ID A0A2P5EIR4_TREOI Unreviewed; 763 AA.
AC A0A2P5EIR4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Fructose-2,6-bisphosphatase {ECO:0000313|EMBL:PON85439.1};
GN ORFNames=TorRG33x02_187190 {ECO:0000313|EMBL:PON85439.1};
OS Trema orientale (Charcoal tree) (Celtis orientalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Trema.
OX NCBI_TaxID=63057 {ECO:0000313|EMBL:PON85439.1, ECO:0000313|Proteomes:UP000237000};
RN [1] {ECO:0000313|Proteomes:UP000237000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-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:PON85439.1}.
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DR EMBL; JXTC01000147; PON85439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5EIR4; -.
DR STRING; 63057.A0A2P5EIR4; -.
DR InParanoid; A0A2P5EIR4; -.
DR OrthoDB; 2013830at2759; -.
DR Proteomes; UP000237000; 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:2001070; F:starch binding; IEA:InterPro.
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; 2.60.40.10; Immunoglobulins; 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; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR013783; Ig-like_fold.
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; PF00686; CBM_20; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM01065; CBM_2; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000237000}.
FT DOMAIN 29..136
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 576
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 649
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 575..582
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 627
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 763 AA; 84534 MW; B5B78018D54A660D CRC64;
MGTGSSKDTE GGSHGREGEG EGERENLDQG GGGQLYVSLK MENYKLKGDL IPHVYGSVPL
IGSWDSSKAL SMERESASMW ELSFVVPPNH ETLDFKFLLK PKYTNTPCVV EEGPNRQLIG
GTLQGDARLA LFKLNGDDGL EYRVFIKADR VSPFDLAASW RAYQENLRPS AVRGIPDVSI
DSVPQTGAEN GSSASLELDL EHYVVPAPST CANSGLVYAA NMTETPRSLT LSGVFSKSDG
ASSAAHSFKD GGGVSVDRPS PIREMEVVVP DPTKVYLSSG MVESKSVGTL SPLQKQDSHR
GLFVDRGVGS PRLVKSSSAS TFSFDLKLDT ETKNSMPAAS GAVAAAAIAD QMLGPKEDRH
LAIVLVGLPA RGKTFTAAKL TRYLRWLGHD TKHFNVGKYR RLKHGANQSA DFFRADNPEG
IEARNEVAAL AFDDMVSWMQ EGGQVGVFDA TNSTRKRRNM LMKMAEGKCK IIFLETICND
ERIIERNIRL KIQQSPDYAE EPDFEAGLRD FKTRLTNYEK VYEPVEEGSY IKMIDMVSGH
GGQIQVNNIS GYLPGRIVFF LVNTHLTPRP ILLTRHGESR DNVRGRIGGD TALSDAGELY
AKKLSNFVEK RLKSERAASI WTSTLQRTIL TASHIGGGFP KIQWRALDEI YAGVCDGMTY
EEIKKNMPEE YEARKKDKLR YRYPRGESYL DVIQRLEPVI IELERQRAPV VVISHQAVLR
ALYAYFADRP LKEIPHIEIP LHTIIEIQMG VTGVQEKRYK LMD
//
