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Database: UniProt
Entry: F7B5I1_ORNAN
LinkDB: F7B5I1_ORNAN
Original site: F7B5I1_ORNAN 
ID   F7B5I1_ORNAN            Unreviewed;       488 AA.
AC   F7B5I1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2 {ECO:0000256|ARBA:ARBA00040487};
DE            EC=2.7.1.105 {ECO:0000256|ARBA:ARBA00012130};
DE            EC=3.1.3.46 {ECO:0000256|ARBA:ARBA00013067};
DE   AltName: Full=6PF-2-K/Fru-2,6-P2ase heart-type isozyme {ECO:0000256|ARBA:ARBA00041796};
GN   Name=PFKFB2 {ECO:0000313|Ensembl:ENSOANP00000004242.2};
OS   Ornithorhynchus anatinus (Duckbill platypus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX   NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000004242.2, ECO:0000313|Proteomes:UP000002279};
RN   [1] {ECO:0000313|Ensembl:ENSOANP00000004242.2, ECO:0000313|Proteomes:UP000002279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000004242.2,
RC   ECO:0000313|Proteomes:UP000002279};
RX   PubMed=18464734; DOI=10.1038/nature06936;
RA   Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA   Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA   Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA   Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA   Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA   Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA   Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA   Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA   Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA   Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA   Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA   Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA   Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA   Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA   Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA   Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA   Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA   Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA   de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT   "Genome analysis of the platypus reveals unique signatures of evolution.";
RL   Nature 453:175-183(2008).
RN   [2] {ECO:0000313|Ensembl:ENSOANP00000004242.2}
RP   IDENTIFICATION.
RC   STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000004242.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC       {ECO:0000256|ARBA:ARBA00003771}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC       mutase family. {ECO:0000256|ARBA:ARBA00008408}.
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DR   AlphaFoldDB; F7B5I1; -.
DR   STRING; 9258.ENSOANP00000004242; -.
DR   Ensembl; ENSOANT00000004243.3; ENSOANP00000004242.2; ENSOANG00000002661.3.
DR   eggNOG; KOG0234; Eukaryota.
DR   GeneTree; ENSGT00950000182835; -.
DR   OMA; RWIQERC; -.
DR   TreeFam; TF313541; -.
DR   Proteomes; UP000002279; Chromosome 7.
DR   Bgee; ENSOANG00000002661; Expressed in testis and 8 other cell types or tissues.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR   PANTHER; PTHR10606:SF48; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE 2; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          2..216
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          412..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         223..230
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   488 AA;  56233 MW;  8759B951517337E0 CRC64;
     MTNSPTLIVM IGLPARGKTY VSKKLTRYLN WIGVPTKVFN LGVYRRQAVK SYKSYDFFRH
     DNKEAMKIRK QCALVALEDV KAYFTDDGGQ IAVFDATNTT RERRDLILNF AQENAFKVFF
     VESVCDDPDV IAANILEVKV SSPDYPERNR ENVMEDFLKR IECYKVTYQP LDPDNYDKDL
     SFIKVMNVGQ RFLVNRVQDY IQSKIVYYLM NIHVQPRTIY LCRHGESQFN LSGKIGGDSG
     LSPRGKQFAQ ALRKFLEEQE ITDLKVWTSQ LKRTIQTAES LGVTYEQWKI LNEIDAGVCE
     EMTYEDIAKQ YPEEFALRDQ EKYLYRYPGG ESYQDLVQRL EPVIMELERQ GNVLVISHQA
     VMRCLLAYFL DKSADELPYL HCPLHTIFKL TPVAYGCKVE VIKLNVEAVN THRDKPTNSH
     PKNQTPVRMR RNSFTPLSSS ESIKRPRNYS VGSRPLKPFG PLRSLDPQEG ADQPKTQVSI
     PVTARLAI
//
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