ID   F16PC_BACSU             Reviewed;         641 AA.
AC   Q45597; Q794W8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Fructose-1,6-bisphosphatase class 3;
DE            Short=FBPase class 3;
DE            EC=3.1.3.11;
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 3;
GN   Name=fbp; Synonyms=yydE; OrderedLocusNames=BSU40190;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9205843; DOI=10.1093/dnares/4.2.155;
RA   Kasahara Y., Nakai S., Ogasawara N.;
RT   "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT   Bacillus subtilis genome.";
RL   DNA Res. 4:155-159(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, COFACTOR, AND INDUCTION.
RX   PubMed=221467; DOI=10.1016/s0021-9258(18)50601-3;
RA   Fujita Y., Freese E.;
RT   "Purification and properties of fructose-1,6-bisphosphatase of Bacillus
RT   subtilis.";
RL   J. Biol. Chem. 254:5340-5349(1979).
RN   [4]
RP   FUNCTION, INDUCTION, IDENTIFICATION OF INITIATION SITE, AND MUTAGENESIS OF
RP   GLY-469.
RC   STRAIN=168 / 1A1;
RX   PubMed=9696785; DOI=10.1128/jb.180.16.4309-4313.1998;
RA   Fujita Y., Yoshida K., Miwa Y., Yanai N., Nagakawa E., Kasahara Y.;
RT   "Identification and expression of the Bacillus subtilis fructose-1, 6-
RT   bisphosphatase gene (fbp).";
RL   J. Bacteriol. 180:4309-4313(1998).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / NRRL NRS-744 / VKM B-501;
RX   PubMed=19270101; DOI=10.1128/jb.01783-08;
RA   Jules M., Le Chat L., Aymerich S., Le Coq D.;
RT   "The Bacillus subtilis ywjI (glpX) gene encodes a class II fructose-1,6-
RT   bisphosphatase, functionally equivalent to the class III Fbp enzyme.";
RL   J. Bacteriol. 191:3168-3171(2009).
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:0000269|PubMed:221467};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:221467};
CC   -!- ACTIVITY REGULATION: Activated by phosphoenolpyruvate (PEP) and by high
CC       concentrations of monovalent cations, NH(4)(+) being most effective. Is
CC       inhibited by two types of compounds which apparently act on the enzyme
CC       at different sites. The first group consists of nucleoside
CC       monophosphates (most effective are AMP and dAMP), phosphorylated
CC       coenzymes, and denatured DNA and RNA, whose inhibition is competed by
CC       PEP. The second group, whose inhibition is not competed by PEP,
CC       consists of highly phosphorylated nucleotides (pppGpp and pppApp are
CC       most effective), nucleoside di- and triphosphates, and PPi.
CC       {ECO:0000269|PubMed:221467}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13 uM for fructose-1,6-bisphosphate {ECO:0000269|PubMed:221467};
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:221467};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- INDUCTION: Constitutively expressed. Expressed at a fairly constant
CC       level in cells undergoing glycolysis or gluconeogenesis.
CC       {ECO:0000269|PubMed:221467, ECO:0000269|PubMed:9696785}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of fbp alone (or ywjI alone) does not
CC       affect growth on various carbon sources. But the ywjI fbp double mutant
CC       is unable to grow with carbon sources demanding FBPase activity, i.e.
CC       glycerol, malate, and a mixture of succinate and glutamate.
CC       {ECO:0000269|PubMed:19270101}.
CC   -!- SIMILARITY: Belongs to the FBPase class 3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA11277.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D78193; BAA11277.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB16056.2; -; Genomic_DNA.
DR   PIR; C69621; C69621.
DR   RefSeq; NP_391899.1; NC_000964.3.
DR   RefSeq; WP_003243329.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; Q45597; -.
DR   STRING; 224308.BSU40190; -.
DR   jPOST; Q45597; -.
DR   PaxDb; Q45597; -.
DR   PRIDE; Q45597; -.
DR   DNASU; 937744; -.
DR   EnsemblBacteria; CAB16056; CAB16056; BSU_40190.
DR   GeneID; 937744; -.
DR   KEGG; bsu:BSU40190; -.
DR   PATRIC; fig|224308.179.peg.4347; -.
DR   eggNOG; COG3855; Bacteria.
DR   InParanoid; Q45597; -.
DR   OMA; AKMHKAI; -.
DR   BioCyc; BSUB:BSU40190-MON; -.
DR   SABIO-RK; Q45597; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001570; 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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Hydrolase; Manganese; Reference proteome.
FT   CHAIN           1..641
FT                   /note="Fructose-1,6-bisphosphatase class 3"
FT                   /id="PRO_0000359981"
FT   MUTAGEN         469
FT                   /note="G->D: In fbp-74; abolishes FBPase activity."
FT                   /evidence="ECO:0000269|PubMed:9696785"
SQ   SEQUENCE   641 AA;  74493 MW;  B4C5EBCA6FCA1596 CRC64;
     MESKYLDLLA QKYDCEEKVV TEIINLKAIL NLPKGTEHFV SDLHGEYQAF QHVLRNGSGR
     VKEKIRDIFS GVIYDREIDE LAALVYYPED KLKLIKHDFD AKEALNEWYK ETIHRMIKLV
     SYCSSKYTRS KLRKALPAQF AYITEELLYK TEQAGNKEQY YSEIIDQIIE LGQADKLITG
     LAYSVQRLVV DHLHVVGDIY DRGPQPDRIM EELINYHSVD IQWGNHDVLW IGAYSGSKVC
     LANIIRICAR YDNLDIIEDV YGINLRPLLN LAEKYYDDNP AFRPKADENR PEDEIKQITK
     IHQAIAMIQF KLESPIIKRR PNFNMEERLL LEKIDYDKNE ITLNGKTYQL ENTCFATINP
     EQPDQLLEEE AEVIDKLLFS VQHSEKLGRH MNFMMKKGSL YLKYNGNLLI HGCIPVDENG
     NMETMMIEDK PYAGRELLDV FERFLREAFA HPEETDDLAT DMAWYLWTGE YSSLFGKRAM
     TTFERYFIKE KETHKEKKNP YYYLREDEAT CRNILAEFGL NPDHGHIING HTPVKEIEGE
     DPIKANGKMI VIDGGFSKAY QSTTGIAGYT LLYNSYGMQL VAHKHFNSKA EVLSTGTDVL
     TVKRLVDKEL ERKKVKETNV GEELLQEVAI LESLREYRYM K