ID A0A316YXJ3_9BASI Unreviewed; 734 AA.
AC A0A316YXJ3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Bifunctional 6-phosphofructo-2-kinase/fructose-2,6-bisphosphate 2-phosphatase {ECO:0000313|EMBL:PWN92793.1};
GN ORFNames=FA10DRAFT_263545 {ECO:0000313|EMBL:PWN92793.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN92793.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN92793.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN92793.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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DR EMBL; KZ819634; PWN92793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316YXJ3; -.
DR STRING; 215250.A0A316YXJ3; -.
DR InParanoid; A0A316YXJ3; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000245768; 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 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 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 Kinase {ECO:0000313|EMBL:PWN92793.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000245768};
KW Transferase {ECO:0000313|EMBL:PWN92793.1}.
FT DOMAIN 270..496
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 503..510
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 554
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 734 AA; 79804 MW; 0042E7ECB1BD22A2 CRC64;
MSEQQRQNTQ SPPIPSTTTT SSSKPGSRDG TPTAKRASSI DSQQQRNRAG NSPLVPLTRL
PPSSSPLTSN AAFSATSSTL PGTVSTTATA TVSSSRGATV VPPSAGTISP SSESGRLARS
SSLHSSRSSR LSNSSVTSSP PTFAQAGRHM SHGGQTRPVP QPTSTQKDMF DQAVASSNLA
SSSEGLQALL RDHPELVSSS LSRAAGPGWS ELSESTRGSR GGSQPGTPGE EGGNEGHILK
DAPHVGEGGA SQSVTPSNAP NLGSTGAKPD YSGEKIVVAM VGLPARGKSY LSNKLMRYLR
WLEYDVKVFN VGQLRRALAK AKLKESGQKE DHTATFFDPH NPAAFKLRTQ MAEECLEQLI
GWLKRGGNVG IHDATNSSRK RRAAIAQRIA KEPDLKLIFL ESLCTDPQVI AANIAVKVSS
GDPDYAGMSP EAAKEDFLKR IKHYEETYES VDAHGDEKDL SYCKITDVGR SVVVNEIHGY
LESRIAFYLM NLHLTPRNIF FSRHGESQYN VEGKIGGDSD LSERGWAYAK ALPQLVKDAV
GDAPLTVWHS TLKRTGQTAS FLPYPKLAWK SLDELDAGVC DAMTYEEIER FYPEDYASRD
EDKFNYRYRG GESYRDVVVR LEPIIMELER QENILIIGHQ AILRALYAYF HALGQDDLPY
IKIPLHTLLE LTPAAFGTRE RRFKAPIEAV NTHRDKPAPR EKISQPPSPA LDPMEEAATS
KPPSQLDPDA QRPE
//
