ID   F16PC_CLOBH             Reviewed;         668 AA.
AC   A5HZ60; A7FZS6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Fructose-1,6-bisphosphatase class 3 {ECO:0000255|HAMAP-Rule:MF_01854};
DE            Short=FBPase class 3 {ECO:0000255|HAMAP-Rule:MF_01854};
DE            EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01854};
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 3 {ECO:0000255|HAMAP-Rule:MF_01854};
GN   Name=fbp {ECO:0000255|HAMAP-Rule:MF_01854};
GN   OrderedLocusNames=CBO0516, CLC_0589;
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(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_01854};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01854};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01854}.
CC   -!- SIMILARITY: Belongs to the FBPase class 3 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01854}.
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DR   EMBL; CP000727; ABS37392.1; -; Genomic_DNA.
DR   EMBL; AM412317; CAL82069.1; -; Genomic_DNA.
DR   RefSeq; WP_011948262.1; NC_009698.1.
DR   RefSeq; YP_001253059.1; NC_009495.1.
DR   RefSeq; YP_001386472.1; NC_009698.1.
DR   AlphaFoldDB; A5HZ60; -.
DR   GeneID; 5184771; -.
DR   KEGG; cbh:CLC_0589; -.
DR   KEGG; cbo:CBO0516; -.
DR   PATRIC; fig|413999.7.peg.518; -.
DR   HOGENOM; CLU_028392_2_0_9; -.
DR   OMA; AKMHKAI; -.
DR   UniPathway; UPA00138; -.
DR   PRO; PR:A5HZ60; -.
DR   Proteomes; UP000001986; Chromosome.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.60.21.10; -; 1.
DR   HAMAP; MF_01854; FBPase_class3; 1.
DR   InterPro; IPR009164; FBPtase_class3.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF06874; FBPase_2; 1.
DR   PIRSF; PIRSF000906; FBPtase_Bacill; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..668
FT                   /note="Fructose-1,6-bisphosphatase class 3"
FT                   /id="PRO_0000363083"
SQ   SEQUENCE   668 AA;  77332 MW;  1DED30B170A82025 CRC64;
     MTLYDENNLH IIKDNLRYLK LLSKQYPSIS SASSEIINLQ AILNLPKGTE HFISDVHGEY
     ESFTHMLKNA SGVIKRKIDD VFGTSLRECD KKNLATLIYY PEQKLDLIKK SEKNLEDWYK
     ITLYRLIRLC QIVSSKYTRS KVRKSLPSDF AYIIEELLNE QGDRVDKQEY YNSIIETIID
     IDRASEFIIA ISNVIQRLVV DKLHIIGDIY DRGPGAEIII EALSKHHSID IQWGNHDIVW
     MGAAAGCEAC IANVIRISLR YANLSTLEDG YGINLLPLAT FAMDFYKEDN CENFKPRTID
     KNLNETDIKL LSKMHKAISI IQFKLEGKII KRRPEFKMGE RLLLDKINIK EGTLNLNEKI
     YKLIDTNFPT LDKENPYELN ERERDLVEKL TNSFINSEKL QRHIKFLYSN GNLYLKYNSN
     LLYHGCIPLN EDGSLKEVTL CKETLKGKSL LDKLDRLARE AYFFKKDPES KLYGMDMMWY
     LWCGSNSPLF GKKKMTTFER YFLDDKNTHK EQKNPYYKYR NDEKMCTMIF EEFELDADNS
     HIINGHIPVK TKEGENPIKA NGKLLVIDGG FCKAYQPQTG IAGYTLIYNS YGLLLTSHEP
     FSSIHKAIVE GNDILSSTTI LEHVSSRKRV LDTDSGEEIK KQIHDLEMLL VAYRKGLIKE
     ENEANIRF