ID A0A3B6I283_WHEAT Unreviewed; 441 AA.
AC A0A3B6I283;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
GN ORFNames=CFC21_054669 {ECO:0000313|EMBL:KAF7045577.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS4A02G387000.1};
RN [1] {ECO:0000313|EMBL:KAF7045577.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7045577.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS4A02G387000.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS4A02G387000.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS4A02G387000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7045577.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7045577.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CM022220; KAF7045577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6I283; -.
DR EnsemblPlants; TraesCS4A02G387000.1; TraesCS4A02G387000.1; TraesCS4A02G387000.
DR Gramene; TraesCAD_scaffold_045841_01G000300.1; TraesCAD_scaffold_045841_01G000300.1; TraesCAD_scaffold_045841_01G000300.
DR Gramene; TraesCS4A02G387000.1; TraesCS4A02G387000.1; TraesCS4A02G387000.
DR Gramene; TraesCS4A03G0964800.1; TraesCS4A03G0964800.1.CDS; TraesCS4A03G0964800.
DR Gramene; TraesPAR_scaffold_036639_01G000700.1; TraesPAR_scaffold_036639_01G000700.1; TraesPAR_scaffold_036639_01G000700.
DR OMA; RACTANA; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000019116; Chromosome 4A.
DR Proteomes; UP000815260; Chromosome 4A.
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:SF27; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 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|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW 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:UP000019116};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03186}.
FT DOMAIN 86..388
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 157..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 182..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 211..213
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 256..258
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 364..367
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT SITE 184
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
SQ SEQUENCE 441 AA; 48011 MW; 7C38E8FB762BD633 CRC64;
MQHFLSNATY YHSARTPTGD EDSTPMDMWN GYVNNDDRAL MKVIKYSSPT SAGAECIDPD
CSWVEQWVHR AGPRKDIYYE PNEVKAAIVT CGGLCPGLND VIRQVVFTLE TYGVKNIVGI
PFGFRGFFEK GLKEMPLSRN LVENINLAGG SFLGVSRGGP KTSEIVDSIQ ARRIDMLFVL
GGNGTHAGAN AIHDECRKRK LKVSVVAVPK TIDNDIPLMD KTFGFDTAVE EAQRAINSAY
IEARSAYHGI GLVKLMGRSS GFIAMHASLS SGQVDVCLIP EVSFALDGEY GVLQHLEQLI
KNKGFCVVCV AEAAGQELLQ NSGATDASGN AILSDIGVHM QQKIKTHFKG IGVHADIKYI
DPTYMVRACR ANASDAILCT VLGQNAVHGA FAGFSGITSC ICNTHYVYLP VTQVITAPKR
VNHKGRMWHR CLTSTGQPDF R
//
