ID A0A1S3ASY7_ERIEU Unreviewed; 339 AA.
AC A0A1S3ASY7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 Name=FBP2 {ECO:0000313|RefSeq:XP_007539929.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007539929.1};
RN [1] {ECO:0000313|RefSeq:XP_007539929.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_007539929.1; XM_007539867.2.
DR AlphaFoldDB; A0A1S3ASY7; -.
DR GeneID; 103128942; -.
DR CTD; 8789; -.
DR eggNOG; KOG1458; Eukaryota.
DR InParanoid; A0A1S3ASY7; -.
DR OrthoDB; 292at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
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 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:UP000079721}.
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; 36846 MW; 77BE99728ACAC013 CRC64;
MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLANLYGI
AGSVNVTGDE VKKLDVLSNS LVINMLQSSY STCVLVSEEN KEAIITDKEK RGKYVVCFDP
LDGSSNIDCL ASIGTIFAIY RKTSEDEPSE KDALQTGRSI VAAGYALYGS ATLVALSTGQ
GVDLFMLDPA LGEFVLVEKD VKIKKKGKIY SLNEGYAKYF DAATTEYVQR KKFPEDGSAP
YGARYVGSMV ADVHRTLVYG GIFLYPANQK NPKGKLRLLY ECNPVAYIIE QAGGLATTGT
QPVLDVKPEA IHQRVPLILG SPDDVQEYLT CVQKSQAGR
//
