GLPX_SHIFL
ID GLPX_SHIFL Reviewed; 336 AA.
AC P0A9D1; 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 113.
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=SF4003, S3744;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M4232;
RX PubMed=1400248; DOI=10.1128/jb.174.21.6981-6991.1992;
RA Truniger V., Boos W., Sweet G.;
RT "Molecular analysis of the glpFKX regions of Escherichia coli and Shigella
RT flexneri.";
RL J. Bacteriol. 174:6981-6991(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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:0000305}.
CC -!- SIMILARITY: Belongs to the FBPase class 2 family. {ECO:0000305}.
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DR EMBL; Z11766; CAA77812.1; -; Genomic_DNA.
DR EMBL; AE005674; AAN45436.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18764.1; -; Genomic_DNA.
DR PIR; S23905; S23905.
DR RefSeq; NP_709729.1; NC_004337.2.
DR RefSeq; WP_001250644.1; NZ_WPGW01000012.1.
DR AlphaFoldDB; P0A9D1; -.
DR SMR; P0A9D1; -.
DR STRING; 198214.SF4003; -.
DR EnsemblBacteria; AAN45436; AAN45436; SF4003.
DR EnsemblBacteria; AAP18764; AAP18764; S3744.
DR GeneID; 1027784; -.
DR GeneID; 67417564; -.
DR KEGG; sfl:SF4003; -.
DR KEGG; sfx:S3744; -.
DR PATRIC; fig|198214.7.peg.4717; -.
DR HOGENOM; CLU_054938_0_0_6; -.
DR OMA; AVFYMDK; -.
DR OrthoDB; 879338at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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;
KW Reference proteome.
FT CHAIN 1..336
FT /note="Fructose-1,6-bisphosphatase class 2"
FT /id="PRO_0000201103"
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"
FT CONFLICT 215
FT /note="V -> G (in Ref. 1; CAA77812)"
FT /evidence="ECO:0000305"
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
