PFKA2_ARATH
ID PFKA2_ARATH Reviewed; 444 AA.
AC Q9FIK0;
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 2 {ECO:0000255|HAMAP-Rule:MF_03186};
DE Short=ATP-PFK 2 {ECO:0000255|HAMAP-Rule:MF_03186};
DE Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03186};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03186};
DE AltName: Full=Phosphohexokinase 2 {ECO:0000255|HAMAP-Rule:MF_03186};
GN Name=PFK2 {ECO:0000255|HAMAP-Rule:MF_03186}; OrderedLocusNames=At5g47810;
GN ORFNames=MCA23.13;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(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: Mostly expressed in roots and stems.
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; AB016886; BAB11328.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95574.1; -; Genomic_DNA.
DR EMBL; AY056779; AAL09725.1; -; mRNA.
DR EMBL; AY090379; AAL91281.1; -; mRNA.
DR RefSeq; NP_199592.1; NM_124155.3.
DR AlphaFoldDB; Q9FIK0; -.
DR SMR; Q9FIK0; -.
DR BioGRID; 20080; 7.
DR IntAct; Q9FIK0; 7.
DR STRING; 3702.AT5G47810.1; -.
DR PaxDb; Q9FIK0; -.
DR PRIDE; Q9FIK0; -.
DR ProteomicsDB; 236670; -.
DR EnsemblPlants; AT5G47810.1; AT5G47810.1; AT5G47810.
DR GeneID; 834832; -.
DR Gramene; AT5G47810.1; AT5G47810.1; AT5G47810.
DR KEGG; ath:AT5G47810; -.
DR Araport; AT5G47810; -.
DR TAIR; locus:2160897; AT5G47810.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_020655_7_3_1; -.
DR InParanoid; Q9FIK0; -.
DR OMA; WFAKQFA; -.
DR OrthoDB; 448001at2759; -.
DR PhylomeDB; Q9FIK0; -.
DR BioCyc; ARA:AT5G47810-MON; -.
DR BRENDA; 2.7.1.11; 399.
DR UniPathway; UPA00109; UER00182.
DR PRO; PR:Q9FIK0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIK0; baseline and differential.
DR Genevisible; Q9FIK0; 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; 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 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; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..444
FT /note="ATP-dependent 6-phosphofructokinase 2"
FT /id="PRO_0000330769"
FT ACT_SITE 205
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 149..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 174..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 203..205
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 248..250
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT BINDING 362..365
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT SITE 176
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0F9"
SQ SEQUENCE 444 AA; 49182 MW; 42E78785792A73EC CRC64;
MAAETSIRKL PSLSGLRHRR NPLEDNPYFH PSNGFYITPS DVILAQVAYD HSAHSQSRVA
YHRAGPRREI MYEPSAVKAA IVTCGGLCPG MNTVIRELVV GLWELYGVRE IYGIPAGYRG
FYSMKAVKLD PKAVHDWHKK GGTVLATSRG GFHLQKIVDA IHLNGYNQVY IIGGDGTMRG
AVEIFKEISL RKLEVGITVI PKTVDNDVGI IDRSFGFQTA VEMAQEAISA AHVEAESAVN
GIGLVKLMGR STGHIALHAT LSSRDVDCCL IPEMDFYLEG KGGLFEFLEK RLKERGHAVL
VVAEGAGQEM IPRNESQKQE RDESGNAVFL DVGVWFKSVL KAWWEREHPD ELFTVKYIDP
TYMIRAVPAN ATDNLYCTLL AHSAIHGVMA GYTGFVPGPI NGNYAYIPLE EVAQTKNQVN
TRDHKWAWVR SVTNQPDFET NVKG
