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Database: UniProt
Entry: W5NAZ7_LEPOC
LinkDB: W5NAZ7_LEPOC
Original site: W5NAZ7_LEPOC 
ID   W5NAZ7_LEPOC            Unreviewed;       480 AA.
AC   W5NAZ7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 {ECO:0000313|Ensembl:ENSLOCP00000017806.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000017806.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000017806.1}
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   EMBL; AHAT01014831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01014832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01014833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01014834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01014835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5NAZ7; -.
DR   STRING; 7918.ENSLOCP00000017806; -.
DR   Ensembl; ENSLOCT00000017838.1; ENSLOCP00000017806.1; ENSLOCG00000014458.1.
DR   eggNOG; KOG0234; Eukaryota.
DR   GeneTree; ENSGT00950000182835; -.
DR   InParanoid; W5NAZ7; -.
DR   OMA; RCLMGYF; -.
DR   Proteomes; UP000018468; Linkage group LG5.
DR   Bgee; ENSLOCG00000014458; Expressed in muscle tissue and 13 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IBA:GO_Central.
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:UP000018468};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          46..260
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          457..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        268
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        337
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         267..274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   480 AA;  55371 MW;  B6FB1C79A5471168 CRC64;
     PVGTDQPPPA AMASPRELTQ NPLKKIWMPC KNGLPEAHSS QRKVCMTNCP TLIVTVGLPA
     RGKTYISKKL TRYLNWIGVP TKEFNVGQYR RECVKIYKSF EFFRPDNEEG LKIRKQCALA
     ALKDVRGYLS EEGGQVAVFD ATNTTRERRD TIVTFAEQNG YKVFFVESVC EDPEVIAANI
     VQVKLSSPDY TDCNTEEAVE DFMKRIKCYE NSYQTLDEVL DRELSYIKIM DVGRRYLVNR
     VLDHIQSRIV YYLMNIHITP RSIYLCRHGE SELNVKGRIG GDSGLSLRGK QFAKCLAKFI
     QDQNIKDLKV WTSQMKRTIQ TAEALGVPYE QWKALNEIDA GVCEEMMYEE IQEHYPLEFA
     LRDQDKYRYR YPKGESYEDL VQRLEPVIME LERQENVLVI CHQAVMRCLL AYFLDKSADE
     LPYLKCPLHT VLKLTPVAYG CRVESISLNV EAVNTHRDRP EKVHVDRSRE DALQTVPPHL
//
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