ID   GLPX_ECOL6              Reviewed;         336 AA.
AC   P0A9D0; P11007; P28860; P28900;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Fructose-1,6-bisphosphatase class 2;
DE            Short=FBPase class 2;
DE            EC=3.1.3.11;
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 2;
GN   Name=glpX; OrderedLocusNames=c4877;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC       fructose 6-phosphate. {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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FBPase class 2 family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN83305.1; -; Genomic_DNA.
DR   RefSeq; WP_001250644.1; NC_004431.1.
DR   AlphaFoldDB; P0A9D0; -.
DR   SMR; P0A9D0; -.
DR   STRING; 199310.c4877; -.
DR   EnsemblBacteria; AAN83305; AAN83305; c4877.
DR   GeneID; 67417564; -.
DR   KEGG; ecc:c4877; -.
DR   eggNOG; COG1494; Bacteria.
DR   HOGENOM; CLU_054938_0_0_6; -.
DR   OMA; AVFYMDK; -.
DR   BioCyc; ECOL199310:C4877-MON; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
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   Carbohydrate metabolism; Cytoplasm; Hydrolase; Manganese; Metal-binding.
FT   CHAIN           1..336
FT                   /note="Fructose-1,6-bisphosphatase class 2"
FT                   /id="PRO_0000201101"
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         210
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   336 AA;  35852 MW;  DEC2A477E5C4062E CRC64;
     MRRELAIEFS RVTESAALAG YKWLGRGDKN TADGAAVNAM RIMLNQVNID GTIVIGEGEI
     DEAPMLYIGE KVGTGRGDAV DIAVDPIEGT RMTAMGQANA LAVLAVGDKG CFLNAPDMYM
     EKLIVGPGAK GTIDLNLPLA DNLRNVAAAL GKPLSELTVT ILAKPRHDAV IAEMQQLGVR
     VFAIPDGDVA ASILTCMPDS EVDVLYGIGG APEGVVSAAV IRALDGDMNG RLLARHDVKG
     DNEENRRIGE QELARCKAMG IEAGKVLRLG DMARSDNVIF SATGITKGDL LEGISRKGNI
     ATTETLLIRG KSRTIRRIQS IHYLDRKDPE MQVHIL