PFKA5_ARATH
ID PFKA5_ARATH Reviewed; 537 AA.
AC Q8VYN6; Q9SJY6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=ATP-dependent 6-phosphofructokinase 5, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03186};
DE Short=ATP-PFK 5 {ECO:0000255|HAMAP-Rule:MF_03186};
DE Short=Phosphofructokinase 5 {ECO:0000255|HAMAP-Rule:MF_03186};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03186};
DE AltName: Full=Phosphohexokinase 5 {ECO:0000255|HAMAP-Rule:MF_03186};
DE Flags: Precursor;
GN Name=PFK5 {ECO:0000255|HAMAP-Rule:MF_03186}; OrderedLocusNames=At2g22480;
GN ORFNames=F14M13.12;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 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).
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;
CC Evidence={ECO:0000255|HAMAP-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: Plastid, chloroplast
CC {ECO:0000269|PubMed:17485088}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAD22353.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006592; AAD22353.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07312.1; -; Genomic_DNA.
DR EMBL; AY070402; AAL49898.1; -; mRNA.
DR EMBL; AY096578; AAM20228.1; -; mRNA.
DR PIR; B84613; B84613.
DR RefSeq; NP_850025.1; NM_179694.4.
DR AlphaFoldDB; Q8VYN6; -.
DR SMR; Q8VYN6; -.
DR BioGRID; 2134; 1.
DR STRING; 3702.AT2G22480.1; -.
DR iPTMnet; Q8VYN6; -.
DR PaxDb; Q8VYN6; -.
DR PRIDE; Q8VYN6; -.
DR ProteomicsDB; 236672; -.
DR EnsemblPlants; AT2G22480.1; AT2G22480.1; AT2G22480.
DR GeneID; 816781; -.
DR Gramene; AT2G22480.1; AT2G22480.1; AT2G22480.
DR KEGG; ath:AT2G22480; -.
DR Araport; AT2G22480; -.
DR TAIR; locus:2041208; AT2G22480.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_020655_7_1_1; -.
DR InParanoid; Q8VYN6; -.
DR OMA; YGHERFA; -.
DR OrthoDB; 380209at2759; -.
DR PhylomeDB; Q8VYN6; -.
DR BioCyc; ARA:AT2G22480-MON; -.
DR BRENDA; 2.7.1.11; 399.
DR UniPathway; UPA00109; UER00182.
DR PRO; PR:Q8VYN6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VYN6; baseline and differential.
DR Genevisible; Q8VYN6; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; ISS: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; ISS:TAIR.
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 Pfam; PF00365; PFK; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Chloroplast; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..537
FT /note="ATP-dependent 6-phosphofructokinase 5,
FT chloroplastic"
FT /id="PRO_0000330772"
FT REGION 35..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 309
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 253..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 278..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 307..309
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 352..354
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 408
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 460..463
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT SITE 280
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0F9"
SQ SEQUENCE 537 AA; 58615 MW; 5A9DD3004D1ACC6A CRC64;
MDALSQAISS GISVPYKNNS SSLVPSHGLT SLILRKSRSP VNPSSRSRVS VRASEIQHSK
TSASSIDLSD PDWKLKYEKD FEQRFSIPHI TDVLPDAEAI RSTFCLKMRS PTEDFVGGYP
SDEEWHGYIN NNDRVLLKVI SYSSPTSAGA ECLDHDCSWV EQWIHRAGPR EKIYFRPEEV
KAAIITCGGL CPGLNDVIRH IVITLEIYGV KNIVGIPFGY RGFSDKDLTE MPLSRKVVQN
IHLSGGSLLG VSRGGPSVSE IVDSMEERGI NMLFVLGGNG THAGANAIHN ECRKRKIKVA
VVGVPKTIDN DILHMDKTFG FDTAVEEAQR AINSAYIEAH SAYHGIGVVK LMGRNSGFIA
MQASLASGQV DICLIPEVPF NLHGPNGVLK HLKYLIETKG SAVICVAEGA GQNFLEKTNA
KDASGNAVLG DFGVYIQQET KKYFKEISTP IDVKYIDPTY MIRAVRANAS DGILCTVLGQ
NAVHGAFAGY SGITVGIINT HYAYLPITEV IAYPKSVDPN SRMWHRCLTS TGQPDFI
