ID A0A151TGX9_CAJCA Unreviewed; 520 AA.
AC A0A151TGX9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=KK1_012599 {ECO:0000313|EMBL:KYP66311.1};
OS Cajanus cajan (Pigeon pea) (Cajanus indicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Cajanus.
OX NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP66311.1, ECO:0000313|Proteomes:UP000075243};
RN [1] {ECO:0000313|EMBL:KYP66311.1, ECO:0000313|Proteomes:UP000075243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX PubMed=22057054; DOI=10.1038/nbt.2022;
RA Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT of resource-poor farmers.";
RL Nat. Biotechnol. 30:83-89(2012).
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; CM003608; KYP66311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151TGX9; -.
DR STRING; 3821.A0A151TGX9; -.
DR OMA; SNSRMWH; -.
DR OrthoDB; 995926at2759; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000075243; Chromosome 6.
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:SF23; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 5, CHLOROPLASTIC; 1.
DR Pfam; PF00365; PFK; 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:UP000075243};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03186}.
FT DOMAIN 165..467
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 292
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 236..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 261..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 290..292
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 335..337
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 443..446
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT SITE 263
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
SQ SEQUENCE 520 AA; 57001 MW; EB3BE1C61CF31597 CRC64;
MGTLSHVITL HGLTSCSYAH SHSNPRFNTS LPTRVPRVFA KLKTQNSTAA IDFTDPYWKT
KFKDDFQQRF RLPHVTDIFP DAASVPSTFC PKKRTSDFPG NYPSDDDWHG YINDNDRVLL
KTIYYSSPTS AGAECIDPGC NWVEQWVHRA GPREKIYFKP EEVKAAIVTC GGLCPGLNDV
IRQIVITLEI YGVTKIVGIP FGYRGFSDKE LIEVPLSRKV VQNIHLSGGS LLGVSRGGPG
VSEIVNSLEE RGINMLFVLG GNGTHAGANA IHNECCKRRL QVSVIGVPKT IDNDILLMDK
TFGFDTAVEE AQRAINSAYI EAHSAYHGIG IVKLMGRDSG FIAMHASLAS GQIDICLIPE
IPFNLHGPSG VLSYLKYLIE TKGSAVVCVA EGAGQDLLQK TNATDASGNT VYRDIGVYTQ
QETKRYFKEI GVHADVKYID PTYMIRACRA NASDGIFCTV LGQNAVHGAF AGFSGITVGT
CNTHYAYFPI PEVISHPRLV DSNSRMWHRC LTATGQPDFI
//
