PFKA_TRYBB
ID PFKA_TRYBB Reviewed; 487 AA.
AC O15648;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
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 Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 13-24; 55-64;
RP 240-247 AND 375-382, AND CATALYTIC ACTIVITY.
RC STRAIN=427;
RX PubMed=9461292; DOI=10.1111/j.1432-1033.1997.00698.x;
RA Michels P.A., Chevalier N., Opperdoes F.R., Rider M.H., Rigden D.J.;
RT "The glycosomal ATP-dependent phosphofructokinase of Trypanosoma brucei
RT must have evolved from an ancestral pyrophosphate-dependent enzyme.";
RL Eur. J. Biochem. 250:698-704(1997).
RN [2]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=427;
RX PubMed=2940090; DOI=10.1111/j.1432-1033.1986.tb09687.x;
RA Misset O., Bos O.J., Opperdoes F.R.;
RT "Glycolytic enzymes of Trypanosoma brucei. Simultaneous purification,
RT intraglycosomal concentrations and physical properties.";
RL Eur. J. Biochem. 157:441-453(1986).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RC STRAIN=427;
RX PubMed=17207816; DOI=10.1016/j.jmb.2006.10.019;
RA Martinez-Oyanedel J., McNae I.W., Nowicki M.W., Keillor J.W., Michels P.A.,
RA Fothergill-Gilmore L.A., Walkinshaw M.D.;
RT "The first crystal structure of phosphofructokinase from a eukaryote:
RT Trypanosoma brucei.";
RL J. Mol. Biol. 366:1185-1198(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 481-487.
RC STRAIN=427;
RX PubMed=18598704; DOI=10.1016/j.jmb.2008.05.089;
RA Sampathkumar P., Roach C., Michels P.A., Hol W.G.;
RT "Structural insights into the recognition of peroxisomal targeting signal 1
RT by Trypanosoma brucei peroxin 5.";
RL J. Mol. Biol. 381:867-880(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ATP.
RC STRAIN=427;
RX PubMed=19084537; DOI=10.1016/j.jmb.2008.11.047;
RA McNae I.W., Martinez-Oyanedel J., Keillor J.W., Michels P.A.,
RA Fothergill-Gilmore L.A., Walkinshaw M.D.;
RT "The crystal structure of ATP-bound phosphofructokinase from Trypanosoma
RT brucei reveals conformational transitions different from those of other
RT phosphofructokinases.";
RL J. Mol. Biol. 385:1519-1533(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 -!- 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:9461292};
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 -!- 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 ECO:0000269|PubMed:19084537, ECO:0000269|PubMed:2940090}.
CC -!- SUBCELLULAR LOCATION: Glycosome {ECO:0000255|HAMAP-Rule:MF_03186,
CC ECO:0000269|PubMed:2940090}.
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; AF008186; AAC47836.1; -; Genomic_DNA.
DR PDB; 2HIG; X-ray; 2.40 A; A/B=1-487.
DR PDB; 3CVL; X-ray; 2.15 A; B=481-487.
DR PDB; 3F5M; X-ray; 2.70 A; A/B/C/D=1-487.
DR PDB; 6QU3; X-ray; 2.35 A; A/B/C/D=1-487.
DR PDB; 6QU4; X-ray; 2.75 A; A/B/C/D=1-487.
DR PDB; 6QU5; X-ray; 3.40 A; A/B/C/D/E/F/G/H=1-487.
DR PDB; 6SY7; X-ray; 2.75 A; A/B/C/D/E/F/G/H=1-487.
DR PDBsum; 2HIG; -.
DR PDBsum; 3CVL; -.
DR PDBsum; 3F5M; -.
DR PDBsum; 6QU3; -.
DR PDBsum; 6QU4; -.
DR PDBsum; 6QU5; -.
DR PDBsum; 6SY7; -.
DR AlphaFoldDB; O15648; -.
DR SMR; O15648; -.
DR BindingDB; O15648; -.
DR ChEMBL; CHEMBL5686; -.
DR DrugCentral; O15648; -.
DR OMA; PYIDQSF; -.
DR BRENDA; 2.7.1.11; 6520.
DR SABIO-RK; O15648; -.
DR UniPathway; UPA00109; UER00182.
DR EvolutionaryTrace; O15648; -.
DR GO; GO:0020015; C:glycosome; IDA:GeneDB.
DR GO; GO:0003872; F:6-phosphofructokinase activity; TAS:GeneDB.
DR GO; GO:0005524; F:ATP binding; IDA:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042301; F:phosphate ion binding; IDA:GeneDB.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IC:GeneDB.
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 PIRSF; PIRSF000534; PPi_PFK_TP0108; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Direct protein sequencing;
KW Glycolysis; Glycosome; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Peroxisome; Transferase.
FT CHAIN 1..487
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000429723"
FT MOTIF 485..487
FT /note="Peroxisomal targeting signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT ACT_SITE 229
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186,
FT ECO:0000269|PubMed:19084537"
FT BINDING 173..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186,
FT ECO:0000269|PubMed:19084537"
FT BINDING 198..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186,
FT ECO:0000269|PubMed:19084537"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19084537"
FT BINDING 227..229
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 272..274
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 341..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186,
FT ECO:0000269|PubMed:19084537"
FT BINDING 380..383
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT SITE 200
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:2HIG"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3F5M"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2HIG"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 241..260
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 302..315
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:6QU3"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:2HIG"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:2HIG"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6QU5"
FT HELIX 349..363
FT /evidence="ECO:0007829|PDB:6QU3"
FT TURN 364..367
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 389..407
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:6QU3"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:2HIG"
FT HELIX 442..450
FT /evidence="ECO:0007829|PDB:6QU3"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:3F5M"
FT HELIX 458..485
FT /evidence="ECO:0007829|PDB:6QU3"
SQ SEQUENCE 487 AA; 53517 MW; 59357FF92ADA1FA9 CRC64;
MAVESRSRVT SKLVKAHRAM LNSVTQEDLK VDRLPGADYP NPSKKYSSRT EFRDKTDYIM
YNPRPRDEPS SENPVSVSPL LCELAAARSR IHFNPTETTI GIVTCGGICP GLNDVIRSIT
LTGINVYNVK RVIGFRFGYW GLSKKGSQTA IELHRGRVTN IHHYGGTILG SSRGPQDPKE
MVDTLERLGV NILFTVGGDG TQRGALVISQ EAKRRGVDIS VFGVPKTIDN DLSFSHRTFG
FQTAVEKAVQ AIRAAYAEAV SANYGVGVVK LMGRDSGFIA AQAAVASAQA NICLVPENPI
SEQEVMSLLE RRFCHSRSCV IIVAEGFGQD WGRGSGGYDA SGNKKLIDIG VILTEKVKAF
LKANKSRYPD STVKYIDPSY MIRACPPSAN DALFCATLAT LAVHEAMAGA TGCIIAMRHN
NYILVPIKVA TSVRRVLDLR GQLWRQVREI TVDLGSDVRL ARKLEIRREL EAINRNRDRL
HEELAKL
