(data stored in ACNUC4932 zone)

HOVERGEN: F262_PONAB

ID   F262_PONAB              Reviewed;         530 AA.
AC   Q5NVT1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   01-SEP-2009, entry version 19.
DE   RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2;
DE   AltName: Full=PFK-2/FBPase-2;
DE   AltName: Full=6PF-2-K/Fru-2,6-P2ASE heart-type 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=PFKFB2;
OS   Pongo abelii (Sumatran orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate
CC       (By similarity).
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 the activation of
CC       the kinase activity (By similarity).
CC   -!- SUBUNIT: Homodimer (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; CR925919; CAI29582.1; -; mRNA.
DR   RefSeq; NP_001127057.1; -.
DR   UniGene; Pab.12002; -.
DR   SMR; Q5NVT1; 38-451.
DR   GeneID; 100174086; -.
DR   CTD; 100174086; -.
DR   HOVERGEN; Q5NVT1; -.
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...; IEA:EC.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR016260; Bifunct_6PFK/fruc_bisP_Ptase.
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.
PE   2: Evidence at transcript level;
DR   PRODOM; Q5NVT1.
DR   SWISS-2DPAGE; Q5NVT1.
KW   ATP-binding; Hydrolase; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   CHAIN         1    530       6-phosphofructo-2-kinase/fructose-2,6-
FT                                biphosphatase 2.
FT                                /FTId=PRO_0000345129.
FT   NP_BIND      45     52       ATP (Potential).
FT   REGION        1    248       6-phosphofructo-2-kinase.
FT   REGION      249    530       Fructose-2,6-bisphosphatase.
FT   ACT_SITE    128    128       Potential.
FT   ACT_SITE    158    158       Potential.
FT   ACT_SITE    257    257       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    326    326       Potential.
FT   ACT_SITE    391    391       Proton donor (By similarity).
FT   BINDING     102    102       Fructose-6-phosphate (By similarity).
FT   BINDING     193    193       Fructose-6-phosphate (By similarity).
FT   MOD_RES      29     29       Phosphoserine; by PKA (By similarity).
FT   MOD_RES     466    466       Phosphoserine; by PKA (By similarity).
FT   MOD_RES     468    468       Phosphothreonine (By similarity).
FT   MOD_RES     475    475       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES     483    483       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine (By similarity).
SQ   SEQUENCE   530 AA;  61168 MW;  B279884ABFB8780E CRC64;
     MSGASSSEQN NNSYETKPPN LRMSEKKCSW ASYMTNSPTL IVMIGLPARG KTYVSKKLTR
     YLNWIGVPTK VFNLGVYRRE AVKSYKSYDF FRHDNEEAMK IRKQCALVAL EDVKAYLTEE
     NGQIAVFDAT NTTRERRDMI LNFAEQNSFK VFFVESVCDD PDVIAANILE VKVSSPDYPE
     RNRENVMEDF LKRIECYKVT YRPLDPDNYD KDLSFIKVIN VGQRFLVNRV QDYIQSKIVY
     YLMNIHVQPR TIYLCRHGES EFSLLGKIGG DSGLSVRGKQ FAQALRKFLE EQEITDLKVW
     TSQLKRTIQT AESLGVPYEQ WKILNEIDAG VCEEMTYAEI EKRYPEEFAL RDQEKYLYRY
     PGGESYQDLV QRLEPVIMEL ERQGNVLVIS HQAVMRCLLA YFLDKGADEL PYLRCPLHTI
     FKLTPVAYGC KVETIKLNVE AVNTHRDKPT NNFPKNQTPV RMRRNSFTPL SSSNTIRRPR
     NYSVGSRPLK PLSPLRAQDM QEGPTSRRPK SHSGWCTVCF PPALASCPCH
//

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