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Database: UniProt
Entry: A0A091D8L3_FUKDA
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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}.
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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
//
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