FBSB_GLOVI
ID FBSB_GLOVI Reviewed; 346 AA.
AC Q7NG31;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=glr3342;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(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; BA000045; BAC91283.1; -; Genomic_DNA.
DR RefSeq; NP_926288.1; NC_005125.1.
DR RefSeq; WP_011143332.1; NC_005125.1.
DR AlphaFoldDB; Q7NG31; -.
DR SMR; Q7NG31; -.
DR STRING; 251221.35213913; -.
DR EnsemblBacteria; BAC91283; BAC91283; BAC91283.
DR KEGG; gvi:glr3342; -.
DR PATRIC; fig|251221.4.peg.3373; -.
DR eggNOG; COG1494; Bacteria.
DR HOGENOM; CLU_054938_0_0_3; -.
DR InParanoid; Q7NG31; -.
DR OMA; AVFYMDK; -.
DR OrthoDB; 879338at2; -.
DR PhylomeDB; Q7NG31; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IBA:GO_Central.
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:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
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"
FT /id="PRO_0000342711"
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; 37030 MW; 6E6D758437BF68CD CRC64;
MEKTLGLEII EVVEQAAIAS ARLMGKGLRN EADGVAVKAM RDRMNQIYMR GRIVIGEGER
DDAPMLYIGE QVGICTQPNA AQMCSIDELL EIDIAVDPCE GTNLVAEGRQ GSMAVLAISE
KGGLLGAPDL YMKKLAAPPQ AKGKVHIDYP ATKNLQIIAE CLDRAIEDLV VIVMKRDRHK
DLISEIRSTG ARVRFIDDGD ISAALSAGIN GTGVHALMGI GAAPEGVISA AALRCLGSHF
QGQLIYDPDV VQTGLLKGTK AEIEEQLKAQ GVEQPDKVWE AEELASGKNV LFAACGITDG
DFIKGVRFFT GSARTETMVI SSQSNTVRFV DTVHILDPAH HASLVI
