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Database: UniProt
Entry: A0A2K5VWX8_MACFA
LinkDB: A0A2K5VWX8_MACFA
Original site: A0A2K5VWX8_MACFA 
ID   A0A2K5VWX8_MACFA        Unreviewed;       484 AA.
AC   A0A2K5VWX8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 28.
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:ENSMFAP00000029297.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000029297.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000029297.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000029297.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A2K5VWX8; -.
DR   Ensembl; ENSMFAT00000003493.2; ENSMFAP00000029297.2; ENSMFAG00000041915.2.
DR   VEuPathDB; HostDB:ENSMFAG00000041915; -.
DR   GeneTree; ENSGT00950000182835; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   Bgee; ENSMFAG00000041915; Expressed in heart and 13 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..484
FT                   /note="6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
FT                   2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030051817"
FT   DOMAIN          10..228
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          424..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        236
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        305
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         235..242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   484 AA;  56183 MW;  39121942DCD760DF CRC64;
     MLFHFLLAWA SYMTNSPTLI VMIGLPARGK TYVSKKLTRY LNWIGVPTKV FNLGVYRREA
     VKSYKSYDFF RHDNEEAMKI RKQCALVALE DVKAYLTEEN GQIAVFDATN TTRERRDMIL
     NFAEQNSFKV FFVESVCDDP DVIAANILEV KVSSPDYPER NRENVMEDFL KRIECYKVTY
     RPLDPDNYDK DLSFIKVINV GQRFLVNRVQ DYIQSKIVYY LMNIHVQPRT IYLCRHGESE
     FNLLGKIGGD SGLSVRGKQF AQALRKFLAE QEITDLKVWT SQLKRTIQTA ESLGVPYEQW
     KILNEIDAGV CEEMTYAEIE KRYPEEFALR DQEKYLYRYP GGESYQDLVQ RLEPVIMELE
     RQGNVLVISH QAVMRCLLAY FLDKGADELP YLRCPLHTIF KLTPVAYGCK VETIKLNVEA
     VNTHRDKPTN NFPKNQTPVR MRRNSFTPLS SSNTIRRPRN YSVGSRPLKP LSPLRAQDLQ
     EGAD
//
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