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   24-JAN-2024, entry version 131.
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};
GN   OrderedLocusNames=At5g61580; 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; 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: 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.Q9FKG3; -.
DR   PaxDb; 3702-AT5G61580-1; -.
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; AT5G61580; PFK4.
DR   eggNOG; KOG2440; Eukaryota.
DR   InParanoid; Q9FKG3; -.
DR   OMA; PYIDQSF; -.
DR   OrthoDB; 995926at2759; -.
DR   PhylomeDB; Q9FKG3; -.
DR   BioCyc; ARA:AT5G61580-MONOMER; -.
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   GO; GO:0009507; C:chloroplast; 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:SF2; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 4, CHLOROPLASTIC; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
DR   Genevisible; Q9FKG3; AT.
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
//