ID   F16PC_PORGI             Reviewed;         655 AA.
AC   Q7MW52;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=PG_0793;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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; AE015924; AAQ65954.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7MW52; -.
DR   STRING; 242619.PG_0793; -.
DR   EnsemblBacteria; AAQ65954; AAQ65954; PG_0793.
DR   KEGG; pgi:PG_0793; -.
DR   eggNOG; COG3855; Bacteria.
DR   HOGENOM; CLU_028392_2_0_10; -.
DR   OMA; AKMHKAI; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000588; 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; Reference proteome.
FT   CHAIN           1..655
FT                   /note="Fructose-1,6-bisphosphatase class 3"
FT                   /id="PRO_0000363107"
SQ   SEQUENCE   655 AA;  75068 MW;  655851538BCE111E CRC64;
     MLKHDLDYLE LLSESFPTAT EAATEIINLE AILNLPKGTE HFLADIHGEY EAFIHVLKNA
     SGSIRRKVDE VFGGQLRQNQ KRELCTLIYY PREKLELVKQ SDERMEDWYM VTLNQLIKVC
     QKAAEKYTRS KVRKTLPPKY SYIIQELLHE DGVNPNKSAY ISSIFSSIIS TGCADDFIIA
     ISETIQRLVI DHLHVVGDVF DRGPGAHIIM DTLMKYHHFD IQWGNHDMLW MGAAVGNASC
     MANVVRIALR YANLDTLESG YGINLLPLAR FAMDTYADDP CTVFKPKLAQ ADQTYDDKSV
     YLISQMHKAI SIIQFKLEHQ IIARHPEYKM DNRDLFHLVN FTDGTIKLSS GVYPMLDMNF
     PTVDPADPYA LTEQEQNIVD RLMGCFMRSE KLQNHLKCLY RHGSMYLTYN MNLLYHASIP
     LNKDKSLKKV RVGDKTYAGR ELLDKVEEMI RTAYVAPEKS DQRLAAVDYM WYLWCGPDSP
     LFDKAMMTTF ERYFIEDKAT HHEEKGYYYV YRQEKAVCEM ILKEFGLEGP DTHIINGHVP
     VKAKKGELPI GAEGKLMLID GGFSKAYQSS TGIAGYTLIF NSQGLHLVQH EPFSSTRKAI
     EEMEDIKSIT VVREVTSHRM LVKDTDNGHL LSKQVENLKK LLQAYSYGLI KERKK