PFKA_TRYCC
ID PFKA_TRYCC Reviewed; 485 AA.
AC Q4E657;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, 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};
GN ORFNames=Tc00.1047053508153.340;
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener;
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
RN [2]
RP CATALYTIC ACTIVITY.
RX PubMed=2946951; DOI=10.1016/0166-6851(86)90013-7;
RA Aguilar Z., Urbina J.A.;
RT "The phosphofructokinase of Trypanosoma (Schizotrypanum) cruzi:
RT purification and kinetic mechanism.";
RL Mol. Biochem. Parasitol. 21:103-111(1986).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=CL Brener;
RX PubMed=19820836; DOI=10.1590/s0074-02762009000500014;
RA Rodriguez E., Lander N., Ramirez J.L.;
RT "Molecular and biochemical characterisation of Trypanosoma cruzi
RT phosphofructokinase.";
RL Mem. Inst. Oswaldo Cruz 104:745-748(2009).
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:19820836}.
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:19820836,
CC ECO:0000269|PubMed:2946951};
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}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.0125 mM for ATP {ECO:0000269|PubMed:19820836};
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 ECO:0000269|PubMed:19820836}.
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; AAHK01000001; EAO00202.1; -; Genomic_DNA.
DR RefSeq; XP_822053.1; XM_816960.1.
DR AlphaFoldDB; Q4E657; -.
DR SMR; Q4E657; -.
DR STRING; 5693.XP_822053.1; -.
DR ChEMBL; CHEMBL3108659; -.
DR PaxDb; Q4E657; -.
DR EnsemblProtists; EAO00202; EAO00202; Tc00.1047053508153.340.
DR GeneID; 3555118; -.
DR KEGG; tcr:508153.340; -.
DR eggNOG; KOG2440; Eukaryota.
DR OMA; YGHERFA; -.
DR OrthoDB; 448001at2759; -.
DR BRENDA; 2.7.1.11; 6524.
DR SABIO-RK; Q4E657; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000002296; Unassembled WGS sequence.
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; Reference proteome;
KW Transferase.
FT CHAIN 1..485
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000429724"
FT MOTIF 483..485
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"
SQ SEQUENCE 485 AA; 53566 MW; 43AFF562EF3EC853 CRC64;
MENRLRDTSR VVRSHAAPLN EVTQEDLKVE RLHGRKYMNP SKKHVMREEF SDKIEHIMHD
PRPQEGVHSE LPVSISPLLC ELAAPRQRIH FNPPETVVGI VTCGGICPGL NDVIRSLTLT
AVNAYRVKRV IGFRFGYWGL SKKGSHTAME LYRTSVTSIH RYGGTILGSS RGPQDTSEMV
DTLERLGVNI LFTVGGDGTQ RGALKIAEEA KRRGANLAVF GIPKTIDNDL SFSHRTFGFE
TAVDKAVEAV RAAYAEAISL NYGVGVVKLM GRDSGFIAAE AAVASAQANI CLVPENPISE
DIVMALIQRR FETSRSCVII VAEGFGQDWE GGTGGHDASG NKKLTDIGVV LTKRIQAWLR
KNKERYPNGT VKYIDPSYMI RACPPSANDA LFCATLSTLA MHEAMAGATN CIIALRYNSY
ILVPIKVATS VRRVLDLRGQ LWRQVREITV GLQDDVRAFK EAEVRRELEA ISLVRERLIG
QLSKL
