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Fructose-1,6-bisphosphatase 1 (FBPase 1) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 1) (Liver FBPase)

 F16P1_RABIT             Reviewed;         338 AA.
P00637;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 4.
25-OCT-2017, entry version 126.
RecName: Full=Fructose-1,6-bisphosphatase 1;
Short=FBPase 1;
EC=3.1.3.11;
AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 1;
AltName: Full=Liver FBPase;
Name=FBP1; Synonyms=FBP;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
PROTEIN SEQUENCE OF 2-338.
TISSUE=Liver;
PubMed=8766709; DOI=10.1016/0014-5793(96)00594-7;
Kaiser R., Olsson H., Erman M., Weeks C.M., Hjelmqvist L., Ghosh D.,
Joernvall H.;
"Fructose-1,6-bisphosphatase. Primary structure of the rabbit liver
enzyme. 'Intermediate' variability of an oligomeric protein.";
FEBS Lett. 389:249-252(1996).
[2]
PROTEIN SEQUENCE OF 2-19, AND ACETYLATION AT ALA-2.
STRAIN=New Zealand white; TISSUE=Liver;
PubMed=189691; DOI=10.1016/0003-9861(77)90185-0;
El-Dorry H.A., Chu D.K., Dzugaj A., Tsolas O., Pontremoli S.,
Horecker B.L.;
"Rabbit liver fructose 1,6-bisphosphatase: the sequence of the amino-
terminal region.";
Arch. Biochem. Biophys. 178:200-207(1977).
[3]
PROTEIN SEQUENCE OF 17-61.
STRAIN=New Zealand white; TISSUE=Liver;
PubMed=197893; DOI=10.1016/0003-9861(77)90558-6;
El-Dorry H.A., Chu D.K., Dzugaj A., Botelho L.H., Pontremoli S.,
Horecker B.L.;
"Primary structure of the S-peptide formed by digestion of rabbit
liver fructose 1,6-biphosphatase with subtilisin.";
Arch. Biochem. Biophys. 182:763-773(1977).
[4]
PROTEIN SEQUENCE OF 20-78.
STRAIN=New Zealand white; TISSUE=Liver;
PubMed=202200; DOI=10.1016/0003-9861(77)90463-5;
Botelho L.H., El-Dorry H.A., Crivellaro O., Chu D.K., Pontremoli S.,
Horecker B.L.;
"Digestion of rabbit liver fructose 1,6-bisphosphatase with
subtilisin: sites of cleavage and activity of the modified enzyme.";
Arch. Biochem. Biophys. 184:535-545(1977).
[5]
PRELIMINARY PROTEIN SEQUENCE OF 84-123 AND 136-155, AND ALLOSTERIC
REGULATION.
TISSUE=Liver;
PubMed=6289748; DOI=10.1016/0003-9861(82)90473-8;
Suda H., Xu G.-J., Kutny R.M., Natalini P., Pontremoli S.,
Horecker B.L.;
"Location of lysyl residues at the allosteric site of fructose 1,6-
bisphosphatase.";
Arch. Biochem. Biophys. 217:10-14(1982).
[6]
PROTEIN SEQUENCE OF 249-289 AND 296-338.
TISSUE=Liver;
PubMed=6284034; DOI=10.1016/0003-9861(82)90075-3;
Xu G.J., Natalini P., Suda H., Tsolas O., Dzugaj A., Sun S.C.,
Pontremoli S., Horecker B.L.;
"Rabbit liver fructose-1,6-bisphosphatase: location of an active site
lysyl residue in the COOH-terminal fragment generated by a lysosomal
proteinase.";
Arch. Biochem. Biophys. 214:688-694(1982).
[7]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
PubMed=10089399; DOI=10.1107/S0907444998008750;
Weeks C.M., Roszak A.W., Erman M., Kaiser R., Joernvall H., Ghosh D.;
"Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A
resolution.";
Acta Crystallogr. D 55:93-102(1999).
-!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to
fructose 6-phosphate in the presence of divalent cations, acting
as a rate-limiting enzyme in gluconeogenesis. Plays a role in
regulating glucose sensing and insulin secretion of pancreatic
beta-cells. Appears to modulate glycerol gluconeogenesis in liver.
Important regulator of appetite and adiposity; increased
expression of the protein in liver after nutrient excess increases
circulating satiety hormones and reduces appetite-stimulating
neuropeptides and thus seems to provide a feedback mechanism to
limit weight gain (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
fructose 6-phosphate + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Subject to complex allosteric regulation. The
enzyme can assume an active R-state, or an inactive T-state.
Intermediate conformations may exist. AMP acts as allosteric
inhibitor. AMP binding affects the turnover of bound substrate and
not the affinity for substrate. Fructose 2,6-bisphosphate acts as
competitive inhibitor. Fructose 2,6-bisphosphate and AMP have
synergistic effects (By similarity). {ECO:0000250}.
-!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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PIR; S70469; S70469.
UniGene; Ocu.3240; -.
PDB; 1BK4; X-ray; 2.30 A; A=2-338.
PDBsum; 1BK4; -.
SMR; P00637; -.
iPTMnet; P00637; -.
PRIDE; P00637; -.
HOGENOM; HOG000191265; -.
HOVERGEN; HBG005627; -.
InParanoid; P00637; -.
SABIO-RK; P00637; -.
UniPathway; UPA00138; -.
EvolutionaryTrace; P00637; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0016208; F:AMP binding; ISS:UniProtKB.
GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
GO; GO:0048029; F:monosaccharide binding; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; ISS:UniProtKB.
GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISS:UniProtKB.
GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
GO; GO:0045820; P:negative regulation of glycolytic process; ISS:UniProtKB.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
CDD; cd00354; FBPase; 1.
HAMAP; MF_01855; FBPase_class1; 1.
InterPro; IPR000146; FBPase_class-1.
InterPro; IPR033391; FBPase_N.
InterPro; IPR028343; FBPtase.
InterPro; IPR020548; Fructose_bisphosphatase_AS.
PANTHER; PTHR11556; PTHR11556; 1.
Pfam; PF00316; FBPase; 1.
PIRSF; PIRSF500210; FBPtase; 1.
PIRSF; PIRSF000904; FBPtase_SBPase; 1.
PRINTS; PR00115; F16BPHPHTASE.
PROSITE; PS00124; FBPASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Carbohydrate metabolism;
Complete proteome; Direct protein sequencing; Gluconeogenesis;
Hydrolase; Magnesium; Metal-binding; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:189691,
ECO:0000269|PubMed:8766709}.
CHAIN 2 338 Fructose-1,6-bisphosphatase 1.
/FTId=PRO_0000200501.
NP_BIND 18 22 AMP. {ECO:0000250}.
NP_BIND 28 32 AMP. {ECO:0000250}.
NP_BIND 113 114 AMP. {ECO:0000250}.
REGION 122 125 Substrate binding. {ECO:0000250}.
REGION 213 216 Substrate binding. {ECO:0000250}.
REGION 244 249 Substrate binding. {ECO:0000250}.
REGION 275 277 Substrate binding. {ECO:0000250}.
METAL 69 69 Magnesium 1. {ECO:0000250}.
METAL 98 98 Magnesium 1. {ECO:0000250}.
METAL 98 98 Magnesium 2.
METAL 119 119 Magnesium 2.
METAL 119 119 Magnesium 3. {ECO:0000250}.
METAL 121 121 Magnesium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 122 122 Magnesium 3. {ECO:0000250}.
METAL 281 281 Magnesium 3. {ECO:0000250}.
BINDING 141 141 AMP. {ECO:0000250}.
BINDING 265 265 Substrate. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:189691}.
MOD_RES 151 151 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9QXD6}.
MOD_RES 216 216 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QXD6}.
MOD_RES 245 245 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QXD6}.
MOD_RES 265 265 Phosphotyrosine.
{ECO:0000250|UniProtKB:P09467}.
CONFLICT 84 84 N -> D (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 89 89 S -> A (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 93 93 C -> S (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 116 117 VC -> SN (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 122 123 DG -> VP (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 268 268 N -> D (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 281 281 E -> Q (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 284 284 Missing (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 301 301 E -> Q (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 308 313 PTDIHQ -> QTPDH (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 327 327 E -> Q (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 330 331 Missing (in Ref. 6; AA sequence).
{ECO:0000305}.
HELIX 14 25 {ECO:0000244|PDB:1BK4}.
HELIX 30 49 {ECO:0000244|PDB:1BK4}.
TURN 50 53 {ECO:0000244|PDB:1BK4}.
HELIX 74 88 {ECO:0000244|PDB:1BK4}.
STRAND 92 97 {ECO:0000244|PDB:1BK4}.
HELIX 108 110 {ECO:0000244|PDB:1BK4}.
STRAND 111 122 {ECO:0000244|PDB:1BK4}.
HELIX 126 129 {ECO:0000244|PDB:1BK4}.
STRAND 133 141 {ECO:0000244|PDB:1BK4}.
HELIX 150 153 {ECO:0000244|PDB:1BK4}.
HELIX 157 159 {ECO:0000244|PDB:1BK4}.
STRAND 161 178 {ECO:0000244|PDB:1BK4}.
STRAND 181 188 {ECO:0000244|PDB:1BK4}.
TURN 189 192 {ECO:0000244|PDB:1BK4}.
STRAND 193 198 {ECO:0000244|PDB:1BK4}.
STRAND 208 211 {ECO:0000244|PDB:1BK4}.
HELIX 214 219 {ECO:0000244|PDB:1BK4}.
HELIX 222 232 {ECO:0000244|PDB:1BK4}.
HELIX 249 259 {ECO:0000244|PDB:1BK4}.
STRAND 262 265 {ECO:0000244|PDB:1BK4}.
STRAND 275 277 {ECO:0000244|PDB:1BK4}.
TURN 278 281 {ECO:0000244|PDB:1BK4}.
HELIX 282 292 {ECO:0000244|PDB:1BK4}.
STRAND 295 297 {ECO:0000244|PDB:1BK4}.
STRAND 299 302 {ECO:0000244|PDB:1BK4}.
HELIX 303 305 {ECO:0000244|PDB:1BK4}.
STRAND 317 320 {ECO:0000244|PDB:1BK4}.
HELIX 322 333 {ECO:0000244|PDB:1BK4}.
TURN 334 336 {ECO:0000244|PDB:1BK4}.
SEQUENCE 338 AA; 36578 MW; 2676BF5964461250 CRC64;
MADKAPFDTD ISTMTRFVME EGRKAGGTGE MTQLLNSLCT AVKAISTAVR KAGIAHLYGI
AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KNAIIVEPEK RGKYVVCFDP
LDGSSNIDCL VSIGTIFGIY RKKSTDEPST KDALQPGRNL VAAGYALYGS ATMLVLAGGS
GVNSFMLDPA IGEFILVDKN VKIKKKGNIY SLNEGYAKDF DPAVTEYIQK KKFPPDNSSP
YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPDGKLRLLY ECNPMAFIME KAGGMATTGK
EAILDIVPTD IHQRAPVILG SPDDVQEFLE IYKKHAVK


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