ID A0A3Q4G6J0_NEOBR Unreviewed; 337 AA.
AC A0A3Q4G6J0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000004240.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000004240.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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_006809639.1; XM_006809576.1.
DR AlphaFoldDB; A0A3Q4G6J0; -.
DR STRING; 32507.ENSNBRP00000004240; -.
DR Ensembl; ENSNBRT00000004376.1; ENSNBRP00000004240.1; ENSNBRG00000003354.1.
DR GeneID; 102787440; -.
DR CTD; 8789; -.
DR GeneTree; ENSGT00390000015513; -.
DR OMA; NSRFWEP; -.
DR OrthoDB; 292at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000003354; Expressed in skeletal muscle tissue and 2 other cell types or tissues.
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:UP000261580}.
FT DOMAIN 13..199
FT /note="Fructose-1-6-bisphosphatase class I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00316"
FT DOMAIN 204..332
FT /note="Fructose-1-6-bisphosphatase class 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18913"
SQ SEQUENCE 337 AA; 36775 MW; 6B5839382015FED8 CRC64;
MSDQSAFETD VWTLTRFVIE TGRQAKGATG ELTQLINAML TAIKAISSAV RKAGLAHLQG
LAGAVNVTGD DVKKLDVLSN DLVINMLQAS YSTCCMVSEE NKELIVTPQE KRGKYVVCFD
PLDGSSNIDC LASIGTIFAI YKRTSEGEPT EKDALQQGNN IVCAGYALYG SATLVAFSTG
AGVNFFTLDP AVGEFILTER NVRIKPKGKI YSLNEGYAKY FHPSINEYLK HKKYPEDGSS
PYGARYVGSM VSDIHRTIAY GGIFMYPANE KSPKGKLRLL YECNPIAFII EQAGGLATTG
TQRILDVQPE SLHQRVPFVV GSPDDVNEYL SFVKKFS
//
