PFPB1_ARATH
ID PFPB1_ARATH Reviewed; 566 AA.
AC Q8W4M5; O65379;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 1 {ECO:0000255|HAMAP-Rule:MF_03185};
DE Short=PFP 1 {ECO:0000255|HAMAP-Rule:MF_03185};
DE EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent 1 {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=PPi-PFK 1 {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase 1 {ECO:0000255|HAMAP-Rule:MF_03185};
GN Name=PFP-BETA1 {ECO:0000255|HAMAP-Rule:MF_03185};
GN OrderedLocusNames=At1g12000; ORFNames=F12F1.13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP REVIEW.
RX PubMed=15501181; DOI=10.1016/j.tplants.2004.09.004;
RA Nielsen T.H., Rung J.H., Villadsen D.;
RT "Fructose-2,6-bisphosphate: a traffic signal in plant metabolism.";
RL Trends Plant Sci. 9:556-563(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=19533038; DOI=10.1007/s10059-009-0085-0;
RA Lim H., Cho M.-H., Jeon J.-S., Bhoo S.H., Kwon Y.-K., Hahn T.-R.;
RT "Altered expression of pyrophosphate: fructose-6-phosphate 1-
RT phosphotransferase affects the growth of transgenic Arabidopsis plants.";
RL Mol. Cells 27:641-649(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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:0000255|HAMAP-Rule:MF_03185,
CC ECO:0000269|PubMed:19533038}.
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:0000255|HAMAP-Rule:MF_03185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03185};
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 2,6-
CC bisphosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_03185}.
CC -!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta (catalytic)
CC chains. {ECO:0000255|HAMAP-Rule:MF_03185}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03185}.
CC -!- DISRUPTION PHENOTYPE: Retarded growth and reduced pyrophosphate--
CC fructose 6-phosphate 1-phosphotransferase (PFP) activity.
CC {ECO:0000269|PubMed:19533038}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Clade 'Long' sub-subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03185}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC17614.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002131; AAC17614.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28825.1; -; Genomic_DNA.
DR EMBL; AY062473; AAL32551.1; -; mRNA.
DR EMBL; AY093260; AAM13259.1; -; mRNA.
DR PIR; A86255; A86255.
DR RefSeq; NP_172664.1; NM_101072.4.
DR AlphaFoldDB; Q8W4M5; -.
DR SMR; Q8W4M5; -.
DR BioGRID; 22992; 5.
DR IntAct; Q8W4M5; 1.
DR STRING; 3702.AT1G12000.1; -.
DR iPTMnet; Q8W4M5; -.
DR PaxDb; Q8W4M5; -.
DR PRIDE; Q8W4M5; -.
DR ProteomicsDB; 235115; -.
DR EnsemblPlants; AT1G12000.1; AT1G12000.1; AT1G12000.
DR GeneID; 837752; -.
DR Gramene; AT1G12000.1; AT1G12000.1; AT1G12000.
DR KEGG; ath:AT1G12000; -.
DR Araport; AT1G12000; -.
DR TAIR; locus:2008920; AT1G12000.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_022288_0_1_1; -.
DR InParanoid; Q8W4M5; -.
DR OMA; SAKKYWH; -.
DR OrthoDB; 347054at2759; -.
DR PhylomeDB; Q8W4M5; -.
DR BioCyc; ARA:AT1G12000-MON; -.
DR UniPathway; UPA00109; UER00182.
DR PRO; PR:Q8W4M5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W4M5; baseline and differential.
DR Genevisible; Q8W4M5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
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; IMP:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008443; F:phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IMP:TAIR.
DR GO; GO:0009749; P:response to glucose; IBA:GO_Central.
DR Gene3D; 3.40.50.460; -; 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 Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
DR TIGRFAMs; TIGR02477; PFKA_PPi; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..566
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase subunit beta 1"
FT /id="PRO_0000420419"
FT ACT_SITE 229
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 105
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 227..229
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 266..267
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 274..276
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 335
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 440..443
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT SITE 200
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:0000255|HAMAP-Rule:MF_03185"
FT SITE 226
FT /note="Important for catalytic activity; stabilizes the
FT transition state when the phosphoryl donor is PPi"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 566 AA; 61459 MW; 8D8C7733FEA4D24D CRC64;
MAPALAVTRD LTAVGSPENA PAKGRASVYS EVQSSRINNT LPLPSVLKGA FKIVEGPASS
AAGNPDEIAK LFPGLYGQPS VAVVPDQDAP SSAPKLKIGV VLSGGQAPGG HNVISGLFDY
LQERAKGSTF YGFKGGPAGI MKCKYVELNA EYIQPYRNQG GFDMICSGRD KIETPDQFKQ
AEETAKKLDL DGLVVIGGDD SNTNACLLAE NFRSKNLKTR VIGCPKTIDG DLKCKEVPTS
FGFDTACKIY SEMIGNVMID ARSTGKYYHF VRLMGRAASH ITLECALQTH PNITIIGEEV
SAQKQTLKNV TDYMVDVICK RAELGYNYGV ILIPEGLIDF IPEVQELIAE LNEILANEVV
DENGLWKKKL TEQSLKLFDL LPEAIQEQLM LERDPHGNVQ VAKIETEKML IQMVETELEK
RKQAGAYKGQ FMGQSHFFGY EGRCGLPTNF DATYCYALGY GAGVLLNSGK TGLISSVGNL
AAPVEEWTVG GTALTALMDV ERRHGKFKPV IKKAMVELEG APFKKFASLR EEWALKNRYI
SPGPIQFTGP GSDSLSHTLL LELGAQ
