ID W6KTD8_9TRYP Unreviewed; 1022 AA.
AC W6KTD8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=6-phosphofructo-2-kinase domain-containing protein {ECO:0000259|Pfam:PF01591};
GN ORFNames=GSEM1_T00006701001 {ECO:0000313|EMBL:CCW65495.1};
OS Phytomonas sp. EM1.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Phytomonas.
OX NCBI_TaxID=479712 {ECO:0000313|EMBL:CCW65495.1, ECO:0000313|Proteomes:UP000027080};
RN [1] {ECO:0000313|EMBL:CCW65495.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EM1 {ECO:0000313|EMBL:CCW65495.1};
RA Genoscope - CEA;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW65495.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM1 {ECO:0000313|EMBL:CCW65495.1};
RX PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA Wincker P., Dollet M.;
RT "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL PLoS Genet. 10:e1004007-e1004007(2014).
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DR EMBL; HF955110; CCW65495.1; -; Genomic_DNA.
DR AlphaFoldDB; W6KTD8; -.
DR EnsemblProtists; CCW65495; CCW65495; GSEM1_T00006701001.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000027080; 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; 2.
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: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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000027080}.
FT DOMAIN 336..407
FT /note="6-phosphofructo-2-kinase"
FT /evidence="ECO:0000259|Pfam:PF01591"
FT REGION 120..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 855
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 1022 AA; 113695 MW; A818A5C2B2EE385C CRC64;
MSFSGLVPDD ICGASTVHPP PLAITVPAYH LEDPFPSRDD VPYPEEVHSP IINTTIIQKA
NYPTPEAARI AEKALRTAKT YYKLFFDAAE EKRGGERRES KKARCVAETP MVEFPAAIPN
HTRAEKCNGA PSTNDHKAAS EDSDEGSSPL QVHDTLYHTF FPPKLSKRQR EAITRRIIGR
EPRPFSKFVW RKLSPRWEGS GSPGGRALLA MPKLSFTTSP RPSLPSPAAD ASLGWGEEGE
GGRASLLPRF TARERDQDGA KPPSSSSPGF PTMEGTLSSM EGPEWAAPRR DFRALATVDP
AREAACGRVL DRSTYTIPAS QQGPEYFSRH VRESGGKTLI VVMVGLPARG KTFLAQKICR
LLGWQGTRAK VMNVQVAWSE VVRRWEAAQA SAAASTRPPP TDAQPKRSTS SASSASSFPL
GSSSVGRGES GTASETTSWR SGRAHRGNSN STTTTTTAPL RFSAPAFHNA VSDPHLRHAA
NDIDDSVLME AFGIGPGAGA AGSLELPQAA GAGRAKPAEK DAILEERERE KEREKTKETE
KKVDGRGAYL RVDHFRRLLC EPEGVERGIY RDVLACFAED CREFFSQGGQ VVLINDDFVT
EEMRREVERL FRPLAEHYMY MEVLRDEGVS RRFNVCKVRD PREYPRDFIS RRDAMRDFEK
RTRLLKSLYE PLEDGAAANT STPTTPFSPP SRCYLKVRNS NVIESHGLSG YLASRIVFFA
MNLSQTRMQH PIYFIRHGES CYNLENRVGG NPLLTEQGMR DASALLEFLS SLKTHLRRID
ALRQRYRRRK RRHRAEKARE VEAERQGAEE RRGKGGAIAV GSRETTSEDS TAPPLARPRR
SRTHTLELWT SQLQRAIQTA ELAERLLNLP TLRWSRLNEI HAGVCEGMTY AEVLAQYPLI
DTFRRKSKYT FRYPDGESYQ DLVARLEPII LELENTDRVV VVVAHQAVLR CLLAYFGSTS
AQSSVCLPVP HRTVWRCGYD SKGIASLEEL RLDDSTAGLP PGRLDFANPT EPHDENPLNG
AT
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