ID   F4P400_BATDJ            Unreviewed;       521 AA.
AC   F4P400;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=6-phosphofructo-2-kinase domain-containing protein {ECO:0000259|Pfam:PF01591};
GN   ORFNames=BATDEDRAFT_11914 {ECO:0000313|EMBL:EGF79713.1};
OS   Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS   fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC   Rhizophydiales incertae sedis; Batrachochytrium.
OX   NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF79713.1, ECO:0000313|Proteomes:UP000007241};
RN   [1] {ECO:0000313|EMBL:EGF79713.1, ECO:0000313|Proteomes:UP000007241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA   Stajich J., Eisen M., Grigoriev I.V.;
RT   "The draft genome of Batrachochytrium dendrobatidis.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL882885; EGF79713.1; -; Genomic_DNA.
DR   RefSeq; XP_006679351.1; XM_006679288.1.
DR   AlphaFoldDB; F4P400; -.
DR   STRING; 684364.F4P400; -.
DR   GeneID; 18236632; -.
DR   HOGENOM; CLU_006383_6_1_1; -.
DR   InParanoid; F4P400; -.
DR   OMA; RWIQERC; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000007241; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IBA:GO_Central.
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   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.
PE   4: Predicted;
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007241}.
FT   DOMAIN          64..292
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  59081 MW;  7E3A2F8ECE5355F7 CRC64;
     MEQLSHSTFV ADTAKPSQES PSNPSLIIAT DSTASHSAPC TSESISSSRP KPNVDTSKPT
     SVEPAAPSCK LACVMVGLPA RGKTYIARKV ARYLTWLGHR SRLFNVGAYR RDAIGVAQPS
     SFFDPSNEDH SRKRMELAMV ALDDMLNWLD DDTTSDGVET TGEFACVAMY DATNSTIERR
     SLIAQRCRER GVDVMFVESI CEDEQLIMAN IREVKISSPD YKDTDPKKAI EDFQHRIKFY
     EQTYETLHPS ELDNRIAFAK LINVGNQVIV NRIRGYIHSR IVYFLMNLNT TPRSFYFSRH
     GESMFNVSQR IGGDSDLSWR GAQFAKKLPD IIQQNLGKET QLTIWTSTLR RTQQTAQHLN
     FPKVQWKQLD EIDSGLCDGL TYAEIELKYP ADFAERDTDK FNYRYHGGES YRDLVHRLEP
     VILELERHHE PNHSILIIGH QAVLRCVYAY FLNISHEELP YIKVPLHTVV KLTPKAYGCE
     EERFALDIAA VDTHRERPAR STIGTTPGSD KSHGEMPPTS R
//