ID A9P9M1_POPTR Unreviewed; 561 AA.
AC A9P9M1;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta {ECO:0000256|HAMAP-Rule:MF_03185};
DE Short=PFP {ECO:0000256|HAMAP-Rule:MF_03185};
DE EC=2.7.1.90 {ECO:0000256|HAMAP-Rule:MF_03185};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_03185};
DE AltName: Full=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_03185};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_03185};
GN Name=PFP-BETA {ECO:0000256|HAMAP-Rule:MF_03185};
GN ORFNames=POPTR_004G003800 {ECO:0000313|EMBL:PNT38909.1};
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694 {ECO:0000313|EMBL:ABK93074.1};
RN [1] {ECO:0000313|EMBL:PNT38909.1, ECO:0000313|Proteomes:UP000006729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually {ECO:0000313|Proteomes:UP000006729}, and
RC Nisqually-1 {ECO:0000313|EMBL:PNT38909.1};
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA Depamphilis C., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J.,
RA Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A.,
RA Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B.,
RA Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjarvi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
RN [2] {ECO:0000313|EMBL:ABK93074.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Phloem and cambium {ECO:0000313|EMBL:ABK93074.1};
RX PubMed=18230180; DOI=10.1186/1471-2164-9-57;
RA Ralph S.G., Chun H.J., Cooper D., Kirkpatrick R., Kolosova N., Gunter L.,
RA Tuskan G.A., Douglas C.J., Holt R.A., Jones S.J., Marra M.A., Bohlmann J.;
RT "Analysis of 4,664 high-quality sequence-finished poplar full-length cDNA
RT clones and their utility for the discovery of genes responding to insect
RT feeding.";
RL BMC Genomics 9:57-57(2008).
RN [3] {ECO:0000313|EMBL:PNT38909.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nisqually-1 {ECO:0000313|EMBL:PNT38909.1};
RA Tuskan G., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U.,
RA Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L.,
RA Aerts A., Bhalerao R., Bhalerao R., Blaudez D., Boerjan W., Brun A.,
RA Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J.,
RA Chen G., Cooper D., Coutinho P., Couturier J., Covert S., Cronk Q.,
RA Cunningham R., Davis J., Degroeve S., Dejardin A., Depamphilis C.,
RA Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B.,
RA Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L.,
RA Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R.,
RA Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R.,
RA Joshi C., Kangasjarvi J., Karlsson J., Kelleher C., Kirkpatrick R.,
RA Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.,
RA Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C.,
RA Nelson D., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G.,
RA Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P.,
RA Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J.,
RA Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.,
RA Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G.,
RA Yin T., Douglas C., Marra M., Sandberg G., Van De Peer Y., Rokhsar D.;
RT "WGS assembly of Populus trichocarpa.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-
CC phosphotransferase. Catalyzes the phosphorylation of D-fructose 6-
CC phosphate, the first committing step of glycolysis. Uses inorganic
CC phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-
CC dependent phosphofructokinases (ATP-PFKs), which renders the reaction
CC reversible, and can thus function both in glycolysis and
CC gluconeogenesis. {ECO:0000256|HAMAP-Rule:MF_03185}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose
CC 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90;
CC Evidence={ECO:0000256|ARBA:ARBA00000628, ECO:0000256|HAMAP-
CC Rule:MF_03185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_03185};
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 2,6-
CC bisphosphate. {ECO:0000256|HAMAP-Rule:MF_03185}.
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_03185}.
CC -!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta (catalytic)
CC chains. {ECO:0000256|HAMAP-Rule:MF_03185}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03185}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}.
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DR EMBL; EF144863; ABK93074.1; -; mRNA.
DR EMBL; CM009293; PNT38909.1; -; Genomic_DNA.
DR RefSeq; XP_006383850.1; XM_006383788.1.
DR AlphaFoldDB; A9P9M1; -.
DR STRING; 3694.A9P9M1; -.
DR EnsemblPlants; Potri.004G003800.1.v4.1; Potri.004G003800.1.v4.1; Potri.004G003800.v4.1.
DR GeneID; 18097303; -.
DR Gramene; Potri.004G003800.1.v4.1; Potri.004G003800.1.v4.1; Potri.004G003800.v4.1.
DR KEGG; pop:18097303; -.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_022288_0_1_1; -.
DR InParanoid; A9P9M1; -.
DR OrthoDB; 197423at2759; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000006729; Chromosome 4.
DR ExpressionAtlas; A9P9M1; baseline and differential.
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:InterPro.
DR GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IBA:GO_Central.
DR GO; GO:0009749; P:response to glucose; IBA:GO_Central.
DR Gene3D; 3.40.50.450; -; 1.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR HAMAP; MF_01980; Phosphofructokinase_II_Long; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR011183; PfpB_PPi_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR NCBIfam; TIGR02477; PFKA_PPi; 1.
DR PANTHER; PTHR43650; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE; 1.
DR PANTHER; PTHR43650:SF1; PYROPHOSPHATE--FRUCTOSE 6-PHOSPHATE 1-PHOSPHOTRANSFERASE SUBUNIT BETA 1; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 2: Evidence at transcript level;
KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03185};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_03185};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03185};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03185};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03185}; Reference proteome {ECO:0000313|Proteomes:UP000006729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03185}.
FT DOMAIN 91..456
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 223
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 99
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 221..223
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 260..261
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 268..270
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT BINDING 434..437
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT SITE 194
FT /note="Important for catalytic activity and substrate
FT specificity; stabilizes the transition state when the
FT phosphoryl donor is PPi; prevents ATP from binding by
FT mimicking the alpha-phosphate group of ATP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
FT SITE 220
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03185"
SQ SEQUENCE 561 AA; 61299 MW; 28AE26970E9B61B6 CRC64;
MAPAFVINGD SARASGRFAS VYSEVQSSRI DHALPLPSVL KNPFKIVDGT RSSAAGNPDE
IAKLFPNLFG QPSAKLVPND VDTLSSDQKL KIGVVLSGGQ APGGHNVISG IFDYLQDRAK
GSVLYGFKGG PAGIMKCKYV ELNADYIYPY RNQGGFDMIC SGRDKIETPE QFKQAEETAK
KLDLDGLLVI GGDDSNTNAC LLAEDFWVKG LKTRVMGCPK TIDGDLKSKE VPTSFGFDTA
CKIYSEMIGN VMIDARSTGK YYHFVRLMGR AASHITLECA LQTHPNITII GEEVAAKQLT
LKNVTDYIVD IICKRSDLGY NYGVILVPEG LIDFIPEVQY LIAELNEILA HDVVDEDGLW
KKKLTNQSLQ LFEFLPPAIQ EQLMLERDPH GNVQVAKIET EKMLIQMVET ELEKRKQIGQ
SNCIFKGQSH FFGYEGRCGL PTNFDATYCY ALGYGAGALL HSGKTGLISS VGNLGAPVAE
WTVGGTALTS LMDVERRHGK FKPVIKKAMV ELEGGPFKKF ESLKNEWAIN NRYISPGPIQ
FIGPGSDAIS HTLLLELGAH A
//
