ID   F16PC_BACFR             Reviewed;         664 AA.
AC   Q64VB2;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 76.
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}; OrderedLocusNames=BF1819;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD48566.1; -; Genomic_DNA.
DR   RefSeq; WP_005794862.1; NZ_UYXF01000005.1.
DR   RefSeq; YP_099100.1; NC_006347.1.
DR   AlphaFoldDB; Q64VB2; -.
DR   STRING; 295405.BF1819; -.
DR   EnsemblBacteria; BAD48566; BAD48566; BF1819.
DR   GeneID; 66329357; -.
DR   KEGG; bfr:BF1819; -.
DR   PATRIC; fig|295405.11.peg.1767; -.
DR   HOGENOM; CLU_028392_2_0_10; -.
DR   OMA; AKMHKAI; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002197; 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   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.
FT   CHAIN           1..664
FT                   /note="Fructose-1,6-bisphosphatase class 3"
FT                   /id="PRO_0000363073"
SQ   SEQUENCE   664 AA;  76138 MW;  8443D63A7565A97D CRC64;
     MTAQSNITPE SIVADLRYLQ LLSRSFPTIA AASTEIINLE AILNLPKGTE HFLTDIHGEY
     EAFQHVLKNA SGAVKRKVNE IFGHTLREIE KKELCTLIYY PEEKLQLIKA TETDIDDWYL
     ITLNQLVKVC QNVSSKYTRS KVRKSLPAEF SYIIQELLHE STIEPNKHAY INVIISTIIS
     TRRADDFIIA MCNLIQRLTI DSLHIVGDIY DRGPGAHIIM DTLCDYHNFD IQWGNHDILW
     MGAASGNEAC MANVIRLSMR YGNLGTLEDG YGINLLPLAT FAMDTYADDP CTIFAPKTNF
     ADSTYNEKTL RLITQMHKAI TIIQFKLEAN IINRRPEFGM GGRKLLEKID FERGVFVYEG
     KEYPLRDTNF PTVDPADPYR LTDEEQELIE KIHYSFMNSE KLKKHMRCLF TYGGMYLVCN
     SNLLYHASVP LNEDGSFKHV NICGKEYWGK NLLDKIDQLI RTAYFDEDDE EEKRFAMDYI
     WYLWCGPDAP SFDKDKMATF ERYFIADKSL HKETKGYYYA LRNKEEICDR ILEEFGVTGQ
     HTHIINGHVP VKTIKGEQPM KAGGKLLVID GGFSKAYQPE TGIAGYTLVY HSHGLQLVQH
     DPFQSTQKAI EEGQDIKSTT FVIEFNSQRM MVKDTDKGKE LVTQILDLKK LLVAYRIGLI
     KEKV