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Database: UniProt
Entry: A0A087YEE1_POEFO
LinkDB: A0A087YEE1_POEFO
Original site: A0A087YEE1_POEFO 
ID   A0A087YEE1_POEFO        Unreviewed;       528 AA.
AC   A0A087YEE1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 46.
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:ENSPFOP00000016394.2};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000016394.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000016394.2}
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   EMBL; AYCK01002406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_016524400.1; XM_016668914.1.
DR   AlphaFoldDB; A0A087YEE1; -.
DR   STRING; 48698.ENSPFOP00000016394; -.
DR   Ensembl; ENSPFOT00000016416.2; ENSPFOP00000016394.2; ENSPFOG00000016271.2.
DR   GeneID; 103134638; -.
DR   CTD; 564852; -.
DR   eggNOG; KOG0234; Eukaryota.
DR   GeneTree; ENSGT00950000182835; -.
DR   OMA; RWIQERC; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
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:UP000028760};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          28..249
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         257..264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   528 AA;  61187 MW;  52EC1A465EFF699F CRC64;
     MSCTQRDIGA STNSTEAKRT DPRCNEKKCS WASYMTNSPT MIVMIGLPAR GKTYMSKKLT
     RYLNWIGVPT KVFNLGVYRR EAVRAYKSYD FFRHDNEEAM KIRKQCALVA LQDVRVYLTE
     EGGQIAVFDA TNTTRERRDL IQAFVKENGF KVFFVESVCD DPDVIAANIL EVKVSSPDYP
     EKHRERVMED FLKRIECYKV TYQPLDPDDY DKDLSFIKVI NVGQRFLVNR VQDYIQSKIV
     YYLMNIHVHS HSIYLCRHGE SNHNVEGRIG GDSELSPRGK KFAHALRDFI EEYELSDLKV
     WTSQLRRTIQ TAEELSVPYE QWKILNEIDA GVCEEMTYQM IQETFPEEFA LRDQDKYHYR
     YPGGESYQDL VQRLEPVIME LERQGNVLVI CHQAVMRCLL AYFLDKGADD LPYMKCPLHT
     VLKLTPVAYG CKVEMFYLNV EAVNTHRDRP LGKVPRDSAL IHRRNSYTPL SSYDQVKRPR
     LYSAGNQPWL PLAPTPSALM PERLQSQDSL CEGIDFDSSE ETSGCVRF
//
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