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FBSB_PROMM
ID   FBSB_PROMM              Reviewed;         334 AA.
AC   Q7V808;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=PMT_0568;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(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; BX548175; CAE20743.1; -; Genomic_DNA.
DR   RefSeq; WP_011129947.1; NC_005071.1.
DR   AlphaFoldDB; Q7V808; -.
DR   SMR; Q7V808; -.
DR   STRING; 74547.PMT_0568; -.
DR   EnsemblBacteria; CAE20743; CAE20743; PMT_0568.
DR   KEGG; pmt:PMT_0568; -.
DR   eggNOG; COG1494; Bacteria.
DR   HOGENOM; CLU_054938_0_0_3; -.
DR   OMA; AVFYMDK; -.
DR   OrthoDB; 879338at2; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000001423; 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_0000342719"
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;  35083 MW;  2F4442DC6DA7A336 CRC64;
     MDRTLIQEIL EVVEQAAIAS AHLTGLGKKD EADAAAVEAM RKRMGQIQMQ GRIVIGEGER
     DEAPMLYIGE EVGSGSGPGV DFAVDPCEGT NLCANNQRGS MAVLAASDRG GLFNAPDFYM
     KKLAAPPSAK GKVDIRKSAT ENINILSQCL GLAVSELTIV VMDRARHKGL ISEIRATGAR
     VQPISDGDVQ AAIACGFAGT GTHCLMGIGA APEGVISAAA MRALGGHFQG QLVYDPAIAQ
     TSEWADYTKE GNIARLNEMG ITDVDKIYEA EELASGKNVV FAGSGITDGL LFHGVKFEPD
     CTRTSSLVIS TLDNTARFTN TVHIKDGAKS IALS
 
 
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