ID X0CHE7_FUSOX Unreviewed; 698 AA.
AC X0CHE7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=6-phosphofructo-2-kinase {ECO:0000313|EMBL:EXK93845.1};
GN ORFNames=FOQG_05038 {ECO:0000313|EMBL:EXK93845.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK93845.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK93845.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK93845.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JH658368; EXK93845.1; -; Genomic_DNA.
DR AlphaFoldDB; X0CHE7; -.
DR eggNOG; KOG0234; Eukaryota.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:SF32; 6-PHOSPHOFRUCTO-2-KINASE 1; 1.
DR PANTHER; PTHR10606; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR Pfam; PF01591; 6PF2K; 2.
DR Pfam; PF00300; His_Phos_1; 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 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EXK93845.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Transferase {ECO:0000313|EMBL:EXK93845.1}.
FT DOMAIN 171..224
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT DOMAIN 273..439
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 698 AA; 78145 MW; 88490C0F9C5DB03D CRC64;
MPSAIPVAPA GRRQSKQSGL LKSVMHNLLG VSPPSPALPA QQTSSNSLPP TSNPSSNPTS
NPTSDPSSNP NNPNNYAVLP PPADGDHDHL PPPANAPSSL AVALRSLNDL TETPTYARSV
TSTAPSSPRI PPLRQNSGHQ TPRVRPHATT LNIPGMTRSR VSPDGRIPSR DVAAKLVIVM
VGLPARGKSY ITKKLQRYLS WQQHDSRIFN VGNRRRVAAG RRVSVHPKLQ PEPEHMDPPV
HAASILLNGN PAPFGPEQAE PEKLDLNDAA QSEVDQSATF FDPKNQTAAA MREQCAMDTL
DELLDYLLDG GGAVGILDAT NSTIERRKNI TNRIKQREPK LGILFIESIC QDPTLLEANM
RLKLSGPDYR DKDPQKSLED FKKRVAAYES AYVPLGEYEE KHDLQYIQMI DVGRKLIQHR
LKGFLSSGIS TYLASFNLAP RQIWITRHGQ SVDNELGRLG GNSPLTERGH CYGQALHNFI
TYQRKHWLIE QKSKKAQATF PPVPGDNTPP YPEMYREIED KNFCVWTSML DRSVDTAEYF
EADDDYDVKN WEMLNEMNSG QFEGMTYAEI AQKEPEEFAK RAQDKLNYIY PGVGGEGYLQ
VVSRLRDMVR EVERIEDHLL IIGHRSVCRV LMAYFMDLSL ADITDMDIPL GMLYSIEPKP
YGLDFHAYRY NEDQGWFDEL PNYKPTKTAR NSIIKPQH
//
