PFPA1_ARATH
ID PFPA1_ARATH Reviewed; 614 AA.
AC Q9SYP2;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_03185};
DE Short=PFP 1 {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-ALPHA1 {ECO:0000255|HAMAP-Rule:MF_03185};
GN OrderedLocusNames=At1g20950; ORFNames=F9H16.6;
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 INDUCTION BY SUCROSE; GLUCOSE AND FRUCTOSE.
RX PubMed=16463203; DOI=10.1007/s10265-005-0251-1;
RA Gonzali S., Loreti E., Solfanelli C., Novi G., Alpi A., Perata P.;
RT "Identification of sugar-modulated genes and evidence for in vivo sugar
RT sensing in Arabidopsis.";
RL J. Plant Res. 119:115-123(2006).
RN [6]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=17205343; DOI=10.1007/s00299-006-0272-9;
RA Lim H.-M., Cho J.-I., Lee S., Cho M.-H., Bhoo S.H., An G., Hahn T.-R.,
RA Jeon J.-S.;
RT "Identification of a 20-bp regulatory element of the Arabidopsis
RT pyrophosphate:fructose-6-phosphate 1-phosphotransferase alpha2 gene that is
RT essential for expression.";
RL Plant Cell Rep. 26:683-692(2007).
RN [7]
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).
CC -!- FUNCTION: Regulatory subunit of pyrophosphate--fructose 6-phosphate 1-
CC phosphotransferase. {ECO:0000255|HAMAP-Rule:MF_03185,
CC ECO:0000269|PubMed:19533038}.
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 -!- INTERACTION:
CC Q9SYP2; Q940G6: GID1C; NbExp=3; IntAct=EBI-1238145, EBI-963794;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03185}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, and flowers (e.g.
CC sepals, petals, stamen and gynoecium). {ECO:0000269|PubMed:17205343}.
CC -!- INDUCTION: By sucrose, glucose, and fructose.
CC {ECO:0000269|PubMed:16463203}.
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}.
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DR EMBL; AC007369; AAD30596.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30045.1; -; Genomic_DNA.
DR EMBL; AY059855; AAL24337.1; -; mRNA.
DR EMBL; BT008374; AAP37733.1; -; mRNA.
DR PIR; D86342; D86342.
DR RefSeq; NP_173519.1; NM_101948.3.
DR AlphaFoldDB; Q9SYP2; -.
DR SMR; Q9SYP2; -.
DR BioGRID; 23928; 14.
DR IntAct; Q9SYP2; 6.
DR STRING; 3702.AT1G20950.1; -.
DR PaxDb; Q9SYP2; -.
DR PRIDE; Q9SYP2; -.
DR ProteomicsDB; 236430; -.
DR EnsemblPlants; AT1G20950.1; AT1G20950.1; AT1G20950.
DR GeneID; 838689; -.
DR Gramene; AT1G20950.1; AT1G20950.1; AT1G20950.
DR KEGG; ath:AT1G20950; -.
DR Araport; AT1G20950; -.
DR TAIR; locus:2037385; AT1G20950.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_022288_2_0_1; -.
DR InParanoid; Q9SYP2; -.
DR OMA; SYTTLEC; -.
DR OrthoDB; 347054at2759; -.
DR PhylomeDB; Q9SYP2; -.
DR BioCyc; ARA:AT1G20950-MON; -.
DR UniPathway; UPA00109; UER00182.
DR PRO; PR:Q9SYP2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYP2; baseline and differential.
DR Genevisible; Q9SYP2; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0015979; P:photosynthesis; IMP:TAIR.
DR GO; GO:0009750; P:response to fructose; IEP:TAIR.
DR GO; GO:0009749; P:response to glucose; IEP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR Gene3D; 3.40.50.460; -; 1.
DR HAMAP; MF_01980; Phosphofructokinase_II_Long; 1.
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 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 Reference proteome; Transferase.
FT CHAIN 1..614
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase subunit alpha 1"
FT /id="PRO_0000420417"
SQ SEQUENCE 614 AA; 67119 MW; 082FAB7359F8CD0A CRC64;
MDSDFGIPRE LSPLQQLRSQ YKPELPPCLQ GTTVRVELGD GTTVAEAADS HTMARAFPHT
LGQPLAHFLR ETAQVPDAHI ITELPSVRVG IVFCGRQAPG GHNVIWGLFE ALKVHNAKST
LLGFLGGSEG LFAQKTLEIT DDILQTYKNQ GGYDLLGRTK DQIKTTEQVN AALKACTDLK
LDGLVIIGGV ISNTDAAHLA EFFAAAKCST KVVGVPVTTN GDLKNQFVEA NVGFDTICKV
NSQLISNACT DALSAEKYYY FIRLMGRKHS HVALECTLQS HPNMVILGEE VAASKLTIFD
IAKQICDAVQ ARAVEDKNHG VILIPEGLIV SIPEVYALLK EIHGLLRQGV SADKISTQLS
PWSSALFEFL PPFIKKQLLL HPESDDSAQL SQIETEKLLA YLVETEMNKR LKEGTYKGKK
FNAICHFFGY QARGSLPSKF DCDYAYVLGH ICYHILAAGL NGYMATVTNL KSPVNKWKCG
ATPITAMMTV KHWSQDASYT LTSIGRPAIH PAMVDLKGKA YDLLRQNAQK FLMEDLYRNP
GPLQYDGPGA DAKAVSLCVE DQDYMGRIKK LQEYLDQVRT IVKPGCSQDV LKAALSVMAS
VTDVLTTISS NGGQ
