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Database: UniProt
Entry: A0A2G5I3W3_CERBT
LinkDB: A0A2G5I3W3_CERBT
Original site: A0A2G5I3W3_CERBT 
ID   A0A2G5I3W3_CERBT        Unreviewed;       539 AA.
AC   A0A2G5I3W3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Putative 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase {ECO:0000313|EMBL:PIA99448.1};
GN   ORFNames=CB0940_03068 {ECO:0000313|EMBL:PIA99448.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA99448.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA99448.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA99448.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:PIA99448.1}.
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DR   EMBL; LKMD01000101; PIA99448.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5I3W3; -.
DR   OrthoDB; 2013830at2759; -.
DR   Proteomes; UP000230605; Chromosome 3.
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; 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE; 1.
DR   PANTHER; PTHR10606:SF39; 6-PHOSPHOFRUCTO-2-KINASE_FRUCTOSE-2,6-BISPHOSPHATASE YLR345W-RELATED; 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   Kinase {ECO:0000313|EMBL:PIA99448.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000313|EMBL:PIA99448.1}.
FT   DOMAIN          45..264
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          481..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   539 AA;  60731 MW;  CA1DDACB0EBBD22B CRC64;
     MDTLLTADVA GSAPNFRRRS STYVDAIHDL PEKASMAPAQ LYSTESGRLF HSGRIVIATV
     GLPARGKTHI SVALARYLRW LGVKTHIFHL GDYRRAFVGA KGEVPEDYFH INASTSSVLL
     RNKILKRCRE DIFNFLNHEN GQIAIYDAVN PLATGRRALA KEFEKHGVQT MFIECTCSDP
     RIIEENVRAV KISSPDYVGW KPEDAVQDYL RRINARIPDY EGVEERDLHY VKMINAGERV
     IVNSCAFGYL SQRIVFYLLN LHIKSRQMYF VRAGTTREEE TFKGDASLSA EGWDYAKRMT
     DAIVAHRETE REMLIKNGAP ESTASKPLQV WTSTRKRTVE TATFFEKLGY RVRQRSQMSQ
     LNPGVCEKLS ERRIRELFPE EVDKHEQDPY HHRYPRAESY HDLAVRLEPI ILELEREQND
     LLIIAHESVL RVLYGYLMAC SAHDIPTLEF PRDEIIEVIP ASYNNSAKRI HIDGLPPSMI
     PSSPQDIQIP VPPSGAVSPL NGGLGTPAGI ATPETAGRES GALPIRPSAT LGETLQPRG
//
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