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Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 2 (PFP 2) (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent 2) (PPi-PFK 2) (Protein MATERNAL EFFECT EMBRYO ARREST 51) (Pyrophosphate-dependent 6-phosphofructose-1-kinase 2)

 PFPB2_ARATH             Reviewed;         569 AA.
F4JGR5; O81437;
28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
10-OCT-2018, entry version 53.
RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 2 {ECO:0000255|HAMAP-Rule:MF_03185};
Short=PFP 2 {ECO:0000255|HAMAP-Rule:MF_03185};
EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_03185};
AltName: Full=6-phosphofructokinase, pyrophosphate dependent 2 {ECO:0000255|HAMAP-Rule:MF_03185};
AltName: Full=PPi-PFK 2 {ECO:0000255|HAMAP-Rule:MF_03185};
AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 51;
AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase 2 {ECO:0000255|HAMAP-Rule:MF_03185};
Name=PFP-BETA2 {ECO:0000255|HAMAP-Rule:MF_03185}; Synonyms=MEE51;
OrderedLocusNames=At4g04040; ORFNames=T24H24.15;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
REVIEW.
PubMed=15501181; DOI=10.1016/j.tplants.2004.09.004;
Nielsen T.H., Rung J.H., Villadsen D.;
"Fructose-2,6-bisphosphate: a traffic signal in plant metabolism.";
Trends Plant Sci. 9:556-563(2004).
[4]
GENE FAMILY, AND NOMENCLATURE.
STRAIN=cv. Columbia;
PubMed=19533038; DOI=10.1007/s10059-009-0085-0;
Lim H., Cho M.-H., Jeon J.-S., Bhoo S.H., Kwon Y.-K., Hahn T.-R.;
"Altered expression of pyrophosphate: fructose-6-phosphate 1-
phosphotransferase affects the growth of transgenic Arabidopsis
plants.";
Mol. Cells 27:641-649(2009).
-!- FUNCTION: Catalytic subunit of pyrophosphate--fructose 6-phosphate
1-phosphotransferase. Catalyzes the phosphorylation of D-fructose
6-phosphate, the first committing step of glycolysis. Uses
inorganic phosphate (PPi) as phosphoryl donor instead of ATP like
common ATP-dependent phosphofructokinases (ATP-PFKs), which
renders the reaction reversible, and can thus function both in
glycolysis and gluconeogenesis. {ECO:0000255|HAMAP-Rule:MF_03185}.
-!- CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate =
phosphate + D-fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_03185}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_03185};
-!- ACTIVITY REGULATION: Allosterically activated by fructose 2,6-
bisphosphate. {ECO:0000255|HAMAP-Rule:MF_03185}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000255|HAMAP-Rule:MF_03185}.
-!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta
(catalytic) chains. {ECO:0000255|HAMAP-Rule:MF_03185}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03185}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. PPi-dependent PFK group II subfamily. Clade "Long" sub-
subfamily. {ECO:0000255|HAMAP-Rule:MF_03185}.
-!- SEQUENCE CAUTION:
Sequence=AAC28214.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB77872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF075598; AAC28214.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161499; CAB77872.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE82365.1; -; Genomic_DNA.
PIR; T01470; T01470.
RefSeq; NP_192313.3; NM_116642.4.
UniGene; At.34079; -.
ProteinModelPortal; F4JGR5; -.
SMR; F4JGR5; -.
STRING; 3702.AT4G04040.1; -.
iPTMnet; F4JGR5; -.
PaxDb; F4JGR5; -.
PRIDE; F4JGR5; -.
EnsemblPlants; AT4G04040.1; AT4G04040.1; AT4G04040.
GeneID; 825716; -.
Gramene; AT4G04040.1; AT4G04040.1; AT4G04040.
KEGG; ath:AT4G04040; -.
Araport; AT4G04040; -.
TAIR; locus:2136652; AT4G04040.
eggNOG; KOG2440; Eukaryota.
eggNOG; COG0205; LUCA.
InParanoid; F4JGR5; -.
KO; K00895; -.
OMA; ENGYNYG; -.
OrthoDB; EOG093606FK; -.
UniPathway; UPA00109; UER00182.
PRO; PR:F4JGR5; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; F4JGR5; baseline and differential.
Genevisible; F4JGR5; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IMP:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
GO; GO:0015979; P:photosynthesis; IMP:TAIR.
HAMAP; MF_01980; Phosphofructokinase_II_Long; 1.
InterPro; IPR022953; ATP_PFK.
InterPro; IPR011183; PfpB_PPi_PFK.
InterPro; IPR000023; Phosphofructokinase_dom.
InterPro; IPR035966; PKF_sf.
Pfam; PF00365; PFK; 1.
PIRSF; PIRSF005677; PPi_PFK_PfpB; 1.
PRINTS; PR00476; PHFRCTKINASE.
SUPFAM; SSF53784; SSF53784; 1.
TIGRFAMs; TIGR02477; PFKA_PPi; 1.
3: Inferred from homology;
Allosteric enzyme; Complete proteome; Cytoplasm; Glycolysis; Kinase;
Magnesium; Metal-binding; Reference proteome; Transferase.
CHAIN 1 569 Pyrophosphate--fructose 6-phosphate 1-
phosphotransferase subunit beta 2.
/FTId=PRO_0000420420.
REGION 229 231 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03185}.
REGION 268 269 Substrate binding; shared with dimeric
partner. {ECO:0000255|HAMAP-
Rule:MF_03185}.
REGION 276 278 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03185}.
REGION 442 445 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03185}.
ACT_SITE 231 231 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03185}.
METAL 201 201 Magnesium; catalytic. {ECO:0000255|HAMAP-
Rule:MF_03185}.
BINDING 107 107 Diphosphate; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_03185}.
BINDING 337 337 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03185}.
SITE 202 202 Important for catalytic activity and
substrate specificity; stabilizes the
transition state when the phosphoryl
donor is PPi; prevents ATP from binding
by mimicking the alpha-phosphate group of
ATP. {ECO:0000255|HAMAP-Rule:MF_03185}.
SITE 228 228 Important for catalytic activity;
stabilizes the transition state when the
phosphoryl donor is PPi.
{ECO:0000255|HAMAP-Rule:MF_03185}.
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


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