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Database: UniProt
Entry: A0A0E0DF53_9ORYZ
LinkDB: A0A0E0DF53_9ORYZ
Original site: A0A0E0DF53_9ORYZ 
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
//
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