ID   F16PC_STAHJ             Reviewed;         654 AA.
AC   Q4L907;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 109.
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=SH0559;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE03868.1; -; Genomic_DNA.
DR   RefSeq; WP_011274884.1; NC_007168.1.
DR   AlphaFoldDB; Q4L907; -.
DR   STRING; 279808.SH0559; -.
DR   EnsemblBacteria; BAE03868; BAE03868; SH0559.
DR   KEGG; sha:SH0559; -.
DR   eggNOG; COG3855; Bacteria.
DR   HOGENOM; CLU_028392_2_0_9; -.
DR   OMA; AKMHKAI; -.
DR   OrthoDB; 378029at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000543; 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; 2.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Manganese.
FT   CHAIN           1..654
FT                   /note="Fructose-1,6-bisphosphatase class 3"
FT                   /id="PRO_0000359998"
SQ   SEQUENCE   654 AA;  76026 MW;  2B2C287D277AEEC0 CRC64;
     MTQTTESELR EKYLDLLSQQ FDSPEKLATE IVNLESILEL PKGTEHFVSD LHGEYESFQH
     VLRNGSGNVR SKINDLYAKT LSQKEIDDLA ALVYYPEEKL KLVKNNFDSK GKLNVWYITT
     IEQLIDLITY CSSKYTRSKL RKALPKEYTY IVEELLYKNN EFNNKKSYYE TLVNQIIELE
     QSDDLIIGLS YSIQRLVVDH LHVVGDIYDR GPQPDKIMDT LINYHSVDIQ WGNHDVLWIG
     AYAGSKACLA NLLRICARYD NLDIIEDAYG INLRPLLTLA EEHYNGENPA FKPKKRPDKP
     VGLSKLEESQ ITKIHQAIAM IQFKLEMPII KRRPTFEMED RLVLEKVNYD TNEITIYGKT
     YPLKDTCFST VDPQDPGKLL PEEEEVMNKL LLSFQQSEKL KRHMSFLMKK GKLYLPYNGN
     LLIHGCIPVD ENGEMESFEI EGEQHKGRDL LDVFERHVRY AYDYKEITDD LSTDLVWYLW
     TGKYSSLFGK RAMTTFERYF IEDKASHKEP KNPYYYLRED VDMIRKMLKD FGLNPDEGRI
     INGHTPVKEI DGEDPIKADG KMLVIDGGFS KAYQKTTGIA GYTLLYNSFG MQLVAHQHFD
     SRDKVLSDGA DELSVRRVVD EELQRKKIRD TNDGKVLQEQ IRILKLLMHD RYLN