ID A0A2Y9JUD8_ENHLU Unreviewed; 535 AA.
AC A0A2Y9JUD8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=LOC111150996 {ECO:0000313|RefSeq:XP_022364386.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022364386.1};
RN [1] {ECO:0000313|RefSeq:XP_022364386.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022364386.1};
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_022364386.1; XM_022508678.1.
DR AlphaFoldDB; A0A2Y9JUD8; -.
DR STRING; 391180.A0A2Y9JUD8; -.
DR KEGG; elk:111150996; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000248482; 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; 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:UP000248482};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 29..251
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 REGION 447..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258..265
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 535 AA; 61427 MW; 5220BD70A696055C CRC64;
MSGNTASSSE QNNNSYETKA SNLRMSEKKC SWASYMTNSP TLIVMIGLPA RGKTYVSKKL
TRYLNWIGVP TKVFNLGVYR REAVKSYKSY DFFRHDNEEA MKIRKQCALV ALEDVKAYLT
EESGQIAVFD ATNTTRERRD MILSFAKENS FKVFFVESVC DDPDVIAANI LEVKVSSPDY
PERNRENVME DFLKRIECYK VTYQPLDPDN YDKDLSFIKV INVGQRFLVN RVQDYIQSKI
VYYLMNIHVQ PRTIYLCRHG ESEFNLLGKI GGDSGLSVRG KQFAQALRKF LEEQEIADLK
VWTSQLKRTI QTAESLGVTY EQWKILNEID AGVCEEMTYA QIEKQYPDEF ALRDQEKYLY
RYPGGESYQD LVQRLEPVIM ELERQGNVLV ISHQAVMRCL LAYFLDKGAD ELPYLRCPLH
TIFKLTPVAY GCKVETIKLN VEAVNTHRDK PTNNFPKNQT PVRMRRNSFT PLSSSNTVRR
PRNYSVGSRP LKPLSPLRAL DTQEGADQPK TQVLKGSAQA ADHPQMLWGL QVDVG
//
