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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//