F16PA_SALTY
ID F16PA_SALTY Reviewed; 332 AA.
AC Q8ZK67;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Fructose-1,6-bisphosphatase class 1 {ECO:0000255|HAMAP-Rule:MF_01855};
DE Short=FBPase class 1 {ECO:0000255|HAMAP-Rule:MF_01855};
DE EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01855};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 {ECO:0000255|HAMAP-Rule:MF_01855};
GN Name=fbp {ECO:0000255|HAMAP-Rule:MF_01855}; OrderedLocusNames=STM4415;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01855};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01855};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01855};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000255|HAMAP-
CC Rule:MF_01855}.
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DR EMBL; AE006468; AAL23235.1; -; Genomic_DNA.
DR RefSeq; NP_463276.1; NC_003197.2.
DR RefSeq; WP_000853764.1; NC_003197.2.
DR AlphaFoldDB; Q8ZK67; -.
DR SMR; Q8ZK67; -.
DR STRING; 99287.STM4415; -.
DR PaxDb; Q8ZK67; -.
DR EnsemblBacteria; AAL23235; AAL23235; STM4415.
DR GeneID; 1255941; -.
DR KEGG; stm:STM4415; -.
DR PATRIC; fig|99287.12.peg.4642; -.
DR HOGENOM; CLU_039977_2_2_6; -.
DR OMA; YIPENCP; -.
DR PhylomeDB; Q8ZK67; -.
DR BioCyc; SENT99287:STM4415-MON; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
DR CDD; cd00354; FBPase; 1.
DR HAMAP; MF_01855; FBPase_class1; 1.
DR InterPro; IPR044015; FBPase_C_dom.
DR InterPro; IPR000146; FBPase_class-1.
DR InterPro; IPR033391; FBPase_N.
DR InterPro; IPR028343; FBPtase.
DR InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR PANTHER; PTHR11556; PTHR11556; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00115; F16BPHPHTASE.
DR PROSITE; PS00124; FBPASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..332
FT /note="Fructose-1,6-bisphosphatase class 1"
FT /id="PRO_0000364697"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 110
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 113..116
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 257..259
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
SQ SEQUENCE 332 AA; 36799 MW; CDC783B1DF8ACE43 CRC64;
MKTLGEFIVE KQHEFSQATG ELTALLSAIK LGAKIIHRDI NKAGLVDILG ASGAENVQGE
VQQKLDLFAN EKLKAALKAR DIVAGIASEE EDEIVVFEGC EHAKYVVLMD PLDGSSNIDV
NVSVGTIFSI YRRVTPVGTP VTEEDFLQPG NKQVAAGYVV YGSSTMLVYT TGCGVHAFTY
DPSLGVFCLC QERMRFPEKG KTYSINEGNY IKFPNGVKKY IKFCQEEDSS TSRPYTSRYI
GSLVADFHRN LLKGGIYLYP STASHPQGKL RLLYECNPMA FLAEQAGGKA SDGKERILDI
IPESLHQRRS FFVGNRHMVD DVERFIREYP DA
