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Database: UniProt
Entry: F2TE17_AJEDA
LinkDB: F2TE17_AJEDA
Original site: F2TE17_AJEDA 
ID   F2TE17_AJEDA            Unreviewed;       702 AA.
AC   F2TE17;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=6-phosphofructo-2-kinase {ECO:0000313|EMBL:EGE81480.1};
GN   ORFNames=BDDG_04422 {ECO:0000313|EMBL:EGE81480.1};
OS   Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS   dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE81480.1};
RN   [1] {ECO:0000313|EMBL:EGE81480.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE81480.1};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Genome Sequencing Center for Infectious Disease.;
RA   Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG749426; EGE81480.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2TE17; -.
DR   HOGENOM; CLU_006383_3_1_1; -.
DR   Proteomes; UP000007802; 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; 2.
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   Kinase {ECO:0000313|EMBL:EGE81480.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000313|EMBL:EGE81480.1}.
FT   DOMAIN          122..175
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   DOMAIN          274..451
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..54
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   702 AA;  78639 MW;  D3AFF119565DF4A7 CRC64;
     MADHLTANGR HGPSNIHHSP EPSLMPPCKT VVGRALAPEH HHHHHHHHHQ HRSLSATHAP
     SQASRDGVGM ALTDTPLSTA PPSPQIGARS HSSGASTPGK HRATTLDIPG LTKSKVSPDG
     RIAQRDVGSK LVIVMVGLPA RGKSYITKKL ARYLNWMQHD TKIFNVGERR RVAAGGSVPS
     AGRSSIFEDE IRDSVREMSI SGSSSGRRDT EHEILPPAAI LLNGAAVESP TPQDQDGITR
     DPSPMSDMPY LYPKSKPASA SISSASLSPE PAIGTMRSTG AGSIDQSAQF FDPANEQAVQ
     LREQVALLTL DELLDYILEQ GGSIGILDAT NSTLKRRKAI MDRIRARAGP ELNVLFLESQ
     CLDKELLESN MRLKLSGPDY RDQDPTLALE DFKKRVALYE KSYVSLGEYE EKHNMPYVQT
     IDVSRKVIAH QVNGFLSSQV MYYLLNFNLS PRQIWICRHG ESLDNVAGRI GGDSPLSENG
     IRYARALTRF IGEQRQLWEQ YQKSKALSTH FPPRPGDSTP PNPQYAGQNA EPRNFCIWSS
     MLTRSIQTVQ FFDDEEYDVK QMRMLDELNA GKMEGMTYEE IRKQFPEEYA NRKRQKLHYR
     YPGPGGEGYL DVINRLKAVI VEVERMTDNV LLVSHRSVAR VLLAYFRGLK REELADLDVP
     LGVLYMLEPK PYGVEFKAYR YNPSTDWFDF MPNYELRQAS YY
//
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