PFKA_LEIDO
ID PFKA_LEIDO Reviewed; 486 AA.
AC Q9BIC6;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03186};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03186};
DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_03186};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03186};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03186};
GN Name=pfk {ECO:0000255|HAMAP-Rule:MF_03186};
OS Leishmania donovani.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5661;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP LYS-224.
RC STRAIN=LSB-51.1;
RX PubMed=12180974; DOI=10.1046/j.1432-1033.2002.03086.x;
RA Lopez C., Chevalier N., Hannaert V., Rigden D.J., Michels P.A.,
RA Ramirez J.L.;
RT "Leishmania donovani phosphofructokinase. Gene characterization,
RT biochemical properties and structure-modeling studies.";
RL Eur. J. Biochem. 269:3978-3989(2002).
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:0000255|HAMAP-Rule:MF_03186,
CC ECO:0000269|PubMed:12180974}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03186, ECO:0000269|PubMed:12180974};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03186};
CC -!- ACTIVITY REGULATION: Allosterically activated by AMP.
CC {ECO:0000255|HAMAP-Rule:MF_03186, ECO:0000269|PubMed:12180974}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.157 mM for fructose 6-phosphate {ECO:0000269|PubMed:12180974};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_03186}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03186}.
CC -!- SUBCELLULAR LOCATION: Glycosome {ECO:0000255|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:0000255|HAMAP-Rule:MF_03186}.
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; AY029213; AAK31633.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9BIC6; -.
DR SMR; Q9BIC6; -.
DR VEuPathDB; TriTrypDB:LdBPK_292620.1; -.
DR VEuPathDB; TriTrypDB:LdCL_290032300; -.
DR VEuPathDB; TriTrypDB:LDHU3_29.3880; -.
DR SABIO-RK; Q9BIC6; -.
DR UniPathway; UPA00109; UER00182.
DR GO; GO:0020015; C:glycosome; 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 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 Pfam; PF00365; PFK; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Glycolysis; Glycosome; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Peroxisome; Transferase.
FT CHAIN 1..486
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000429721"
FT MOTIF 484..486
FT /note="Peroxisomal targeting signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT ACT_SITE 227
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 171..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 196..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 197
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 225..227
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 270..272
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 378..381
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT SITE 198
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT MUTAGEN 224
FT /note="K->G: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:12180974"
SQ SEQUENCE 486 AA; 53988 MW; DCBABC2C464C3651 CRC64;
METRHHLNTK MVPSYQAPLS KVTAADLTVE RLPGCKYMNP SKKHILREEY RDKVKHIMYD
PRPQEDLDAE YPVSCNKLVC ELAAARKHLH FNPSETSIGI VTCGGICPGL NDVIRSITLT
GIISYRVKRV VGFRYGYWGL SKEGSKTAIE LSRSDVRQIH RFGGTILGSS RGPQNPKEMV
DTLVRMKINI LFTVGGDGTQ RGALTIYEEA KRPGENIAVF GVPKTIDNDL AFSHRTFGFQ
TAVEQAVNAV RAAYAEAVSL NYGVGIVKLM GRESGFIAAQ TTVASAQANI CLIPENPLPK
ETVMRLIERR LQQSRNCVIV VAEGFGQDWE TGTGGHDASG NKKLVDIGFI LKKEVESWLR
ANKEKFPQGT VKYIDPSYMI RACPPSSNDA LFCTNLATLA VHEAMAGATG CIISMRYNNY
ILVPIKAATS VRRVVSLRGA LWRQVREITV GLSDDVQQWN EQDLRRHLES LNVERERIIA
RLASKV
