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Database: UniProt
Entry: A0A093PE49_9PASS
LinkDB: A0A093PE49_9PASS
Original site: A0A093PE49_9PASS 
ID   A0A093PE49_9PASS        Unreviewed;       437 AA.
AC   A0A093PE49;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 4 {ECO:0000313|EMBL:KFW74686.1};
DE   Flags: Fragment;
GN   ORFNames=N305_08630 {ECO:0000313|EMBL:KFW74686.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW74686.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW74686.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW74686.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-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; KL668904; KFW74686.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093PE49; -.
DR   STRING; 328815.ENSMVIP00005019058; -.
DR   Proteomes; UP000053258; 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:KFW74686.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053258};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFW74686.1}.
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:KFW74686.1"
FT   NON_TER         437
FT                   /evidence="ECO:0000313|EMBL:KFW74686.1"
SQ   SEQUENCE   437 AA;  50575 MW;  E85CD924D89E2B9A CRC64;
     VCMTNCPTLI VMVGLPARGK TYISKKLTRY LNWIGVPTKE FNVGQYRRDL VKKYKSFEFF
     LPDNEEGLKI RRQCALAALN 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 NTHRDKPENV
     DISRPPEDAL VTVPGHQ
//
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