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Database: UniProt
Entry: A0A2D0PK25_ICTPU
LinkDB: A0A2D0PK25_ICTPU
Original site: A0A2D0PK25_ICTPU 
ID   A0A2D0PK25_ICTPU        Unreviewed;       469 AA.
AC   A0A2D0PK25;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=pfkfb2b {ECO:0000313|RefSeq:XP_017306372.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017306372.1};
RN   [1] {ECO:0000313|RefSeq:XP_017306372.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017306372.1};
RG   RefSeq;
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   RefSeq; XP_017306372.1; XM_017450883.3.
DR   AlphaFoldDB; A0A2D0PK25; -.
DR   GeneID; 108255158; -.
DR   CTD; 564852; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000221080; Chromosome 21.
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   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          16..237
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   BINDING         245..252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         295
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   469 AA;  54100 MW;  660F1C42FFC9B444 CRC64;
     MCDEAKRAEP RANGKQCSWA SYMTNSPTLI VMIGLPARGK TYMSKKLTRY LNWIGVPTKV
     FNLGVYRREA VKAYKSYDFF RHDNQEAMKI RKKCALVALQ DVKAYLNEEG GQIAVFDATN
     TTRERRDLIL NFVKENAYKV FFVESVCDDP DVIAANILEV KVSSPDYPES HRERVMDDFL
     KRIECYKVTY QPLDPDDYDK DLSFIKVMNV GRRFLVNRIQ DYIQSKIVYY LMNIRVHSHC
     IYLCRHGESD HNTQGRIGGD AELSSRGKQF AAALRAFIEE HGLSDLKVWT SQLRRSIQTA
     EALGVPYEQW KILNEIDAGV CEEMTYEMIQ NSFPEEFALR DQDKYHYRYP GGESYQDLVQ
     RLEPVIMELE RQGNVLVICH QAVMRCLLAY FLDKNADDLP YLKCPLHTVL KLTPVAYGCK
     VEMFYLNVEA VNTHRDRPLL RVSGSFLNPC VKESSLKAQK TPLTVSASE
//
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