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F16PA_CAMC1
ID   F16PA_CAMC1             Reviewed;         287 AA.
AC   A7ZCB2;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Ccon26_05230;
GN   ORFNames=CCC13826_1544;
OS   Campylobacter concisus (strain 13826).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13826;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., On S., Nelson K.E.;
RT   "Genome sequence of Campylobacter concisus 13826 isolated from human
RT   feces.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000792; EAT99007.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7ZCB2; -.
DR   SMR; A7ZCB2; -.
DR   STRING; 360104.CCC13826_1544; -.
DR   EnsemblBacteria; EAT99007; EAT99007; CCC13826_1544.
DR   KEGG; cco:CCC13826_1544; -.
DR   eggNOG; COG0158; Bacteria.
DR   HOGENOM; CLU_039977_0_0_7; -.
DR   OMA; YIPENCP; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001121; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
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; IPR023079; SBPase.
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; PR01958; S17BPHPHTASE.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..287
FT                   /note="Fructose-1,6-bisphosphatase class 1"
FT                   /id="PRO_0000364508"
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         86
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         89..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         89
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
SQ   SEQUENCE   287 AA;  32398 MW;  75377DBBE3061C0D CRC64;
     MQELNQIFNT IKDIAKEISE VIKYADLGYT THENATGDTQ LKLDVKSDEI ITAKFKQLSC
     VKALISEEKE DELEINKNAK FIIAYDPLDG SSLVDVNFAV GSIFGIYEDE VKPENLIAAA
     YSIYGPRLEL VIAEKKGALP KFYRLGKDGE FKFVKELELK EKGKLNATGA TQKGWSQTHR
     NFINELFNEG YRLRYSGAMV SDLHQILLKG GGLFSYPATS DHPNGKLRVV FEVLPFAFIY
     ENAKGATTDG KNQTLFDIKI EKIHQTTPCF FGSRDEISLL HKFYEQK
 
 
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