ID A0A340XNG5_LIPVE Unreviewed; 449 AA.
AC A0A340XNG5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 1 isoform X3 {ECO:0000313|RefSeq:XP_007460834.1};
DE SubName: Full=6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 1 isoform X4 {ECO:0000313|RefSeq:XP_007460835.1};
GN Name=PFKFB1 {ECO:0000313|RefSeq:XP_007460834.1,
GN ECO:0000313|RefSeq:XP_007460835.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007460834.1};
RN [1] {ECO:0000313|RefSeq:XP_007460834.1, ECO:0000313|RefSeq:XP_007460835.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC {ECO:0000256|ARBA:ARBA00003771}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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_007460834.1; XM_007460772.1.
DR RefSeq; XP_007460835.1; XM_007460773.1.
DR GeneID; 103073042; -.
DR CTD; 5207; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000265300; Unplaced.
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; 2.
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:SF15; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE 1; 1.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 2.
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 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:UP000265300};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 74..229
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 428..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 237
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 306
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 236..243
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 449 AA; 51962 MW; 33C1CD1E1F04FE9F CRC64;
MSREMGELTQ TRLQKIWIPH NGGNSRLQRR RGSSIPQFTN SPTMVIMVGL PARGKTYIST
KLTRYLNWIG TPTKDNMEAL LIRKQCAIAA LKDVHNYLSC EEGHVAVFDA TNTTRERRSL
ILQFAKEHGY KVFFIESICN DPDVIAENIR QVKLGSPDYI DCDRENVLGD FLKRIECYEV
NYQPLDDELD SHLSYIKIFD VGTRYMVNRV QDHIQSRTVY YLMNIHVTPR SIYLCRHGES
ELNLRGRIGG DSGLSARGKQ YAYALANFIQ SQGISSLKVW TSHMKRTIQT AEALVVPYEQ
WKALNEIDAG VCEEMTYEEI QKHYPEEFAL RDQDKYRYRY PKGESYEDLV QRLEPVIMEL
ERQENVLVIC HQAVMRCLLA YFLDKSSEEL PYLRCPLHTV LKLTPVAYGC KVESIYLNVE
AVNTHREKPE NVNVSREPEE ALDTVPAHY
//
