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Database: UniProt
Entry: A0A3P9A885_ESOLU
LinkDB: A0A3P9A885_ESOLU
Original site: A0A3P9A885_ESOLU 
ID   A0A3P9A885_ESOLU        Unreviewed;       452 AA.
AC   A0A3P9A885;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 {ECO:0000313|Ensembl:ENSELUP00000037228.2};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000037228.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000037228.2, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000037228.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A3P9A885; -.
DR   Ensembl; ENSELUT00000026554.2; ENSELUP00000037228.2; ENSELUG00000016845.2.
DR   GeneTree; ENSGT00950000182835; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000265140; LG17.
DR   Bgee; ENSELUG00000016845; Expressed in bone element and 15 other cell types or tissues.
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:SF14; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE 4; 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:UP000265140};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          18..232
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   BINDING         239..246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   452 AA;  52344 MW;  D45A6ED4F9A89329 CRC64;
     MWEERSYPFY QLELNLCMTN CPTLIVTVGL PARGKTYISK KLTRYLNWIG VPTKEFNVGQ
     YRRECVKIYK SFEFFNPSNE EGLKIRRQCA LTALNDVRQY LSVEGGQVAV FDATNTTRER
     RGTITRFADQ NGFKVFFVES VCEDPDVIAE NIVQVKLGSP DYIDCNTEEA MEDFMKRIKC
     YENSYQPLDE ILDRDLSYIK IMDVGRRYLV NRVLDHIQSR IVYYLMNIHI TPRAIYLCRH
     GESDLNVKGR IGGDSGLSSR GKEFAKCLGK FIQGQNITDL KVWTSQMKRT IQTAEAIAVP
     YEQWKALNEI DAGVCEEMMY EEIQGHFPLE FALRDQDKYR YRYPKGESYE DLVQRLEPVI
     MELERQENVL VICHQAVMRC LLAYFLDKSA EELPYLKCPL HTVLKLTPVA YGCKVESVCL
     NVEAVNTHRD KPDNVDPSRM PEEALLTVPA HQ
//
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