ID O64983_SPIOL Unreviewed; 750 AA.
AC O64983;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase {ECO:0000313|RefSeq:XP_021849695.1};
DE SubName: Full=Fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase {ECO:0000313|EMBL:AAC18055.1};
DE EC=2.7.1.105 {ECO:0000313|EMBL:AAC18055.1};
DE EC=3.1.3.46 {ECO:0000313|EMBL:AAC18055.1};
GN Name=LOC110789345 {ECO:0000313|RefSeq:XP_021849695.1};
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562 {ECO:0000313|EMBL:AAC18055.1};
RN [1] {ECO:0000313|EMBL:AAC18055.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:AAC18055.1};
RX PubMed=11856361; DOI=10.1046/j.1432-1033.2002.02771.x;
RA Markham J.E., Kruger N.J.;
RT "Kinetic properties of bifunctional 6-phosphofructo-2-kinase/fructose-2,6-
RT bisphosphatase from spinach leaves.";
RL Eur. J. Biochem. 269:1267-1277(2002).
RN [2] {ECO:0000313|Proteomes:UP001155700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Sp75 {ECO:0000313|Proteomes:UP001155700};
RX PubMed=28537264; DOI=10.1038/ncomms15275;
RA Xu C., Jiao C., Sun H., Cai X., Wang X., Ge C., Zheng Y., Liu W., Sun X.,
RA Xu Y., Deng J., Zhang Z., Huang S., Dai S., Mou B., Wang Q., Fei Z.,
RA Wang Q.;
RT "Draft genome of spinach and transcriptome diversity of 120 Spinacia
RT accessions.";
RL Nat. Commun. 8:15275-15275(2017).
RN [3] {ECO:0000313|RefSeq:XP_021849695.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF041848; AAC18055.1; -; mRNA.
DR PIR; T08994; T08994.
DR RefSeq; XP_021849695.1; XM_021994003.1.
DR STRING; 3562.O64983; -.
DR KEGG; soe:110789345; -.
DR OrthoDB; 2013830at2759; -.
DR BRENDA; 2.7.1.105; 5812.
DR BRENDA; 3.1.3.46; 5812.
DR Proteomes; UP001155700; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IBA:GO_Central.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Hydrolase {ECO:0000313|EMBL:AAC18055.1};
KW Kinase {ECO:0000313|EMBL:AAC18055.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP001155700};
KW Transferase {ECO:0000313|EMBL:AAC18055.1}.
FT DOMAIN 25..130
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 563..570
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 615
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 750 AA; 83375 MW; F8691FD4BFBECE0D CRC64;
MGAGTSKNSD STSHGDGDGE ERDEYEGGGQ LYVSLKMENY TLNADLLPHV FGSASLVGSW
DSSRALPLER ESTSMWQLSF VVPPNHETLD FKFLLRPKDS NNPCIIEEGP NRILSGGRLQ
GDARAALFRL NADAVLEYRV CINADRISPF DLASSWRAYQ ENIHPSTVRG ILDVSMNSET
CFESSSSANL ELDLERYVVP SPATSATSGL VYPANLAETP RYISARKYSS ESDFSKSGDT
GSQPIGPTAD KEMEVKIQDL AKVSTTSAAV EDKLATTASP TQKQESHKGV FVDRGVGSPR
LVKSTSAGTF ADDVKLGSGN KTAMPAAAGA VAAAAVADQM LGPKEDRHLA IVLVGLPARG
KTFTAAKLTR YLRWLGHDTK HFNVGKYRRL KLGTNQSAEF FRGDNTEGIE ARNEVAALAM
EDMISWMQEG GQVGIFDATN STRERRNMLM KLAEGNCKII FLETLCYDER IIERNIRLKV
QQSPDYAEQP DFEAGYRDFK RRLDNYEKVY EPVEEGSYIK MIDTVSGNGG QIQVNNISGY
LPGRIVFFLV NTHLTPRPIL LTRHGESQDN VRARIGGDSS LSDTGELYAK KLANFVEKRL
KPERAASIWT STLHRSISTA NHIVGFPKVQ WRALDEINAG ACDGMTYLEI KMDMPEEYES
REKDKLRYRY PRGESYLDVI QRLEPVIIEL ERQRAPVVVI SHQAVLRALY AYFADRPLKE
IPHIEVPLHT IIEIQMGVTG VQEKRYKLMD
//
