LFNGVKFEKD
CTRTSSLVIS TLDSTARFTN TVHIKDGAKS ISLS
