ID D6XDN4_TRYB2 Unreviewed; 487 AA.
AC D6XDN4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=Tb03.3K10.320 {ECO:0000313|EMBL:AAZ10361.1};
GN Synonyms=pfk {ECO:0000256|HAMAP-Rule:MF_03186};
GN ORFNames=Tb927.3.3270 {ECO:0000313|EMBL:AAZ10361.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000313|EMBL:AAZ10361.1, ECO:0000313|Proteomes:UP000008524};
RN [1] {ECO:0000313|EMBL:AAZ10361.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ10361.1};
RX PubMed=16020724; DOI=10.1126/science.1112181;
RA El-Sayed N.M., Myler P.J., Blandin G., Berriman M., Crabtree J.,
RA Aggarwal G., Caler E., Renauld H., Worthey E.A., Hertz-Fowler C.,
RA Ghedin E., Peacock C., Bartholomeu D.C., Haas B.J., Tran A.N.,
RA Wortman J.R., Alsmark U.C., Angiuoli S., Anupama A., Badger J.,
RA Bringaud F., Cadag E., Carlton J.M., Cerqueira G.C., Creasy T.,
RA Delcher A.L., Djikeng A., Embley T.M., Hauser C., Ivens A.C.,
RA Kummerfeld S.K., Pereira-Leal J.B., Nilsson D., Peterson J., Salzberg S.L.,
RA Shallom J., Silva J.C., Sundaram J., Westenberger S., White O.,
RA Melville S.E., Donelson J.E., Andersson B., Stuart K.D., Hall N.;
RT "Comparative genomics of trypanosomatid parasitic protozoa.";
RL Science 309:404-409(2005).
RN [2] {ECO:0000313|EMBL:AAZ10361.1, ECO:0000313|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ10361.1,
RC ECO:0000313|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
RN [3] {ECO:0000313|EMBL:AAX70509.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GUTat10.1 {ECO:0000313|EMBL:AAX70509.1};
RA Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA Wortman J., Fraser C.M., El-Sayed N.M.A.;
RT ".";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AAZ10361.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:AAZ10361.1};
RA Ghedin E., Blandin G., Bartholomeu D., Caler E., Haas B., Hannick L.,
RA Shallom J., Hou L., Djikeng A., Feldblyum T., Hostetler J., Johnson J.,
RA Jones K., Koo H.L., Larkin C., Pai G., Peterson J., Khalak H.G.,
RA Salzberg S., Simpson A.J., Tallon L., Van Aken S., Wanless D., White O.,
RA Wortman J., Fraser C.M., El-Sayed N.M.A.;
RT "Sequencing, closure, and annotation of Trypanosoma brucei chromosomes 2
RT through 8.";
RL Submitted (APR-2005) 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: Glycosome {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; AC159446; AAX70509.1; -; Genomic_DNA.
DR EMBL; CP000066; AAZ10361.1; -; Genomic_DNA.
DR RefSeq; XP_843920.1; XM_838827.1.
DR AlphaFoldDB; D6XDN4; -.
DR SMR; D6XDN4; -.
DR STRING; 185431.D6XDN4; -.
DR PaxDb; 5691-AAZ10361; -.
DR GeneID; 3656265; -.
DR KEGG; tbr:Tb927.3.3270; -.
DR VEuPathDB; TriTrypDB:Tb927.3.3270; -.
DR eggNOG; KOG2440; Eukaryota.
DR InParanoid; D6XDN4; -.
DR OMA; PYIDQSF; -.
DR OrthoDB; 995926at2759; -.
DR UniPathway; UPA00109; UER00182.
DR EvolutionaryTrace; D6XDN4; -.
DR Proteomes; UP000008524; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0020015; C:glycosome; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
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; -; 2.
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:SF11; 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 Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_03186}; Glycosome {ECO:0000256|HAMAP-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 Peroxisome {ECO:0000256|HAMAP-Rule:MF_03186};
KW Reference proteome {ECO:0000313|Proteomes:UP000008524};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03186}.
FT DOMAIN 100..404
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT MOTIF 485..487
FT /note="Peroxisomal targeting signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT ACT_SITE 229
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 173..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 198..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 227..229
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 272..274
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 380..383
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT SITE 200
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
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
//
