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Database: UniProt
Entry: X6M5M9_RETFI
LinkDB: X6M5M9_RETFI
Original site: X6M5M9_RETFI 
ID   X6M5M9_RETFI            Unreviewed;       355 AA.
AC   X6M5M9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Diphosphate--fructose-6-phosphate 1-phosphotransferase {ECO:0000313|EMBL:ETO09298.1};
DE   Flags: Fragment;
GN   ORFNames=RFI_28089 {ECO:0000313|EMBL:ETO09298.1};
OS   Reticulomyxa filosa.
OC   Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC   Reticulomyxidae; Reticulomyxa.
OX   NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO09298.1, ECO:0000313|Proteomes:UP000023152};
RN   [1] {ECO:0000313|EMBL:ETO09298.1, ECO:0000313|Proteomes:UP000023152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24332546;
RA   Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA   Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA   Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT   "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL   Curr. Biol. 0:0-0(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC         1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC         Evidence={ECO:0000256|ARBA:ARBA00000628};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETO09298.1}.
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DR   EMBL; ASPP01024158; ETO09298.1; -; Genomic_DNA.
DR   AlphaFoldDB; X6M5M9; -.
DR   EnsemblProtists; ETO09298; ETO09298; RFI_28089.
DR   OrthoDB; 5475590at2759; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000023152; Unassembled WGS sequence.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.450; -; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   PANTHER; PTHR43650; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE; 1.
DR   PANTHER; PTHR43650:SF1; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT BETA 1; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023152};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ETO09298.1}.
FT   DOMAIN          94..325
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   REGION          64..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..94
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         355
FT                   /evidence="ECO:0000313|EMBL:ETO09298.1"
SQ   SEQUENCE   355 AA;  39288 MW;  1DEF22FA17161453 CRC64;
     MTDETLLGKL RREFVPRIPK SLEHLEKLKF ETGEKTKSIS NQKEISGLFP LTYGQPLLHL
     AHSDEEKSLE HSPPPIAYKN TKKKKKKKKK KTNSGQASGG HNVITGLFDA LKHLNGESTM
     IGFLDGPIGV IQNKYIKIDK NVVDEYRNTG GFDMIRSGRD KIETSQQQES ALKSVVSHDL
     NGLVIIGGDD SNTNAAVLAE YFASQKCKCV PKTIDGDLQN EYIEMSFGFD TAVKTYSEMI
     SNICRDAKSA AKSWHFIKLM GRDASHVTLD CALQTHVNIT LIGEEVEKQD LLLHDIADHM
     ADVIATRQAK GKDYGIVLIP EGIISFIPSM KALIGELSSL LKKGSSHLKA LDERP
//
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