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Database: UniProt
Entry: G5BP91_HETGA
LinkDB: G5BP91_HETGA
Original site: G5BP91_HETGA 
ID   G5BP91_HETGA            Unreviewed;       480 AA.
AC   G5BP91;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=6-phosphofructo-2-kinase/fructose-2, 6-biphosphatase 3 {ECO:0000313|EMBL:EHB11102.1};
DE   Flags: Fragment;
GN   ORFNames=GW7_20013 {ECO:0000313|EMBL:EHB11102.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB11102.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB11102.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC       mutase family. {ECO:0000256|ARBA:ARBA00008408}.
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DR   EMBL; JH171233; EHB11102.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5BP91; -.
DR   STRING; 10181.G5BP91; -.
DR   eggNOG; KOG0234; Eukaryota.
DR   InParanoid; G5BP91; -.
DR   Proteomes; UP000006813; 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:SF41; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE 3; 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:EHB11102.1};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHB11102.1}.
FT   DOMAIN          2..221
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          415..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..429
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        229
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        298
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         228..235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EHB11102.1"
FT   NON_TER         480
FT                   /evidence="ECO:0000313|EMBL:EHB11102.1"
SQ   SEQUENCE   480 AA;  55081 MW;  E85EB4FAF90335B2 CRC64;
     ACGPKLTNSP TVIVMVGLPA RGKTYISKKL TRYLNWIGVP TKVFNVGEYR REAVKQYSSY
     NFFRPDNEEA MKVRKQCALA ALRDVKSYLT KEGGQIAVFD ATNTTRERRH MILHFAKEND
     FKAFFIESVC DDPTVVASNI MEVKISSPDY KDCNSAEAMD DFMKRISCYE ASYQPLDPDK
     SDRDLSLIKV IDVGRRFLVN RVQDHIQSRI VYYLMNIHVQ PRTIYLCRHG ENEYNLQGKI
     GGDSGLSSRG KKFANALSKF VEEQNLKDLR VWTSQLKSTI QTAEALKLPY EQWKALNEID
     AGVCEELTYE EIRDTYPEEY VLREQDKYYY RYPTGESYQD LVQRLEPVIM ELERQENVLV
     ICHQAVLRCL LAYFLDKSAE EMPYLKCPLH TVLKLTPVAY GCRVESIYLN VESVSTHRER
     SEDAKKGPNP LMRRNSVTPL ASPEPTKKPR INSFEEHVAS TSAALPSYLP PEVPTQLPGQ
//
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