ID H2TID0_TAKRU Unreviewed; 456 AA.
AC H2TID0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-like {ECO:0000313|Ensembl:ENSTRUP00000024432.3};
GN Name=LOC115249212 {ECO:0000313|Ensembl:ENSTRUP00000024432.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000024432.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000024432.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000024432.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC mutase family. {ECO:0000256|ARBA:ARBA00008408}.
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DR AlphaFoldDB; H2TID0; -.
DR STRING; 31033.ENSTRUP00000077798; -.
DR Ensembl; ENSTRUT00000024531.3; ENSTRUP00000024432.3; ENSTRUG00000009725.3.
DR GeneTree; ENSGT00950000182835; -.
DR Proteomes; UP000005226; Chromosome 3.
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:SF78; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2, 6-BIPHOSPHATASE 1 ISOFORM X1; 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 Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 18..235
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT ACT_SITE 244
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 313
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 243..250
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 456 AA; 52604 MW; 129E2CB902A75204 CRC64;
MGCNLNSCVC APVFVSASVP QFCNSPTMIV MVGLPARGKT YISKKLTRYL NWIGVPTKMF
NVGQYRREAV KIYENFEFFK PDNEGAMRIR KACAAAALKD VAAYFTKEQG QVAVFDATNT
TRERRTIILT FAKERGYKVF FVESICDDPE IIAENIRQVK SGSPDYADRD VEEAMEDFIQ
RIECYKSSYM PIDDERDRKL SYIKIFNVGS RYLVNRVQDH IQSRIVYYLM NIHVTARSIY
LSRHGESELN LLGRIGGDSG LSPRGQKYAN ALATFIQGQN IRDLKVWTSH MKRTIQTAQS
LGVQYEQWKA LNEIDAGVCE ELTYEEIQEN FPEEFALRDQ DKYRYRYPKG ESYEDLVHRL
EPVIMELERQ ENVLVICHQA IMRCLLAYFL DKPADELPYL RCPLHTVLKL TPVAYGCKVE
PFFLNIEAVN THREKPVNVD INRNPEDALQ TVPEHI
//
