(data stored in ACNUC4932 zone)

HOVERGEN: F261_BOVIN

ID   F261_BOVIN              Reviewed;         471 AA.
AC   P49872;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   22-SEP-2009, entry version 71.
DE   RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1;
DE   AltName: Full=6PF-2-K/Fru-2,6-P2ASE liver isozyme;
DE   Includes:
DE     RecName: Full=6-phosphofructo-2-kinase;
DE              EC=2.7.1.105;
DE   Includes:
DE     RecName: Full=Fructose-2,6-bisphosphatase;
DE              EC=3.1.3.46;
GN   Name=PFKFB1;
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 [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=91378600; PubMed=1654864; DOI=10.1016/0003-9861(91)90617-R;
RA   Lange A.J., El-Maghrabi M.R., Pilkis S.J.;
RT   "Isolation of bovine liver 6-phosphofructo-2-kinase/fructose-2,6-
RT   bisphosphatase cDNA: bovine liver and heart forms of the enzyme are
RT   separate gene products.";
RL   Arch. Biochem. Biophys. 290:258-263(1991).
CC   -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC   -!- CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + beta-D-
CC       fructose 2,6-bisphosphate.
CC   -!- ENZYME REGULATION: Phosphorylation results in inhibition of the
CC       kinase activity (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- TISSUE SPECIFICITY: Liver (By similarity).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       phosphoglycerate mutase family.
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CC   -!- GENE_FAMILY: HBG005628 [ FAMILY / ALN / TREE ]
DR   EMBL; M64323; AAA30696.1; -; mRNA.
DR   EMBL; S55569; AAB19845.1; -; mRNA.
DR   IPI; IPI00708146; -.
DR   PIR; A44872; A44872.
DR   RefSeq; NP_776997.3; -.
DR   UniGene; Bt.562; -.
DR   HSSP; P07953; 1C80.
DR   SMR; P49872; 42-470.
DR   STRING; P49872; -.
DR   Ensembl; ENSBTAT00000000198; ENSBTAP00000000198; ENSBTAG00000000172; Bos taurus.
DR   GeneID; 282304; -.
DR   KEGG; bta:282304; -.
DR   CTD; 282304; -.
DR   HOVERGEN; P49872; -.
DR   BRENDA; 2.7.1.105; 251.
DR   BRENDA; 3.1.3.46; 251.
DR   GO; GO:0043540; C:6-phosphofructo-2-kinase/fructose-2,6-bipho...; ISS:UniProtKB.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase act...; ISS:UniProtKB.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; ISS:UniProtKB.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR016260; Bifunct_6PFK/fruc_bisP_Ptase.
DR   InterPro; IPR001345; PG/BPGM_mutase_AC.
DR   InterPro; IPR013078; PG_mutase.
DR   PANTHER; PTHR10606; 6Pfruct_kin; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; P49872.
DR   SWISS-2DPAGE; P49872.
KW   ATP-binding; Hydrolase; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   DOMAIN        1     46       PRODOM:2005.1:PD023347  6
FT   DOMAIN       48    252       PRODOM:2005.1:PD324818  79
FT   DOMAIN      259    471       PRODOM:2005.1:PD858890  96
FT   CHAIN         1    471       6-phosphofructo-2-kinase/fructose-2,6-
FT                                biphosphatase 1.
FT                                /FTId=PRO_0000179959.
FT   NP_BIND      49     56       ATP (Potential).
FT   REGION        1    250       6-phosphofructo-2-kinase.
FT   REGION      251    471       Fructose-2,6-bisphosphatase.
FT   ACT_SITE    131    131       Potential.
FT   ACT_SITE    161    161       Potential.
FT   ACT_SITE    259    259       Tele-phosphohistidine intermediate.
FT   ACT_SITE    328    328       Potential.
FT   ACT_SITE    393    393       Proton donor (By similarity).
FT   BINDING     105    105       Fructose-6-phosphate (By similarity).
FT   BINDING     196    196       Fructose-6-phosphate (By similarity).
FT   MOD_RES      33     33       Phosphoserine; by PKA (By similarity).
SQ   SEQUENCE   471 AA;  54657 MW;  79C330B873B2D9EB CRC64;
     MSQEMGELTQ TRLQKIWIPH NNGNSRLQRR RGSSIPQFTN SPTMVIMVGL PARGKTYIST
     KLTRYLNWIG TPTKVFNLGQ YRREAVSYKN YEFFLPDNME ALLIRKQCAL AALKDVHSYL
     SHEEGRVAVF DATNTTRERR SLILQFAKEH GYKVFFIESI CNDPDVIAEN IRQVKLGSPD
     YIDCDREKVL EDFLKRIECY EVNYQPLDDE LDSHLSYIKI FDVGTRYMVN RVQDHIQSRT
     VYYLMNIHVT PRSIYLCRHG ESELNLRGRI GGDSGLSARG KQYAYALANF IQSQGISSLK
     VGTSHMKRTI QTAEALGLPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF ALRDQDKYRY
     RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL LAYFLDKSSD ELPYLKCPLH
     TVLKLTPVAY GCKVESIYLN VEAVNTHREK PENVDITREP EEALDTVPAH Y
//

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