ID   F16P1_BOVIN             Reviewed;         338 AA.
AC   Q3SZB7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 35.
DE   RecName: Full=Fructose-1,6-bisphosphatase 1;
DE            Short=FBPase 1;
DE            EC=3.1.3.11;
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 1;
GN   Name=FBP1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate.
CC   -!- COFACTOR: Binds 3 magnesium ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Subject to complex allosteric regulation. The
CC       enzyme can assume an active R-state, or an inactive T-state.
CC       Intermediate conformations may exist. AMP acts as allosteric
CC       inhibitor. AMP binding affects the turnover of bound substrate and
CC       not the affinity for substrate. Fructose-2,6-biphosphate acts as
CC       competitive inhibitor. Fructose-2,6-biphosphate and AMP have
CC       synergistic effects (By similarity).
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family.
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DR   EMBL; BC102974; AAI02975.1; -; mRNA.
DR   IPI; IPI00704584; -.
DR   RefSeq; NP_001029619.1; -.
DR   UniGene; Bt.24314; -.
DR   SMR; Q3SZB7; 7-337, 8-338.
DR   PRIDE; Q3SZB7; -.
DR   Ensembl; ENSBTAG00000009733; Bos taurus.
DR   GeneID; 513483; -.
DR   KEGG; bta:513483; -.
DR   HOVERGEN; Q3SZB7; -.
DR   BRENDA; 3.1.3.11; 251.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase act...; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR000146; Fructose_bisphosphatase.
DR   InterPro; IPR017955; IMPase/FBPase.
DR   PANTHER; PTHR11556; In_FB_phphtase; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   PRINTS; PR00115; FBPHPHTASE.
DR   PRINTS; PR00377; INFBPHPHTASE.
DR   ProDom; PD001491; In_FB_phphtase; 1.
DR   PROSITE; PS00124; FBPASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Allosteric enzyme; Carbohydrate metabolism;
KW   Gluconeogenesis; Hydrolase; Magnesium; Metal-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    338       Fructose-1,6-bisphosphatase 1.
FT                                /FTId=PRO_0000247322.
FT   NP_BIND      18     22       AMP (By similarity).
FT   NP_BIND      28     32       AMP (By similarity).
FT   NP_BIND     113    114       AMP (By similarity).
FT   REGION      122    125       Substrate binding (By similarity).
FT   REGION      213    216       Substrate binding (By similarity).
FT   REGION      244    249       Substrate binding (By similarity).
FT   REGION      275    277       Substrate binding (By similarity).
FT   METAL        69     69       Magnesium 1 (By similarity).
FT   METAL        98     98       Magnesium 1 (By similarity).
FT   METAL        98     98       Magnesium 2 (By similarity).
FT   METAL       119    119       Magnesium 2 (By similarity).
FT   METAL       119    119       Magnesium 3 (By similarity).
FT   METAL       121    121       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       122    122       Magnesium 3 (By similarity).
FT   METAL       281    281       Magnesium 3 (By similarity).
FT   BINDING     141    141       AMP.
FT   BINDING     265    265       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylthreonine (By similarity).
SQ   SEQUENCE   338 AA;  36728 MW;  83EB68040BC2664F CRC64;
     MTDQAAFDTN IVTVTRFVME EGRKARGTGE MTQLLNSLCT AVKAISTAVR KAGIAHLYGI
     AGTTNVTGDQ VKKLDVLSND LVVNVLKSSF ATCVLVSEED EHAIIVEPEK RGKYVVCFDP
     LDGSSNIDCL VSIGTIFGIY KKISKDDPSE KDALQPGRNL VAAGYALYGS ATMLVLAMAN
     GVNCFMLDPA IGEFILVDRD VKIKKKGSIY SLNEGYAKDF DPALTEYVQR KKFPPDNSAP
     YGARYVGSMV ADVHRTLVYG GIFMYPANKK SPSGKLRLLY ECNPMAYVIE KAGGMATTGK
     ETVLDIVPTD IHQKSPIILG SPEDVTEFLE IYKKHAAK
//