ID M7BU78_CHEMY Unreviewed; 290 AA.
AC M7BU78;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Fructose-1,6-bisphosphatase 1 {ECO:0000256|ARBA:ARBA00040734};
DE EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 1 {ECO:0000256|ARBA:ARBA00042758};
DE AltName: Full=Liver FBPase {ECO:0000256|ARBA:ARBA00042792};
GN ORFNames=UY3_03452 {ECO:0000313|EMBL:EMP39340.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP39340.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC fructose 6-phosphate in the presence of divalent cations, acting as a
CC rate-limiting enzyme in gluconeogenesis. Plays a role in regulating
CC glucose sensing and insulin secretion of pancreatic beta-cells. Appears
CC to modulate glycerol gluconeogenesis in liver. Important regulator of
CC appetite and adiposity; increased expression of the protein in liver
CC after nutrient excess increases circulating satiety hormones and
CC reduces appetite-stimulating neuropeptides and thus seems to provide a
CC feedback mechanism to limit weight gain.
CC {ECO:0000256|ARBA:ARBA00037308}.
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:0000256|ARBA:ARBA00001273};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family.
CC {ECO:0000256|ARBA:ARBA00010941, ECO:0000256|RuleBase:RU000508}.
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DR EMBL; KB517028; EMP39340.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BU78; -.
DR STRING; 8469.M7BU78; -.
DR eggNOG; KOG1458; Eukaryota.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR CDD; cd00354; FBPase; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR HAMAP; MF_01855; FBPase_class1; 1.
DR InterPro; IPR044015; FBPase_C_dom.
DR InterPro; IPR000146; FBPase_class-1.
DR InterPro; IPR033391; FBPase_N.
DR InterPro; IPR028343; FBPtase.
DR InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR PANTHER; PTHR11556:SF11; FRUCTOSE-1,6-BISPHOSPHATASE 1; 1.
DR PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00115; F16BPHPHTASE.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00124; FBPASE; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000508};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000508};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443}.
FT DOMAIN 10..150
FT /note="Fructose-1-6-bisphosphatase class I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00316"
FT DOMAIN 155..284
FT /note="Fructose-1-6-bisphosphatase class 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18913"
SQ SEQUENCE 290 AA; 31571 MW; FF95D7ED4F327A18 CRC64;
MRISFHCFSY GIAGSTNVTG DQVKKLDVLS NDLVINMLKS SFTTCVIVSE ENKNAIIVDA
EKRGKYIVCM DPLDGSSNID CLVSIGTIFA IYRKASSEKP SEKDALQPGR NLVAAGYALY
GSATVLVLAI ESGVNCFMLD PAIGEFILVD KNVKIKKRGN IYSLNEGYAA YFDPAVTEYL
KKKKFPQDGS SPYGARYIGS MVADVHRTLV YGGIFLYPAN SKSPKGKLRL LYECNPMAFV
IEKAGGIATT GNQAVLDIVP EDIHQRAPIA LGSPDDVQEY IDMVKKHSAK
//
