ID M3XVT7_MUSPF Unreviewed; 472 AA.
AC M3XVT7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 {ECO:0000313|Ensembl:ENSMPUP00000003187.1};
GN Name=PFKFB1 {ECO:0000313|Ensembl:ENSMPUP00000003187.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000003187.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000003187.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-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 EMBL; AEYP01105459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01105460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01105461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3XVT7; -.
DR STRING; 9669.ENSMPUP00000003187; -.
DR Ensembl; ENSMPUT00000003252.1; ENSMPUP00000003187.1; ENSMPUG00000003220.1.
DR eggNOG; KOG0234; Eukaryota.
DR GeneTree; ENSGT00950000182835; -.
DR HOGENOM; CLU_006383_1_1_1; -.
DR InParanoid; M3XVT7; -.
DR OMA; GECYGMT; -.
DR GO; GO:0043540; C:6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex; IEA:Ensembl.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:Ensembl.
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: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; 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 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 34..252
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT ACT_SITE 260
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 329
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 259..266
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 472 AA; 54558 MW; 71CB73C925015B07 CRC64;
QTRTIGHLFQ DSSVTGGIPR GCKTTYVNSE LSASIPQFTN SPTMLIMVGL PARGKTYIST
KLTRYLNWIG TPTKVFNLGQ YRREAVSYKN YEFFLPDNME ALHIRKQCAL AALKDVHDYL
SHEEGHVAVF DATNTTRERR SLILQFAKEH GYKVFFIESI CNDPGIIAEN IRQVKLGSPD
YIDCDREKVL EDFLKRIECY EVNYQPLDDE RWPSHLSYIK IFDVGTRYTV NRVQDHIQSR
TVYYLMNIHV TPRSIYLCRH GESELNLRGR IGGDSGLSAR GKQYAYALAN FIQSQGISSL
KVWTSHMKRT IQTAEALGVP YEQWKALNEI DAGVCEEMTY EEIQEHYPEE FALRDQDKYR
YRYPKGESYE DLVQRLEPVI MELERQENVL VICHQAVMRC LLAYFLDKSS DELPYLKCPL
HTVLKLTPVA YGCKVESIYL NVEAVNTHRE KPENVDITRE PEEALDTVPA HY
//
