PFPA2_ARATH
ID PFPA2_ARATH Reviewed; 617 AA.
AC Q9C9K3; Q0WNI9; Q56WC4;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_03185};
DE Short=PFP 2 {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=Pyrophosphate-dependent 6-phosphofructose-1-kinase 2 {ECO:0000255|HAMAP-Rule:MF_03185};
GN Name=PFP-ALPHA2 {ECO:0000255|HAMAP-Rule:MF_03185};
GN OrderedLocusNames=At1g76550; ORFNames=F14G6.15;
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=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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 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 [6]
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: Regulatory subunit of pyrophosphate--fructose 6-phosphate 1-
CC phosphotransferase. {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 -!- TISSUE SPECIFICITY: Expressed in roots and specific parts such as the
CC trichomes of leaves, cotyledon veins, as well as in stamen and
CC gynoecium of flowers. {ECO:0000269|PubMed:17205343}.
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; AC015450; AAG51940.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35858.1; -; Genomic_DNA.
DR EMBL; AK222118; BAD95089.1; -; mRNA.
DR EMBL; AK229451; BAF01310.1; -; mRNA.
DR PIR; E96793; E96793.
DR RefSeq; NP_177781.1; NM_106305.3.
DR AlphaFoldDB; Q9C9K3; -.
DR SMR; Q9C9K3; -.
DR BioGRID; 29207; 7.
DR STRING; 3702.AT1G76550.1; -.
DR PaxDb; Q9C9K3; -.
DR PRIDE; Q9C9K3; -.
DR ProteomicsDB; 236786; -.
DR EnsemblPlants; AT1G76550.1; AT1G76550.1; AT1G76550.
DR GeneID; 843988; -.
DR Gramene; AT1G76550.1; AT1G76550.1; AT1G76550.
DR KEGG; ath:AT1G76550; -.
DR Araport; AT1G76550; -.
DR TAIR; locus:2011671; AT1G76550.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_022288_2_0_1; -.
DR InParanoid; Q9C9K3; -.
DR OMA; NKWHCGA; -.
DR OrthoDB; 347054at2759; -.
DR PhylomeDB; Q9C9K3; -.
DR BioCyc; ARA:AT1G76550-MON; -.
DR UniPathway; UPA00109; UER00182.
DR PRO; PR:Q9C9K3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9K3; baseline and differential.
DR Genevisible; Q9C9K3; AT.
DR GO; GO:0005739; C:mitochondrion; 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: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; 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 2: Evidence at transcript level;
KW Allosteric enzyme; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..617
FT /note="Pyrophosphate--fructose 6-phosphate 1-
FT phosphotransferase subunit alpha 2"
FT /id="PRO_0000420418"
FT CONFLICT 387
FT /note="S -> Y (in Ref. 3; BAF01310)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 67559 MW; D3AC3C2CBCC4AD8B CRC64;
MDSDFGIPRE LSPLQQLRSQ YHPELPPCLQ GTTVRVELGD GTTVAKAGDA HIIARAFPHT
LGQPLAHFLR ATAKVADAQI ITEHPVKRVG IVFCGRQAPG GHNVVWGLYE ALKVHNAKNT
LLGFLGGSEG LFAQKTLEIT DEVLQTYKNQ GGYDMLGRTK DQIRTTEQVN AALKACTDLK
LDSLVIIGGV TSNTDAAHLA EFFAEAKCST KVVGVPVTIN GDLKNQFVEA NVGFDTTCKV
NSQLISNICT DALSAEKYYY FVRLMGRKHS HVALECTLQS HPNMVILGEE VTASKLTIFD
IIKQICDAVQ ARAEQDKNHG VILIPEGLVE SIPELYALLK EIHGLLKEGV QVDNISTQLS
SWSSALFEFL PPFIKKQLLL HPESDDSAQL SQIETEKLLA YLVETEMNKR LKEGTYKGKK
FNAICHFFGY QARGSLPSKF DCDYAYVLGH VCYHILAAGL NGYMATVTNL KSPVNKWKCG
AAPISAMMTV KRWSQNSGST TIGRPVIHPA SVDLKGKAYD LLRQNAQKFL MEDMYRNPGP
VQYDGPGADA KAVSLCVEDQ DYMGKIKKLQ EYLDQVRTIV KPGCSQDVLK AALSVMASVT
DVLTTISSSS TSGQQFA
