ID   F16PC_LIGS1             Reviewed;         641 AA.
AC   Q1WQZ0;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 83.
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=LSL_1903;
OS   Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OG   Plasmid pMP118.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCC118;
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA   Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE00708.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000234; ABE00708.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_536791.1; NC_007930.1.
DR   AlphaFoldDB; Q1WQZ0; -.
DR   EnsemblBacteria; ABE00708; ABE00708; LSL_1903.
DR   KEGG; lsl:LSL_1903; -.
DR   PATRIC; fig|362948.14.peg.2029; -.
DR   HOGENOM; CLU_028392_2_0_9; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000006559; Plasmid pMP118.
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; Plasmid; Reference proteome.
FT   CHAIN           1..641
FT                   /note="Fructose-1,6-bisphosphatase class 3"
FT                   /id="PRO_0000363097"
SQ   SEQUENCE   641 AA;  74546 MW;  3A27DB5D924F956D CRC64;
     MNAYSHNLLK EKYPTKQDVI TEIMNLEAIL HLPKGTEHFV SDLHGEYTAF DHVLRNGSGS
     IKQKIQDYFS DRMTEQTMQD FALLIYYPED ELALVKKKLR TENELQQWYL DNISHLLEFL
     ELSGSKYTRS KVRKALNPNF VYITEELLYN DPQEFNKRSY INQLLKNILK LDQADKFIIA
     TCYTIQRLVV DHLHVLGDVY DRGEEPDKIM DRLMNYHSVD MQWGNHDLLW LGAMAGSKLC
     MLNLLRICAR YNNLNIIEDA YGINLRHLSR FAEEQYEDNP QFRPKLTNGD GYRFNGEKLQ
     ITQIHQAVAM MQFKLEGQVI ARRPELKMDD RDLLNKIDYK KNVINLNGKE YSLQNTCFNT
     VDPKNPNELT DEENAIVDEL LISIQHSTKL KRHLDFMMNK GSMYRTYNGN LLFHGCIPAD
     EEGNFCSLKI GSKEYSGKKL FDFSEKMIRK AYSKPNVKDD FATDFMWYLW QGALSPLFGK
     KSMTTFERYF IADKACHEEV KNPYYKLREN KDFCIKILQE FGFAGDDTNH IINGHTPVKR
     GHNAICAEGY MLVIDGGYSK AYQPTTGIAG YTLLYNSYGL QLVSHQPFTS KQDAIRSGKD
     IVSTVRVVKH ELQRKSVADT DIGENIKEKI RVLYNLLRNY D