ID   F16P2_BOVIN             Reviewed;         339 AA.
AC   Q2KJJ9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   05-MAY-2009, entry version 27.
DE   RecName: Full=Fructose-1,6-bisphosphatase isozyme 2;
DE            Short=FBPase 2;
DE            EC=3.1.3.11;
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 2;
GN   Name=FBP2;
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=Ileum;
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. Fructose-2,6-biphosphate acts as competitive inhibitor
CC       (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; BC102390; AAI02391.1; -; mRNA.
DR   IPI; IPI00716812; -.
DR   RefSeq; NP_001039629.1; -.
DR   UniGene; Bt.28208; -.
DR   SMR; Q2KJJ9; 9-335.
DR   Ensembl; ENSBTAG00000019554; Bos taurus.
DR   GeneID; 514066; -.
DR   KEGG; bta:514066; -.
DR   HOVERGEN; Q2KJJ9; -.
DR   OMA; Q2KJJ9; ATGELTQ.
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   Carbohydrate metabolism; Gluconeogenesis; Hydrolase; Magnesium;
KW   Metal-binding; Phosphoprotein.
FT   CHAIN         1    339       Fructose-1,6-bisphosphatase isozyme 2.
FT                                /FTId=PRO_0000247323.
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 (By similarity).
FT   BINDING     265    265       Substrate (By similarity).
FT   MOD_RES     216    216       Phosphotyrosine (By similarity).
SQ   SEQUENCE   339 AA;  36767 MW;  DB3FE9856DDC5FB2 CRC64;
     MGDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLANLYGI
     AGSVNVTGDE VKKLDVLSNA LVINMLQSSY STCVLVSEEN KEAIITSKEK RGKYVVCFDP
     LDGSSNIDCL ASIGTIFAIY RKTSEDEPSE KDALQPGRNI VAAGYALYGS ATLVALSTGQ
     GVDLFMLDPA LGEFVLVEKD VKIKKKGKIY SLNEGYAKYF DAATTEYVQK KKFPEDGSAP
     YGARYVGSMV ADVHRTLVYG GIFLYPANQK SPKGKLRLLY ECNPVAYIIE QAGGLATTGT
     QPVLDVKPEA IHQRVPLILG SPEDVQEYLT CVQKNQAGR
//