PFKA7_ARATH
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 03-AUG-2022, entry version 119.
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}; OrderedLocusNames=At5g56630;
GN 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;
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: 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; 6.
DR STRING; 3702.AT5G56630.1; -.
DR iPTMnet; Q9C5J7; -.
DR MetOSite; Q9C5J7; -.
DR PaxDb; Q9C5J7; -.
DR PRIDE; Q9C5J7; -.
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; locus:2165046; AT5G56630.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_020655_7_2_1; -.
DR InParanoid; Q9C5J7; -.
DR OMA; ITETQNN; -.
DR OrthoDB; 172878at2759; -.
DR PhylomeDB; Q9C5J7; -.
DR BioCyc; ARA:AT5G56630-MON; -.
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 Genevisible; Q9C5J7; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 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 PIRSF; PIRSF000534; PPi_PFK_TP0108; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
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
