ID   PFKA7_ARATH             Reviewed;         485 AA.
AC   Q9C5J7; Q9FJU5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase 7 {ECO:0000255|HAMAP-Rule:MF_03186};
DE            Short=ATP-PFK 7 {ECO:0000255|HAMAP-Rule:MF_03186};
DE            Short=Phosphofructokinase 7 {ECO:0000255|HAMAP-Rule:MF_03186};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03186};
DE   AltName: Full=Phosphohexokinase 7 {ECO:0000255|HAMAP-Rule:MF_03186};
GN   Name=PFK7 {ECO:0000255|HAMAP-Rule:MF_03186};
GN   OrderedLocusNames=At5g56630; ORFNames=MIK19.8;
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].
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: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03186,
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=BAB09881.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB013392; BAB09881.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED96790.1; -; Genomic_DNA.
DR   EMBL; AF360207; AAK25917.1; -; mRNA.
DR   EMBL; AY040055; AAK64113.1; -; mRNA.
DR   RefSeq; NP_568842.1; NM_125046.3.
DR   AlphaFoldDB; Q9C5J7; -.
DR   SMR; Q9C5J7; -.
DR   BioGRID; 21008; 5.
DR   IntAct; Q9C5J7; 7.
DR   STRING; 3702.Q9C5J7; -.
DR   iPTMnet; Q9C5J7; -.
DR   MetOSite; Q9C5J7; -.
DR   PaxDb; 3702-AT5G56630-1; -.
DR   ProteomicsDB; 236150; -.
DR   DNASU; 835764; -.
DR   EnsemblPlants; AT5G56630.1; AT5G56630.1; AT5G56630.
DR   GeneID; 835764; -.
DR   Gramene; AT5G56630.1; AT5G56630.1; AT5G56630.
DR   KEGG; ath:AT5G56630; -.
DR   Araport; AT5G56630; -.
DR   TAIR; AT5G56630; PFK7.
DR   eggNOG; KOG2440; Eukaryota.
DR   HOGENOM; CLU_020655_7_2_1; -.
DR   InParanoid; Q9C5J7; -.
DR   OMA; REEGHMV; -.
DR   OrthoDB; 995926at2759; -.
DR   PhylomeDB; Q9C5J7; -.
DR   BioCyc; ARA:AT5G56630-MONOMER; -.
DR   BRENDA; 2.7.1.11; 399.
DR   UniPathway; UPA00109; UER00182.
DR   PRO; PR:Q9C5J7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9C5J7; 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:SF34; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 7; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000534; PPi_PFK_TP0108; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
DR   Genevisible; Q9C5J7; AT.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..485
FT                   /note="ATP-dependent 6-phosphofructokinase 7"
FT                   /id="PRO_0000330774"
FT   REGION          449..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        220
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   BINDING         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   BINDING         164..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   BINDING         189..192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   BINDING         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   BINDING         218..220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   BINDING         263..265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   BINDING         319
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            191
FT                   /note="Important for substrate specificity; cannot use PPi
FT                   as phosphoryl donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
SQ   SEQUENCE   485 AA;  53482 MW;  6F0C6CFF43EAA7B5 CRC64;
     MSSPRSNKPK IVNGPGGYIL QDVPHLIDYL PDLPTYPNPL QDNPAYSVVK QYFVHADDSV
     PEKVVVHKDG PRGVHFRRAG PRQKVYFESD EVHACIVTCG GLCPGLNTVI REVVSSLSYM
     YGVKRILGID GGYRGFYAKN TIPLNSKVVN DIHKRGGTII GTSRGGHDTN KIVDSIQDRG
     INQVYIIGGD GTQRGASVIF EEIRRRRLKV AVVGIPKTID NDIPVIDKSF GFDTAVEEAQ
     RAINAAHVEA ESNENGIGFV KLMGRYSGYI AMYATLASRD VDCCLIPESP FYLEGEGGLF
     EFIERRLKDH GHMVIVLAEG AGQDLMCKSM ESTPMDASGN KLLKDVGLWL SQSIKDHFKK
     NKMVMNLKYI DPTYMIRAVP SNASDNVYCT LLAQSAVHGA MAGYTGYTSG LVNGRQTYIP
     FYRITETQNN VVITDRMWAR LLSSTNQPSF LGPKDTSEEK KELPETPLLD DGAVDIPPVT
     KEVTK
//