ID A0A087HIX1_ARAAL Unreviewed; 617 AA. AC A0A087HIX1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 19-JAN-2022, entry version 39. DE RecName: Full=Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit alpha {ECO:0000256|HAMAP-Rule:MF_03185}; DE Short=PFP {ECO:0000256|HAMAP-Rule:MF_03185}; DE AltName: Full=6-phosphofructokinase, pyrophosphate dependent {ECO:0000256|HAMAP-Rule:MF_03185}; DE AltName: Full=PPi-PFK {ECO:0000256|HAMAP-Rule:MF_03185}; DE AltName: Full=Pyrophosphate-dependent 6-phosphofructose-1-kinase {ECO:0000256|HAMAP-Rule:MF_03185}; GN Name=PFP-ALPHA {ECO:0000256|HAMAP-Rule:MF_03185}; GN ORFNames=AALP_AA2G207700 {ECO:0000313|EMBL:KFK42073.1}; OS Arabis alpina (Alpine rock-cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis. OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK42073.1, ECO:0000313|Proteomes:UP000029120}; RN [1] {ECO:0000313|Proteomes:UP000029120} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120}; RX PubMed=27246759; DOI=10.1038/nplants.2014.23; RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V., RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B., RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L., RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L., RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R., RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F., RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H., RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.; RT "Genome expansion of Arabis alpina linked with retrotransposition and RT reduced symmetric DNA methylation."; RL Nat. Plants 1:14023-14023(2015). CC -!- FUNCTION: Regulatory subunit of pyrophosphate--fructose 6-phosphate 1- CC phosphotransferase. {ECO:0000256|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:0000256|ARBA:ARBA00000628}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- ACTIVITY REGULATION: Allosterically activated by fructose 2,6- CC bisphosphate. {ECO:0000256|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:0000256|ARBA:ARBA00004679, ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- SUBUNIT: Tetramer of two alpha (regulatory) and two beta (catalytic) CC chains. {ECO:0000256|HAMAP-Rule:MF_03185}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_03185}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03185}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CM002870; KFK42073.1; -; Genomic_DNA. DR STRING; 50452.A0A087HIX1; -. DR EnsemblPlants; KFK42073; KFK42073; AALP_AA2G207700. DR Gramene; KFK42073; KFK42073; AALP_AA2G207700. DR eggNOG; KOG2440; Eukaryota. DR OMA; NKWHCGA; -. DR OrthoDB; 347054at2759; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000029120; Chromosome 2. 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; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. 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 {ECO:0000256|HAMAP-Rule:MF_03185}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03185}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_03185}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03185}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03185}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03185}; Reference proteome {ECO:0000313|Proteomes:UP000029120}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03185}. FT DOMAIN 88..453 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" SQ SEQUENCE 617 AA; 67435 MW; 70EB47E66A9999ED CRC64; MDSDFGIPRE LSPLQQLRSQ YQPLLPPCLQ GTTVRVELGD GTTGAKAGDA HIIARAFPHT LGQPLAHFLR ANAKVVDAQI ITEHPAIRVG IVFSGRQAPG GHNVIWGLYE ALKVHNAKNT LLGFLGGSEG LFAQKTVEIT DDVLQTYKNQ GGFDLLGRTK DQIRTTEQVN AALKACTDLK LDGLVIIGGV TSNTDAGHLA EFFAETKCPT KVVGVPVTIN GDLKNQFVEA NVGFDTICKV NSQLISNVCT DALSAEKYYY FIRLMGRKHS HVALECTLQS HPNMVILGEE VAASKLTIFD IAKQICDAVQ ARAEQDKNHG VILIPEGLVE SIPELFALLK EIHGLLKEGV DADKISTKLS PWSFALFEFL PPFMKKQLLL HPESDDSAQL SQIETEKLLA YLVETEMNKR MKVGTYKGKK FNAICHFFGY QARGSLPSKF DCDYAYVLGH ICYHILAAGL NGYMATVTNL KSPVNKWKCG AAPITAMMTV KRWSQNAGST SIGRPVIHPA TVDLKGKAYD LLRQNAQKFL MEDMYRNPGP LQYDGPGADA KAVSLCVEDQ DYMGRIKKLQ EYLDQVRTIV KPGCSQDVLK AALSVMASVT DVLSTISSSS TSGQQFA //