FBSB_PROMP
ID FBSB_PROMP Reviewed; 333 AA.
AC Q7V1T8;
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=PMM0767;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
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; BX548174; CAE19226.1; -; Genomic_DNA.
DR RefSeq; WP_011132401.1; NC_005072.1.
DR AlphaFoldDB; Q7V1T8; -.
DR SMR; Q7V1T8; -.
DR STRING; 59919.PMM0767; -.
DR EnsemblBacteria; CAE19226; CAE19226; PMM0767.
DR KEGG; pmm:PMM0767; -.
DR eggNOG; COG1494; Bacteria.
DR HOGENOM; CLU_054938_0_0_3; -.
DR OMA; AVFYMDK; -.
DR OrthoDB; 879338at2; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000001026; 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_0000342723"
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; 35150 MW; 1D6CA247CABCE8F2 CRC64;
MNQTLIQEIL EVVEQAAIAS AKLTGLGQKD EADAAAVEAM RLRMGKIEMK GKIVIGEGER
DEAPMLYIGE EVGSGNGPGV DFAVDPCEGT NLCANNQRGS MAVLAASDTG GLFNAPDFYM
NKLAAPPAAK GKVDIRNSAT ENLKILSNCL DLAIDELTVV VMDRARHKGL IKEIRECGAK
IQPISDGDVQ AAIACGFAGT GTHCLMGIGA APEGVISAAA MRALGGHFQG QLVYDPAIAQ
TSEWADYTKE GNIKRLNEMG ITDIDKIYEA NELASGENVI FAGSGITDGL LFDGVKFEKD
CTRTSSLVIS TLDSTCRFTN TIHMKDGAKS ISL
