ID   FBSB_NOSS1              Reviewed;         345 AA.
AC   Q8YY12;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, 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=alr1041;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB72998.1; -; Genomic_DNA.
DR   PIR; AF1936; AF1936.
DR   RefSeq; WP_010995215.1; NZ_RSCN01000025.1.
DR   AlphaFoldDB; Q8YY12; -.
DR   SMR; Q8YY12; -.
DR   STRING; 103690.17130387; -.
DR   EnsemblBacteria; BAB72998; BAB72998; BAB72998.
DR   KEGG; ana:alr1041; -.
DR   eggNOG; COG1494; Bacteria.
DR   OMA; AVFYMDK; -.
DR   OrthoDB; 879338at2; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000002483; 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..345
FT                   /note="D-fructose 1,6-bisphosphatase class 2/sedoheptulose
FT                   1,7-bisphosphatase"
FT                   /id="PRO_0000342708"
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;  36737 MW;  E8F4B4CE7ED291EF CRC64;
     MENTLGLEII EVVEQAAIAS AKWMGKGEKN TADQVAVEAM RERMNKIYMR GRIVIGEGER
     DDAPMLYIGE EVGICTQPNA DQLCNPDELV EIDIAVDPCE GTNLVAYGQP GSMAVLAISE
     KGGLFAAPDF YMKKLAAPPA AKGKVDINKS ATENLKILSE CLDRSIDELV VVVMKRDRHQ
     GLIKEIRDAG ARVQLISDGD VGAAISCGFA GTNVHALMGI GAAPEGVISA AAMRALGGHF
     QGQLIYDPEV VKTGLIGESK QANLDRLSSM GINDPDKVYD AHELASGENV LFAGCGITSG
     NLMQGVRFFH GGARTQSLVI SSQSQTARFV DTIHMAGQPK TVQLH