ID A0A395RG83_FUSSP Unreviewed; 442 AA.
AC A0A395RG83;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Fructose-2,6-bisphosphatase {ECO:0000313|EMBL:RGP59116.1};
GN ORFNames=FSPOR_11559 {ECO:0000313|EMBL:RGP59116.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP59116.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP59116.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP59116.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP59116.1}.
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DR EMBL; PXOF01000235; RGP59116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395RG83; -.
DR STRING; 5514.A0A395RG83; -.
DR Proteomes; UP000266152; 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: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.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000266152}.
FT DOMAIN 11..225
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
SQ SEQUENCE 442 AA; 50646 MW; 6D2294E75AC7AA70 CRC64;
MPSRTNGVGV QAEDTRICVV MVGLPARGKS YIAQRAQRYL QWLSIPAQTF NVGNYRRNDA
PQPTADFFDI NNPEGERTRR AAAEAAVADM LAWFRSGGIV GILDATNSTL ERRKWVLEVC
NENGVEVLFV ESKCDDEELI MANIRDVKTT SPDYRGQDPE TAALDFRNRI RNYEKVYCTI
DADGKESHLT YLKIMDVGKQ VIISRIRDYL QSRIVYYLMN LHIRPRSVWL SRHGESLYNI
DGRIGGDTLL SPRGEQYARK LPELVRKSVG DDRPLTVWTS TLRRTIATAR FLPDHYNQLQ
WKALDELDSG VCDGLTYQEI KDRYPEDFAA RDEDKYNYRY RGGESYRDVV IRLEPIIMEL
ERSEDILIVT HQAVLRCIYA YFMKKDQSKS PWMNVPLHTL IKLTPGAYGT EEVRYEANIP
AVSTWRGKGS TAKHENPAPG VM
//
