PFKA4_ARATH
ID PFKA4_ARATH Reviewed; 530 AA.
AC Q9FKG3; Q2V2W5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ATP-dependent 6-phosphofructokinase 4, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03186};
DE Short=ATP-PFK 4 {ECO:0000255|HAMAP-Rule:MF_03186};
DE Short=Phosphofructokinase 4 {ECO:0000255|HAMAP-Rule:MF_03186};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03186};
DE AltName: Full=Phosphohexokinase 4 {ECO:0000255|HAMAP-Rule:MF_03186};
DE Flags: Precursor;
GN Name=PFK4 {ECO:0000255|HAMAP-Rule:MF_03186}; OrderedLocusNames=At5g61580;
GN ORFNames=K11J9.3;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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] (ISOFORM 1).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FKG3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FKG3-2; Sequence=VSP_033114;
CC -!- TISSUE SPECIFICITY: Expressed in 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}.
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DR EMBL; AB012239; BAB09002.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97492.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97493.1; -; Genomic_DNA.
DR EMBL; AY099694; AAM20545.1; -; mRNA.
DR EMBL; AY128873; AAM91273.1; -; mRNA.
DR RefSeq; NP_001032120.1; NM_001037043.1. [Q9FKG3-2]
DR RefSeq; NP_200966.2; NM_125551.4. [Q9FKG3-1]
DR AlphaFoldDB; Q9FKG3; -.
DR SMR; Q9FKG3; -.
DR BioGRID; 21523; 1.
DR STRING; 3702.AT5G61580.1; -.
DR PaxDb; Q9FKG3; -.
DR PRIDE; Q9FKG3; -.
DR ProteomicsDB; 236671; -. [Q9FKG3-1]
DR EnsemblPlants; AT5G61580.1; AT5G61580.1; AT5G61580. [Q9FKG3-1]
DR EnsemblPlants; AT5G61580.2; AT5G61580.2; AT5G61580. [Q9FKG3-2]
DR GeneID; 836279; -.
DR Gramene; AT5G61580.1; AT5G61580.1; AT5G61580. [Q9FKG3-1]
DR Gramene; AT5G61580.2; AT5G61580.2; AT5G61580. [Q9FKG3-2]
DR KEGG; ath:AT5G61580; -.
DR Araport; AT5G61580; -.
DR TAIR; locus:2151571; AT5G61580.
DR eggNOG; KOG2440; Eukaryota.
DR InParanoid; Q9FKG3; -.
DR OMA; PYIDQSF; -.
DR PhylomeDB; Q9FKG3; -.
DR BioCyc; ARA:AT5G61580-MON; -.
DR BRENDA; 2.7.1.11; 399.
DR UniPathway; UPA00109; UER00182.
DR PRO; PR:Q9FKG3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKG3; baseline and differential.
DR Genevisible; Q9FKG3; 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; 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 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; Alternative splicing; ATP-binding; Chloroplast;
KW Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..530
FT /note="ATP-dependent 6-phosphofructokinase 4,
FT chloroplastic"
FT /id="PRO_0000330771"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 215..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 240..243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 269..271
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 314..316
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 427..430
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT SITE 242
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0F9"
FT VAR_SEQ 476
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_033114"
SQ SEQUENCE 530 AA; 58467 MW; 7CF9AC8460F44DF4 CRC64;
MEASISFLGS TKPNISLFNP SSNVLPRRDF PLPALKLKKV SVLPRILHQK RLIRAQCSDG
FKPEEDDGFV LEDVPHLTKF LPDLPSYPNP LKESQAYAIV KRTFVSSEDV VAQNIVVQKG
SKRGVHFRRA GPRERVYFRS DEVKACIVTC GGLCPGINTV IREIVCGLNN MYGVNNILGI
QGGYRGFYSK NTMNLTPKVV NDIHKRGGTF LQTSRGGHDT AKIVDNIQDR GINQVYIIGG
GGTQKGAEKI YEEVERRGLQ VAVSGIPKTI DNDIAVIDKS FGFDTAVEEA QRAINAAHVE
VESVENGVGI VKLMGRYSGF IAMIATLANR DVDCCLIPES PFFLEGKGGL FEFIEERLKE
NRHMVIVIAE GAGQDYVAQS MRASETKDAS GNRLLLDVGL WLTQQIKDHF TNVRKMMINM
KYIDPTYMIR AIPSNASDNV YCTLLAQSAV HGAMAGYSGF TVGPVNSRHA YIPISQVTEV
TNTVKLTDRM WARLLASTNQ PSFLTGEGAL QNVIDMETQE KIDNMKISSI
