FBSB1_ACAM1
ID FBSB1_ACAM1 Reviewed; 346 AA.
AC B0C1Z3;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase 1;
DE Short=FBPase class 2/SBPase 1;
DE EC=3.1.3.11;
DE EC=3.1.3.37;
GN OrderedLocusNames=AM1_2283;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW27294.1; -; Genomic_DNA.
DR RefSeq; WP_012162769.1; NC_009925.1.
DR AlphaFoldDB; B0C1Z3; -.
DR SMR; B0C1Z3; -.
DR STRING; 329726.AM1_2283; -.
DR EnsemblBacteria; ABW27294; ABW27294; AM1_2283.
DR KEGG; amr:AM1_2283; -.
DR eggNOG; COG1494; Bacteria.
DR HOGENOM; CLU_054938_0_0_3; -.
DR OrthoDB; 879338at2; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000000268; 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..346
FT /note="D-fructose 1,6-bisphosphatase class 2/sedoheptulose
FT 1,7-bisphosphatase 1"
FT /id="PRO_0000342706"
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 346 AA; 37165 MW; 2F355F46C297FF56 CRC64;
MDNVIGLEII EVVEQAAIAS ALWMGKGEKD TADAVAVDAM RNRMNQIHMR GRIVIGEGER
DDAPMLYIGE QVGICTQENA AEFCTLDELI EIDIAVDPCE GTNLVAYGQN GSMAVLAISE
KGGLFAAPDF YMKKLAAPPA AKGKVDIRKS ATENLQIIAE CLDRSISELV VVVMKRARHD
GLIKEIREAG ARVRLIEDGD VSAALSCAFS GTNIHALMGI GAAPEGVISA AAMRALGGHF
QGQLIYDPEI VQTGLIGESK ESNLARLKEM GIDDPDRIYE AEELACGETV LFAACGITPG
TLMKGARFFP GGVRTESLII STQSKTVRFV DTIHKLDDKH RALQLH
