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Database: UniProt
Entry: A0A178ES21_TRIRU
LinkDB: A0A178ES21_TRIRU
Original site: A0A178ES21_TRIRU 
ID   A0A178ES21_TRIRU        Unreviewed;       471 AA.
AC   A0A178ES21;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Fructose-2,6-bisphosphatase {ECO:0000313|EMBL:OAL62515.1};
GN   ORFNames=A7C99_7101 {ECO:0000313|EMBL:OAL62515.1};
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL62515.1, ECO:0000313|Proteomes:UP000243015};
RN   [1] {ECO:0000313|EMBL:OAL62515.1, ECO:0000313|Proteomes:UP000243015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA   Zhan P., Tao Y., Liu W.;
RT   "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL   Submitted (MAY-2016) 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:OAL62515.1}.
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DR   EMBL; LHPM01000019; OAL62515.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178ES21; -.
DR   VEuPathDB; FungiDB:TERG_03775; -.
DR   OMA; RWIQERC; -.
DR   Proteomes; UP000243015; 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:UP000243015}.
FT   DOMAIN          36..249
FT                   /note="6-phosphofructo-2-kinase"
FT                   /evidence="ECO:0000259|Pfam:PF01591"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        257
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        333
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         256..263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   471 AA;  53236 MW;  7F3A3F7C5357C3EE CRC64;
     MAAPVKASSA YHPCPEESPA AHDGKHRTLE RLANNKKNDD AKICVVMVGL PARGKSLIAG
     KALRYLSWIG IPAKIFNVGQ YRRQDTPRPT AAFFDTSNPD GERLRRAAAE AAVTDMLHWF
     STTGGQVAIL DATNSTKERR KWIRDVCQSA GIEPLFVESK CDDRELIMNN IREVKTTSPD
     YVGQDPEVAA QDFMERISNY EKVYQTIEED EDVSYIQLIN VGTSVVINNI RDYLSSRLVY
     YTINLHIKPR SIWLSRHGES EFNLSGQIGG DANLSSRGEA YARALPSLLK ESGVPPGTKI
     VIWTSTLKRT IQTARFLQAE TGYDKLEWKA LDELDSGVCD GLTYEEIAER YPEDFKARDD
     DKYNYRYRGG ESYRDVVIRL EPIIMELERS ENVLIVTHQA VLRCIYSYFL NMSQEQSPWM
     EVPLHTLIKL TPRAYGTEEK RFKANIPAVS TWRGKGSSAK HQEPACQPVA K
//
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