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Database: UniProt
Entry: A0A091GJ15_9AVES
LinkDB: A0A091GJ15_9AVES
Original site: A0A091GJ15_9AVES 
ID   A0A091GJ15_9AVES        Unreviewed;       418 AA.
AC   A0A091GJ15;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 4 {ECO:0000313|EMBL:KFO82360.1};
DE   Flags: Fragment;
GN   ORFNames=N303_08642 {ECO:0000313|EMBL:KFO82360.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO82360.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO82360.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO82360.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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; KL448312; KFO82360.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091GJ15; -.
DR   STRING; 55661.A0A091GJ15; -.
DR   Proteomes; UP000053760; 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; 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, ECO:0000313|EMBL:KFO82360.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFO82360.1}.
FT   DOMAIN          3..217
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   ACT_SITE        225
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        294
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         224..231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO82360.1"
FT   NON_TER         418
FT                   /evidence="ECO:0000313|EMBL:KFO82360.1"
SQ   SEQUENCE   418 AA;  48521 MW;  4282512267701DD7 CRC64;
     VCMTNCPTLI VMVGLPARGK TYISKKLTRY LNWIGVPTKE FNVGQYRRDL VKKYKSFEFF
     LPDNEEGLKI RKQCALAALN DVRQYLSEEN GHVAVFDATN TTRERRETIY KFGEENGYKT
     FFVESVCVDP EVIAANIVQV KLGSPDYVDC SNDEATEDFM KRIECYKNSY ETLDETLDKD
     LSYIKIMDVG RSYLVNRVMD HIQSRIVYYL MNIHVTPRSI YLCRHGESEL NLKGRIGGDP
     GLSVRGKEFA KSLAQFINEQ NIKDLKVWTS QMKRTIQTAE ALGVPYEQWK VLNEIDAGVC
     EEMTYEEIQE NYPLEFALRD QDKYRYRYPK GESYEDLVQR LEPVIMELER QENVLVICHQ
     AVMRCLLAYF LDKPAEQLPY LKCPLHTVLK LTPVAYGCKV ESIFLNVEAV NTHRDKPE
//
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