PFPB2_ARATH
ID PFPB2_ARATH Reviewed; 569 AA.
AC F4JGR5; O81437;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 2 {ECO:0000255|HAMAP-Rule:MF_03185};
DE Short=PFP 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=PPi-PFK 2 {ECO:0000255|HAMAP-Rule:MF_03185};
DE AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 51;
DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase 2 {ECO:0000255|HAMAP-Rule:MF_03185};
GN Name=PFP-BETA2 {ECO:0000255|HAMAP-Rule:MF_03185}; Synonyms=MEE51;
GN OrderedLocusNames=At4g04040; ORFNames=T24H24.15;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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 [4]
RP 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).
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 -!- 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 -!- 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=AAC28214.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB77872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF075598; AAC28214.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161499; CAB77872.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82365.1; -; Genomic_DNA.
DR PIR; T01470; T01470.
DR RefSeq; NP_192313.3; NM_116642.4.
DR AlphaFoldDB; F4JGR5; -.
DR SMR; F4JGR5; -.
DR BioGRID; 11029; 2.
DR STRING; 3702.AT4G04040.1; -.
DR iPTMnet; F4JGR5; -.
DR PaxDb; F4JGR5; -.
DR PRIDE; F4JGR5; -.
DR ProteomicsDB; 234990; -.
DR EnsemblPlants; AT4G04040.1; AT4G04040.1; AT4G04040.
DR GeneID; 825716; -.
DR Gramene; AT4G04040.1; AT4G04040.1; AT4G04040.
DR KEGG; ath:AT4G04040; -.
DR Araport; AT4G04040; -.
DR TAIR; locus:2136652; AT4G04040.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_022288_0_1_1; -.
DR InParanoid; F4JGR5; -.
DR OMA; ENGYNYG; -.
DR OrthoDB; 347054at2759; -.
DR UniPathway; UPA00109; UER00182.
DR PRO; PR:F4JGR5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JGR5; baseline and differential.
DR Genevisible; F4JGR5; AT.
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; 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:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
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 3: Inferred from homology;
KW Allosteric enzyme; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..569
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase subunit beta 2"
FT /id="PRO_0000420420"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 107
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 229..231
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 268..269
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03185"
FT BINDING 276..278
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 337
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 442..445
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 202
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 228
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"
SQ SEQUENCE 569 AA; 62742 MW; 9CF647A1BD6A7FCB CRC64;
MASQLDLIGG DYIAGISINP PTNSRVTSVY SEVQASRIDH TLPLPSVFKT PFKIIDGPPS
SSAGHPEEIE KLFPNLFGQP SALLVPNQSN EVSSDQKLKI GVVLSGGQAP GGHNVICGIF
DYLQEYARGS SLFGFRGGPA GIMKGKYIEL TSEFVYPYRN QGGFDMICSG RDKIETPEQF
KQAEETVTKM DLDGLVVIGG DDSNTNACLL AEHFRAKNMK TLVIGCPKTI DGDLKSKEVP
TSFGFDTACK IYSEMIGNVM IDARSTGKYY HFVRLMGRAA SHITLECALQ THPNITIIGE
EVFEKKLTLK NVTDNIVDVI YKRAENGYNY GVILVPEGLI DFIPEVQQLI SELNEVLAEG
NVDEEGQWKK NLKKETLEIF EFLPQTIQEQ LMLERDPHGN VQVAKIETEK MLIQMVETEL
EKKKTEGTYE REFMGKSHFF GYEGRCGLPT NFDATYCYAL GYGAGSLLQS GKTGLISSVG
NLAAPVEEWT VGGTALTSLM DVERRHGKFK PVIKKAMVEL EGAPFKKFAS QREEWALKNR
YISPGPIQFK GPGSDARNHT LMLELGAQA
