ID A0A0E0DF53_9ORYZ Unreviewed; 478 AA.
AC A0A0E0DF53;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03186};
DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03186};
DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03186};
DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03186};
DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03186};
GN Name=PFK {ECO:0000256|HAMAP-Rule:MF_03186};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI04G13430.1};
RN [1] {ECO:0000313|EnsemblPlants:OMERI04G13430.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI04G13430.1};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI04G13430.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000256|HAMAP-Rule:MF_03186}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000432, ECO:0000256|HAMAP-
CC Rule:MF_03186};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_03186};
CC -!- ACTIVITY REGULATION: Allosterically activated by AMP.
CC {ECO:0000256|HAMAP-Rule:MF_03186}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000256|HAMAP-Rule:MF_03186}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03186}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03186}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X'
CC sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_03186}.
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DR AlphaFoldDB; A0A0E0DF53; -.
DR STRING; 40149.A0A0E0DF53; -.
DR EnsemblPlants; OMERI04G13430.1; OMERI04G13430.1; OMERI04G13430.
DR EnsemblPlants; OMERI04G13430.3; OMERI04G13430.3; OMERI04G13430.
DR EnsemblPlants; OMERI04G13430.4; OMERI04G13430.4; OMERI04G13430.
DR Gramene; OMERI04G13430.1; OMERI04G13430.1; OMERI04G13430.
DR Gramene; OMERI04G13430.3; OMERI04G13430.3; OMERI04G13430.
DR Gramene; OMERI04G13430.4; OMERI04G13430.4; OMERI04G13430.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_020655_7_3_1; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000008021; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.450; -; 1.
DR HAMAP; MF_01981; Phosphofructokinase_II_X; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR012004; PyroP-dep_PFK_TP0108.
DR PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR PANTHER; PTHR45770:SF9; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 2; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000534; PPi_PFK_TP0108; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03186};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03186};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03186};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_03186};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03186};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03186};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03186}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03186};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03186}.
FT DOMAIN 111..421
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 184..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 209..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 238..240
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 283..285
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 397..400
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT SITE 211
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
SQ SEQUENCE 478 AA; 51415 MW; 7086A51A502BB97B CRC64;
MDPTAPNSGD ANGGAAADAT APSNTTVTLP PLTLRDVPLL PSAAAAATDP IPNPISRHPY
FHPPATFYIS PGDVSLRHAF FDLASASPFP LVAYRRAGPR AGVAVDPARA RAAVVTCGGL
CPGLNTVLRE LVVGLRELYG VRDVFGVAAG YRGFYGPDAD HVRLDPAAVD DWHKKGGTVL
KTTRGGFDLN KIVDGIVARG YTQVYAIGGD GTMRGAVAIF NEFKRRGLNI SITGIPKTVD
NDIGIIDRSF GFQTAVEIAQ QAIDAAHVEA VSAVNGIGLV KLMGRSTGHI ALHATLSSRD
VDCCLIPEVD FYLEGKGGLF EFLYERIKQK GHAVVVVAEG AGQELIPRTD DQKREQDESG
NVVFLDVGPW LKSELGKWWK REHPSELFTV KYIDPTYMIR AVPANATDNL YCTLLAHSAI
HGIMAGYTGF VPGPINGNYS YIPLEDVAVA KNPVDVNDHK WAWVRSVTNQ PDFMKPKY
//