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Database: UniProt
Entry: A0A3B0K700_DROGU
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ID   A0A3B0K700_DROGU        Unreviewed;       536 AA.
AC   A0A3B0K700;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Blast:6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 {ECO:0000313|EMBL:SPP89987.1};
GN   ORFNames=DGUA_6G020737 {ECO:0000313|EMBL:SPP89987.1};
OS   Drosophila guanche (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP89987.1, ECO:0000313|Proteomes:UP000268350};
RN   [1] {ECO:0000313|Proteomes:UP000268350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC       mutase family. {ECO:0000256|ARBA:ARBA00008408}.
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DR   EMBL; OUUW01000044; SPP89987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0K700; -.
DR   STRING; 7266.A0A3B0K700; -.
DR   OMA; RWIQERC; -.
DR   Proteomes; UP000268350; Unassembled WGS sequence.
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:SF44; 6-PHOSPHOFRUCTO 2-KINASE_FRUCTOSE 2,6-BISPHOSPHATASE LONG FORM; 1.
DR   PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 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   Kinase {ECO:0000313|EMBL:SPP89987.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000313|EMBL:SPP89987.1}.
FT   DOMAIN          73..285
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   ACT_SITE        293
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        378
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         292..299
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   536 AA;  60914 MW;  2FD1BD137C91E368 CRC64;
     MDMPYNTSPS LRVRTTSLNQ LKKTADLAIE NELHVCPSVM SEELRKLLPP TSETVMTKPF
     PIRGERTIAD CTTPHVIAMV GLPARGKTFI SKKLARYLNW IGIATRVFNL GEYRRHATTA
     YKSHEFFRAD NEEAMAIRNR CANQALHDSC EWLLSGQGSI AVFDATNSTR DRRQLIYNIV
     VKQHGFRLFF VESICDDPQI IEQNILEVKV SSPDYLNMNT ELVVRDFLQR IEHYEERYQP
     IDEVTESHLS FMKVYNAGKK VVVYNNEGHV ESRIVYYLMN IHITPRTIYL TRHGESEHNL
     SGLIGGDSNL SARGHQYGRA LSSFISQQHI DGLRVWTSWM KRAIQTVANV KAPQERWKAL
     NEIDAGHCEE MTYEQIKERF PEEFKARDVN KFAYRYPRGE SYEDLVARLE PVIMELERQG
     NVLVVSHQAV LRCLFAYFLD KSADELPYLY VPLHTVIKLT PVAYGCKVEH IKLPIDAVDT
     HRPKPKIPGD VSEPGLDGLS GELVAPDGVG KVLIVGDDVA TATNVNGARV DSQPNQ
//
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