ID   F16PC_DESPS             Reviewed;         605 AA.
AC   Q6AMN0;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=DP1666;
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54;
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(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; CR522870; CAG36395.1; -; Genomic_DNA.
DR   RefSeq; WP_011188907.1; NC_006138.1.
DR   AlphaFoldDB; Q6AMN0; -.
DR   STRING; 177439.DP1666; -.
DR   PRIDE; Q6AMN0; -.
DR   EnsemblBacteria; CAG36395; CAG36395; DP1666.
DR   KEGG; dps:DP1666; -.
DR   eggNOG; COG3855; Bacteria.
DR   HOGENOM; CLU_028392_2_0_7; -.
DR   OMA; AKMHKAI; -.
DR   OrthoDB; 378029at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000602; 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   SUPFAM; SSF56300; SSF56300; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..605
FT                   /note="Fructose-1,6-bisphosphatase class 3"
FT                   /id="PRO_0000363090"
SQ   SEQUENCE   605 AA;  70302 MW;  FB6609C7C27096E6 CRC64;
     MAEKICITEI DKLSQKLLRI ETELNANIPT TLWISDLHGE GDRFKSILRG RFGMLYQTCK
     EGLPATFTPE KIQYLAKIVR KKNYFADSQQ QMDRQDVILC FVQILKYKLT NSTNRNREIF
     LPEFRETIGR LLAGLPVPDP IFEESIISDR LIFHLSYAIR QVLLDRIQVL GDVFDRGSQP
     DKIIRILSSP AYKEMVDYVF GNHDILWMGA AAGTPSLVAE TLRITCRYDH FRLLNRLRFD
     TSRLAEFAER TYEIKKATGK FKAKTDRGRA MEKALTVIQF KLEEKLINDF PHYGMEKRLW
     LERLAEMLKT GATEELNDSD FPTIDLENPS KLSKEESEII NDLIEQFRSN KYLKRLLKFF
     FEEGSTYHIS NNFLNIHALV PSTKEGEFEE FMGHKGKDLL DYIQKVIRRT GQNYLYNREQ
     SADDLALFFY LWCGPKSPFF GKHAMKTFER YFLLDKERHA EHSLYWQKNM QSDAFKEKMQ
     EEFGIQRVIF GHTPVNYMQG NKMASEDGVA INVDGGFAAA YYNRGHALVH TPHQLYGIIL
     PTPDELIKAA VRLEPAPLDI EFIDEFPQPL KIKNTIAGKL LQQERDLIMG KIQSYNSQNR
     DSDIN