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Database: UniProt
Entry: A0A2Y9NSL2_DELLE
LinkDB: A0A2Y9NSL2_DELLE
Original site: A0A2Y9NSL2_DELLE 
ID   A0A2Y9NSL2_DELLE        Unreviewed;       526 AA.
AC   A0A2Y9NSL2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 3 isoform X1 {ECO:0000313|RefSeq:XP_022435936.1};
GN   Name=PFKFB3 {ECO:0000313|RefSeq:XP_022435936.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022435936.1};
RN   [1] {ECO:0000313|RefSeq:XP_022435936.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022435936.1};
RG   RefSeq;
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   RefSeq; XP_022435936.1; XM_022580228.2.
DR   AlphaFoldDB; A0A2Y9NSL2; -.
DR   STRING; 9749.A0A2Y9NSL2; -.
DR   Ensembl; ENSDLET00000020708; ENSDLEP00000018785; ENSDLEG00000013561.
DR   KEGG; dle:111177981; -.
DR   InParanoid; A0A2Y9NSL2; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:SF41; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE 3; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; His_Phos_1; 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:UP000248483};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          26..246
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          443..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        254
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        323
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         253..260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   526 AA;  60344 MW;  16E3B1DAAE1AF0D0 CRC64;
     MPLELTQSRV QKIWIPVDHR PSLPRSCGPK LTNSPTVIVM VGLPARGKTY ISKKLTRYLN
     WIGVPTKVFN VGEYRREAVK QYSSYNFFRP DNEEAMKVRK QCALAALRDV KSYLTKEGGQ
     IAVFDATNTT RERRHMILHF AKENDFKVFF IESVCDDPTV VASNIMEVKI SSPDYKDCNS
     AEAMDDFMKR INCYEASYQP LDPDKCDRDL SLIKVIDVGR RFLVNRVQDH IQSRIVYYLM
     NIHVQPRTIY LCRHGESEHN LQGKIGGDSG LSSRGRKFAS ALSKFVEEQN LKDLRVWTSQ
     LKSTIQTAEA LQLPYEQWKA LNEIDAGVCE EMTYEEIKDT YPEEYALREQ DKYYYRYPTG
     ESYQDLVQRL EPVIMELERQ ENVLVICHQA VLRCLLAYFL DKSAEEMPYL KCPLHAVLKL
     TPVAYGCRVE SIYLNVESVS THRERSEDAK KGPNPLMRRN SVTPLASPEP TKKPRINSFE
     EHVASTSAAL PTCLPPEVPT QLPGQPLLGK ACLRTVCHIF SKFSPY
//
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