ID A0A1E1LFU0_9HELO Unreviewed; 640 AA.
AC A0A1E1LFU0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Probable 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 {ECO:0000313|EMBL:CZT09406.1};
GN ORFNames=RCO7_07389 {ECO:0000313|EMBL:CZT09406.1};
OS Rhynchosporium commune.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Ploettnerulaceae; Rhynchosporium.
OX NCBI_TaxID=914237 {ECO:0000313|EMBL:CZT09406.1, ECO:0000313|Proteomes:UP000178129};
RN [1] {ECO:0000313|EMBL:CZT09406.1, ECO:0000313|Proteomes:UP000178129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UK7 {ECO:0000313|EMBL:CZT09406.1,
RC ECO:0000313|Proteomes:UP000178129};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FJUW01000050; CZT09406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E1LFU0; -.
DR STRING; 914237.A0A1E1LFU0; -.
DR InParanoid; A0A1E1LFU0; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000178129; 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; 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 Kinase {ECO:0000313|EMBL:CZT09406.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000178129};
KW Transferase {ECO:0000313|EMBL:CZT09406.1}.
FT DOMAIN 111..165
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT DOMAIN 219..383
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 479
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 640 AA; 71530 MW; B9674C6D25897165 CRC64;
MAANSPLENI TTSITLPHPS YNSPSLLAPP TICSLGRALQ SLDMNSPTSQ NGSSPGVDTP
EASNPSTANG SPRLRPVRQN SGTVTPRIRP PATTLNIPGM TRSRVSPDGK IAQRDVGAKL
VVIMVGLPAR GKSYITKKLH RYLSWQQYDC EIFNVGSRRR TAAGPQSPPQ SPEKTSSICR
TGSLAEVVDA PTQAAHILLN GHYSGEDPND LSKLPSADTM EQSAQFFDPK NAKASQLREQ
VALSTLDELL DFLLNEGGSV GILDATNSTI ERRQILFKAI KEREPKLGIL FIESVCEDEK
LLEANMHLKL KGPDYKDKDP ESSLADFKKR VAAYESAYVP LGKFEEDNNM QYIKMIDVGR
KVIHFRLQGF LAGGIASYLS TFNLSPRQIW ITRHGQSQDN LAGKIGGDSE LTDAGRNYAT
VLYNFVSKKR AEWEIDQKER ALTEAALPMQ AGDQTPPYPD ILGELEEKNF CVWTSMLQRS
IQTAECFQDD ENYDVKNWEM LKELDAGSFE GMTYEDIQEK FPEQYAKRRA DKLSYIYPGV
GGEGYLQVIS RLRDMVREIE RIKDHVLIIG HRSVCRVLMA YFMDLTRDDI ADMDVPLGML
FAIEPKPYGI EFHAYKYNPN EYVFEELPNY KPQKAIGHTN
//
