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Database: UniProt
Entry: A0A384DSC9_URSMA
LinkDB: A0A384DSC9_URSMA
Original site: A0A384DSC9_URSMA 
ID   A0A384DSC9_URSMA        Unreviewed;       445 AA.
AC   A0A384DSC9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 1 isoform X3 {ECO:0000313|RefSeq:XP_008709903.1};
GN   Name=PFKFB1 {ECO:0000313|RefSeq:XP_008709903.1};
OS   Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008709903.1};
RN   [1] {ECO:0000313|RefSeq:XP_008709903.1}
RP   IDENTIFICATION.
RC   TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008709903.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC       {ECO:0000256|ARBA:ARBA00003771}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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_008709903.1; XM_008711681.2.
DR   AlphaFoldDB; A0A384DSC9; -.
DR   GeneID; 103682099; -.
DR   CTD; 5207; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000261680; Chromosome X.
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:SF15; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE 1; 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:UP000261680};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          8..228
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   ACT_SITE        236
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        305
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         235..242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   445 AA;  51763 MW;  4AB52C87DEE32A0C CRC64;
     MEEKTSRRTA SIPQFTNSPT MVIMVGLPAR GKTYISTKLT RYLNWIGTPT KVFNLGQYRR
     EAVSYKNYEF FLPDNMEALL IRKQCALAAL KDVHDYLSHE EGHVAVFDAT NTTRERRSLI
     LQFAKEHGYK VFFIESICND PGIIAENIRQ VKLGSPDYID CDREKVLEDF LKRIECYEVN
     YQPLDDELDS HLSYIKIFDV GTRYMVNRVQ DHIQSRTVYY LMNIHVTPRS IYLCRHGESE
     LNLRGRIGGD SGLSARGKQY AYALANFIQS QGISSLKVWT SHMKRTIQTA EALGVPYEQW
     KALNEIDAGV CEEMTYEEIQ EHYPEEFALR DQDKYRYRYP KGESYEDLVQ RLEPVIMELE
     RQENVLVICH QAVMRCLLAY FLDKSSDELP YLKCPLHTVL KLTPVAYGCK VESIYLNVEA
     VNTHREKPEQ EDIHLQARGR GFIRN
//
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