ID   F16PC_PORG3             Reviewed;         655 AA.
AC   B2RIZ0;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 66.
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=PGN_0816;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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=BAG33335.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP009380; BAG33335.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B2RIZ0; -.
DR   STRING; 431947.PGN_0816; -.
DR   EnsemblBacteria; BAG33335; BAG33335; PGN_0816.
DR   KEGG; pgn:PGN_0816; -.
DR   eggNOG; COG3855; Bacteria.
DR   HOGENOM; CLU_028392_2_0_10; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000008842; 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.
FT   CHAIN           1..655
FT                   /note="Fructose-1,6-bisphosphatase class 3"
FT                   /id="PRO_0000363108"
SQ   SEQUENCE   655 AA;  75096 MW;  CFD29DEB4DF91118 CRC64;
     MLKHDLDYLE LLSESFPTAT EVATEIINLE 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