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F16A3_METPP
ID   F16A3_METPP             Reviewed;         357 AA.
AC   A2SJK3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Fructose-1,6-bisphosphatase class 1 3 {ECO:0000255|HAMAP-Rule:MF_01855};
DE            Short=FBPase class 1 3 {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 3 {ECO:0000255|HAMAP-Rule:MF_01855};
GN   Name=fbp3 {ECO:0000255|HAMAP-Rule:MF_01855}; OrderedLocusNames=Mpe_A2788;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
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; Calvin cycle. {ECO:0000255|HAMAP-
CC       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; CP000555; ABM95742.1; -; Genomic_DNA.
DR   RefSeq; WP_011830371.1; NC_008825.1.
DR   AlphaFoldDB; A2SJK3; -.
DR   SMR; A2SJK3; -.
DR   STRING; 420662.Mpe_A2788; -.
DR   EnsemblBacteria; ABM95742; ABM95742; Mpe_A2788.
DR   KEGG; mpt:Mpe_A2788; -.
DR   eggNOG; COG0158; Bacteria.
DR   HOGENOM; CLU_039977_2_2_4; -.
DR   OMA; NSRFWEP; -.
DR   OrthoDB; 945770at2; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000000366; 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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniRule.
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   Calvin cycle; Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..357
FT                   /note="Fructose-1,6-bisphosphatase class 1 3"
FT                   /id="PRO_0000364598"
FT   BINDING         94
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         116
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         119..122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT   BINDING         283
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
SQ   SEQUENCE   357 AA;  39078 MW;  4328E8BE427BBB7E CRC64;
     MPTGGKSTLT QFLIEERRKH PAATGELNAL ITDVSLACKA ISRKVAFGGL AGVLGSAGSG
     NVQGEEQKTL DVLSNTMFLR ATEWGGHVAG MVSEELEAPY TLPPQYARGK YLLMFDPLDG
     SSNIDVNVTV GSIFAIHRAP QPRQDPQPQD YLQPGTTMVC GGYAIYGPST MLVLTLGDGT
     HAFTLDPQLG EWVLSHPNLR IPEKTREFAI NASNSRFWEP AVKRYVDECL AGSTGPRGTD
     FNMRWIASLV AETHRILMRG GVFLYPRDSK DPNKAGRLRL LYEANPISFL IEQAGGMAST
     GRKRLLEVQP EDIHQRIGFV FGSTEEVARI EAYHRDEPPT PYNSPLFGKR GLFAEAG
 
 
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