ID PFKA6_ARATH Reviewed; 462 AA. AC Q9M076; Q8LA55; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 139. DE RecName: Full=ATP-dependent 6-phosphofructokinase 6 {ECO:0000255|HAMAP-Rule:MF_03186}; DE Short=ATP-PFK 6 {ECO:0000255|HAMAP-Rule:MF_03186}; DE Short=Phosphofructokinase 6 {ECO:0000255|HAMAP-Rule:MF_03186}; DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03186}; DE AltName: Full=Phosphohexokinase 6 {ECO:0000255|HAMAP-Rule:MF_03186}; GN Name=PFK6 {ECO:0000255|HAMAP-Rule:MF_03186}; GN OrderedLocusNames=At4g32840; ORFNames=T16I18.50; 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=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). 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 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY, RP AND NOMENCLATURE. RX PubMed=17485088; DOI=10.1016/j.febslet.2007.04.060; RA Mustroph A., Sonnewald U., Biemelt S.; RT "Characterisation of the ATP-dependent phosphofructokinase gene family from RT Arabidopsis thaliana."; RL FEBS Lett. 581:2401-2410(2007). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to CC fructose 1,6-bisphosphate by ATP, the first committing step of CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_03186}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6- CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03186, ECO:0000269|PubMed:17485088}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03186}; CC -!- ACTIVITY REGULATION: Allosterically activated by AMP. CC {ECO:0000255|HAMAP-Rule:MF_03186}. 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_03186}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03186}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03186, CC ECO:0000269|PubMed:17485088}. Note=May be associated with the outer CC membrane of mitochondria. CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers. CC {ECO:0000269|PubMed:17485088}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. CC PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X' CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03186}. 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; AL161582; CAB80001.1; -; Genomic_DNA. DR EMBL; CP002687; AEE86125.1; -; Genomic_DNA. DR EMBL; BT006001; AAO64936.1; -; mRNA. DR EMBL; AK227471; BAE99473.1; -; mRNA. DR EMBL; AY088020; AAM65566.1; -; mRNA. DR PIR; T10691; T10691. DR RefSeq; NP_195010.1; NM_119437.3. DR AlphaFoldDB; Q9M076; -. DR SMR; Q9M076; -. DR BioGRID; 14705; 1. DR STRING; 3702.Q9M076; -. DR iPTMnet; Q9M076; -. DR PaxDb; 3702-AT4G32840-1; -. DR ProteomicsDB; 235096; -. DR EnsemblPlants; AT4G32840.1; AT4G32840.1; AT4G32840. DR GeneID; 829420; -. DR Gramene; AT4G32840.1; AT4G32840.1; AT4G32840. DR KEGG; ath:AT4G32840; -. DR Araport; AT4G32840; -. DR TAIR; AT4G32840; PFK6. DR eggNOG; KOG2440; Eukaryota. DR HOGENOM; CLU_020655_7_4_1; -. DR InParanoid; Q9M076; -. DR OMA; KGAATIH; -. DR OrthoDB; 995926at2759; -. DR PhylomeDB; Q9M076; -. DR BioCyc; ARA:AT4G32840-MONOMER; -. DR BRENDA; 2.7.1.11; 399. DR UniPathway; UPA00109; UER00182. DR PRO; PR:Q9M076; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q9M076; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:TAIR. DR GO; GO:0003872; F:6-phosphofructokinase activity; IDA:TAIR. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IDA:TAIR. DR Gene3D; 3.40.50.450; -; 1. DR HAMAP; MF_01981; Phosphofructokinase_II_X; 1. DR InterPro; IPR022953; ATP_PFK. DR InterPro; IPR000023; Phosphofructokinase_dom. DR InterPro; IPR035966; PKF_sf. DR InterPro; IPR012004; PyroP-dep_PFK_TP0108. DR PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1. DR PANTHER; PTHR45770:SF53; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 6; 1. DR Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000534; PPi_PFK_TP0108; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; Phosphofructokinase; 1. DR Genevisible; Q9M076; AT. PE 1: Evidence at protein level; KW Acetylation; Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..462 FT /note="ATP-dependent 6-phosphofructokinase 6" FT /id="PRO_0000330773" FT ACT_SITE 221 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186" FT BINDING 102 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186" FT BINDING 165..166 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186" FT BINDING 190..193 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186" FT BINDING 191 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186" FT BINDING 219..221 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186" FT BINDING 264..266 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186" FT BINDING 320 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186" FT BINDING 374..377 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186" FT SITE 192 FT /note="Important for substrate specificity; cannot use PPi FT as phosphoryl donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895" FT MOD_RES 71 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9M0F9" FT CONFLICT 282 FT /note="V -> A (in Ref. 5; AAM65566)" FT /evidence="ECO:0000305" SQ SEQUENCE 462 AA; 50788 MW; 283E7758C5DB8C24 CRC64; MASNGVDEQI KLVEGPAGYV LEDVPHLSDY ILDLPTYPNP LQSNAAYSVV RQYFVDEDDT VQEKIVVHKD SPRGTHFRRA GPRQKVYFKP SDVRACIVTC GGLCPGLNTV IREIVCGLHF MYGVTEVIGV DCGFRGFYSK NTVALTPKTV SDIHKRGGTI LGTSRGGHDT SKIVDNIQDR EINQVYIIGG DGTQKGANAI YKEIRRRGLK VAVAGIPKTI DNDIPVIDKS FGFDTAVEEA QRAINAAHVE ATSVENGIGI VKLMGRYSGF IAMYATLASR DVDCCLIPES PFYLEGKGGL YEFIAKRLRE NGHMVIVIAE GAGQDLVAES IEQQDASGNK LLKDVGLWMS LKIKEYFAKH NVMDITLKYI DPTYMIRAIP ANASDNVYST LLAQSAVHGA MAGYTGFVSG LVNGRHTYIP FNRITERQNK VVITDRMWAR MLSSTNQPSF MNPPKGTTEF TD //