ID A0A091D8L3_FUKDA Unreviewed; 339 AA.
AC A0A091D8L3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Fructose-1,6-bisphosphatase isozyme 2 {ECO:0000256|ARBA:ARBA00040321};
DE EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 2 {ECO:0000256|ARBA:ARBA00042757};
DE AltName: Full=Muscle FBPase {ECO:0000256|ARBA:ARBA00043165};
GN ORFNames=H920_10330 {ECO:0000313|EMBL:KFO28469.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO28469.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO28469.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO28469.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
CC fructose 6-phosphate in the presence of divalent cations and probably
CC participates in glycogen synthesis from carbohydrate precursors, such
CC as lactate. {ECO:0000256|ARBA:ARBA00037516}.
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. Interacts with ALDOA; the interaction blocks
CC inhibition by physiological concentrations of AMP and reduces
CC inhibition by Ca(2+). Interacts with alpha-actinin and F-actin.
CC {ECO:0000256|ARBA:ARBA00038670}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000256|ARBA:ARBA00004216}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family.
CC {ECO:0000256|ARBA:ARBA00010941, ECO:0000256|RuleBase:RU000508}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN122776; KFO28469.1; -; Genomic_DNA.
DR RefSeq; XP_010634429.1; XM_010636127.2.
DR AlphaFoldDB; A0A091D8L3; -.
DR STRING; 885580.ENSFDAP00000007184; -.
DR Ensembl; ENSFDAT00000020403; ENSFDAP00000007184; ENSFDAG00000006447.
DR GeneID; 104870441; -.
DR CTD; 8789; -.
DR eggNOG; KOG1458; Eukaryota.
DR OMA; MNMLAAG; -.
DR OrthoDB; 292at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000028990; 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:SF13; FRUCTOSE-1,6-BISPHOSPHATASE ISOZYME 2; 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 Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000508};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT DOMAIN 13..198
FT /note="Fructose-1-6-bisphosphatase class I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00316"
FT DOMAIN 203..332
FT /note="Fructose-1-6-bisphosphatase class 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18913"
SQ SEQUENCE 339 AA; 36869 MW; BA2C7E89974F8E05 CRC64;
MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLAHLYGI
AGSVNVTGDE VKKLDVLSNA LVINMLQSSY STCVLVSEEN KEAIITSQER RGKYVVCFDP
LDGSSNIDCL ASIGTIFAIY RKTTEEEPSE KDALQAGRNI VAAGYALYGS ATLVALSTGQ
GVDLFMLDPA LGEFVLVEKD VKIKKKGKIF SLNEGYAKYF DAATTEYVQK KKFPEDGSAP
YGARYVGSMV ADVHRTLVYG GIFLYPANQK SPKGKLRLLY ECKPVAYIIE QAGGMATTGT
QPVLDVKPES IHQRVPLILG SPDDVQEYLT CVQKTQAGR
//