ID M7U666_BOTF1 Unreviewed; 706 AA.
AC M7U666;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative 6-phosphofructo-2-kinase protein {ECO:0000313|EMBL:EMR82088.1};
GN ORFNames=BcDW1_9364 {ECO:0000313|EMBL:EMR82088.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR82088.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
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DR EMBL; KB708057; EMR82088.1; -; Genomic_DNA.
DR AlphaFoldDB; M7U666; -.
DR STRING; 1290391.M7U666; -.
DR HOGENOM; CLU_006383_3_1_1; -.
DR Proteomes; UP000012045; 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: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.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EMR82088.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000313|EMBL:EMR82088.1}.
FT DOMAIN 158..228
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT DOMAIN 281..448
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 94..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 545
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 706 AA; 79367 MW; 81EE522548D45855 CRC64;
MDSVSTNAPL AAEYRRQSQL SQIAKAAVFN NCTAMNPPPK PSSQPLTSFP GNTILERDFA
VCNPQLDNHI TLPPSVIPPV FNRSFHEKFG MTSDGVTEGV GHPLSDTPLP SGPSTAQSSP
RILPLRQNSG TTTPRVRAPA TTLNIPGMTR SRVSPDGKIA QRDVASKLVV IMVGLPARGK
SYITKKIQRY LSWQQHETRI FNVGNRRRVA AGKPRPSNGT PLKNQESAHR PSVQSQPIRT
GSNSGIIDAP TQAAHMILNG VDPTQETKGS ATKKTSTQSQ NPETMDQSAN FFDPLNSKAA
LIREQVAMAT LDELLDFLLL GNGAVGILDA TNSTIERRKL LFDHVKFREP KLGILFIESV
CEDESLLEAN MRLKLRGPDY KDKDPESSLR DFKLRVAAYE SAYVPLGKYE EDNHMQYIKM
IDVGRKVVHY QLKGFLTGGI ASYLSTFNLS PRQIWITRHG KSNDNKVGKL GGDSDLTEEG
QQYARVLHSF ITNSRRQWLF EQQQSAIESA KYPPGGEAVR TPPYPDIMGE LDEKNFCVWT
SMLQRSIQTA EHFEMDEDYD VKNWEMLNEL NAGSFEGLTY KEIESRFPDE YGKRAKDKLH
YIYPGVGGEG YLQVISRLRD MVRELERITD HVLIIGHRSV ARVLMAYFMD LTRDDIADLD
VPLGMLYAIE PKPYGIEFHA YRYNEQQQWF DELPNYKPRK ETEKGN
//