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Database: UniProt
Entry: A0A1S3WTJ2_ERIEU
LinkDB: A0A1S3WTJ2_ERIEU
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ID   A0A1S3WTJ2_ERIEU        Unreviewed;       448 AA.
AC   A0A1S3WTJ2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 1 isoform X3 {ECO:0000313|RefSeq:XP_016049650.1};
GN   Name=PFKFB1 {ECO:0000313|RefSeq:XP_016049650.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016049650.1};
RN   [1] {ECO:0000313|RefSeq:XP_016049650.1}
RP   IDENTIFICATION.
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_016049650.1; XM_016194164.1.
DR   AlphaFoldDB; A0A1S3WTJ2; -.
DR   STRING; 9365.ENSEEUP00000011485; -.
DR   GeneID; 103125956; -.
DR   CTD; 5207; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000079721; Unplaced.
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:UP000079721};
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   448 AA;  52038 MW;  6BAFDF492A14EEE9 CRC64;
     MEEKVSRRKA SIPQFTNSPT MVIMVGLPAR GKTYISTKLT RYLNWIGTPT KVFNLGQYRR
     EAVNYKNYEF FLPDNMEALH IRKQCALAAL KDVHDFLSQG EGHVAVFDAT NTTRERRSMI
     LQFAKQHSYK AFFIESICND PGIIAENIKQ VKLSSPDYID CDQEKVLEDF LKRIECYATN
     YQPLDDELDS HLSYIKIFDV GMRYLVNRLQ DHIQSRTVYY LMNIHVTPRS IYLCRHGESE
     LNLRGRIGGD SGLSARGKQY SYALANFIQS QDINSLKVWT SHMKRTIQTA EALGVPYEQW
     KALNEIDAGV CEEMTYEEIQ EHYPEEFALR DQDKYRYRYP KGESYEDLVQ RLEPVIMELE
     RQENVLVICH QAVMRCLLAY FLDKNSGELP YLKCPLHTVL KLTPVAYGCK VESIYLNVEA
     INTHREKPEN VDITRESEEA LDTVPAHY
//
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