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Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 1 (PFP 1) (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent 1) (PPi-PFK 1) (Pyrophosphate-dependent 6-phosphofructose-1-kinase 1)

 PFPB1_ARATH             Reviewed;         566 AA.
Q8W4M5; O65379;
28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
10-OCT-2018, entry version 114.
RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 1 {ECO:0000255|HAMAP-Rule:MF_03185};
Short=PFP 1 {ECO:0000255|HAMAP-Rule:MF_03185};
EC=2.7.1.90 {ECO:0000255|HAMAP-Rule:MF_03185};
AltName: Full=6-phosphofructokinase, pyrophosphate dependent 1 {ECO:0000255|HAMAP-Rule:MF_03185};
AltName: Full=PPi-PFK 1 {ECO:0000255|HAMAP-Rule:MF_03185};
AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase 1 {ECO:0000255|HAMAP-Rule:MF_03185};
Name=PFP-BETA1 {ECO:0000255|HAMAP-Rule:MF_03185};
OrderedLocusNames=At1g12000; ORFNames=F12F1.13;
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=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[6]
FUNCTION, DISRUPTION PHENOTYPE, 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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(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,
ECO:0000269|PubMed:19533038}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Retarded growth and reduced pyrophosphate--
fructose 6-phosphate 1-phosphotransferase (PFP) activity.
{ECO:0000269|PubMed:19533038}.
-!- 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=AAC17614.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AC002131; AAC17614.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE28825.1; -; Genomic_DNA.
EMBL; AY062473; AAL32551.1; -; mRNA.
EMBL; AY093260; AAM13259.1; -; mRNA.
PIR; A86255; A86255.
RefSeq; NP_172664.1; NM_101072.4.
UniGene; At.21087; -.
ProteinModelPortal; Q8W4M5; -.
SMR; Q8W4M5; -.
BioGrid; 22992; 3.
STRING; 3702.AT1G12000.1; -.
iPTMnet; Q8W4M5; -.
PaxDb; Q8W4M5; -.
PRIDE; Q8W4M5; -.
EnsemblPlants; AT1G12000.1; AT1G12000.1; AT1G12000.
GeneID; 837752; -.
Gramene; AT1G12000.1; AT1G12000.1; AT1G12000.
KEGG; ath:AT1G12000; -.
Araport; AT1G12000; -.
TAIR; locus:2008920; AT1G12000.
eggNOG; KOG2440; Eukaryota.
eggNOG; COG0205; LUCA.
HOGENOM; HOG000017164; -.
InParanoid; Q8W4M5; -.
KO; K00895; -.
OMA; GGFDMIG; -.
OrthoDB; EOG093606FK; -.
PhylomeDB; Q8W4M5; -.
BioCyc; ARA:AT1G12000-MONOMER; -.
UniPathway; UPA00109; UER00182.
PRO; PR:Q8W4M5; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q8W4M5; baseline and differential.
Genevisible; Q8W4M5; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0016020; C:membrane; 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:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
GO; GO:0015979; P:photosynthesis; IMP:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009735; P:response to cytokinin; IDA: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.
1: Evidence at protein level;
Allosteric enzyme; Complete proteome; Cytoplasm; Glycolysis; Kinase;
Magnesium; Metal-binding; Phosphoprotein; Reference proteome;
Transferase.
CHAIN 1 566 Pyrophosphate--fructose 6-phosphate 1-
phosphotransferase subunit beta 1.
/FTId=PRO_0000420419.
REGION 227 229 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03185}.
REGION 266 267 Substrate binding; shared with dimeric
partner. {ECO:0000255|HAMAP-
Rule:MF_03185}.
REGION 274 276 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03185}.
REGION 440 443 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03185}.
ACT_SITE 229 229 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03185}.
METAL 199 199 Magnesium; catalytic. {ECO:0000255|HAMAP-
Rule:MF_03185}.
BINDING 105 105 Diphosphate; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_03185}.
BINDING 335 335 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03185}.
SITE 200 200 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 226 226 Important for catalytic activity;
stabilizes the transition state when the
phosphoryl donor is PPi.
{ECO:0000255|HAMAP-Rule:MF_03185}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:19245862,
ECO:0000244|PubMed:19376835}.
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


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