(data stored in SCRATCH zone)

SWISSPROT: PFKA3_ARATH

ID   PFKA3_ARATH             Reviewed;         489 AA.
AC   Q94AA4; Q9STQ7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 112.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase 3 {ECO:0000255|HAMAP-Rule:MF_03186};
DE            Short=ATP-PFK 3 {ECO:0000255|HAMAP-Rule:MF_03186};
DE            Short=Phosphofructokinase 3 {ECO:0000255|HAMAP-Rule:MF_03186};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03186};
DE   AltName: Full=Phosphohexokinase 3 {ECO:0000255|HAMAP-Rule:MF_03186};
GN   Name=PFK3 {ECO:0000255|HAMAP-Rule:MF_03186}; OrderedLocusNames=At4g26270;
GN   ORFNames=T25K17.80;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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 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=CAB38956.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79482.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL049171; CAB38956.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161564; CAB79482.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85178.1; -; Genomic_DNA.
DR   EMBL; AY049245; AAK83587.1; -; mRNA.
DR   EMBL; AY090267; AAL90928.1; -; mRNA.
DR   PIR; T06011; T06011.
DR   RefSeq; NP_567742.1; NM_118760.3.
DR   SMR; Q94AA4; -.
DR   BioGrid; 14020; 11.
DR   IntAct; Q94AA4; 5.
DR   STRING; 3702.AT4G26270.1; -.
DR   PaxDb; Q94AA4; -.
DR   PRIDE; Q94AA4; -.
DR   DNASU; 828733; -.
DR   EnsemblPlants; AT4G26270.1; AT4G26270.1; AT4G26270.
DR   GeneID; 828733; -.
DR   Gramene; AT4G26270.1; AT4G26270.1; AT4G26270.
DR   KEGG; ath:AT4G26270; -.
DR   Araport; AT4G26270; -.
DR   TAIR; locus:2136849; AT4G26270.
DR   eggNOG; KOG2440; Eukaryota.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000016186; -.
DR   InParanoid; Q94AA4; -.
DR   KO; K00850; -.
DR   OMA; PYIDQSF; -.
DR   OrthoDB; 448001at2759; -.
DR   PhylomeDB; Q94AA4; -.
DR   BioCyc; ARA:AT4G26270-MONOMER; -.
DR   BRENDA; 2.7.1.11; 399.
DR   UniPathway; UPA00109; UER00182.
DR   PRO; PR:Q94AA4; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q94AA4; baseline and differential.
DR   Genevisible; Q94AA4; AT.
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:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IDA:TAIR.
DR   GO; GO:0010053; P:root epidermal cell differentiation; IMP: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;
DR   PRODOM; Q94AA4.
DR   SWISS-2DPAGE; Q94AA4.
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..489
FT                   /note="ATP-dependent 6-phosphofructokinase 3"
FT                   /id="PRO_0000330770"
FT   NP_BIND         164..165
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   NP_BIND         189..192
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   REGION          218..220
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   REGION          263..265
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   REGION          375..378
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   ACT_SITE        220
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   METAL           190
FT                   /note="Magnesium; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   BINDING         101
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03186"
FT   BINDING         319
FT                   /note="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   489 AA;  53666 MW;  AE2C1EA15B64F7E0 CRC64;
     MSTVESSKPK IINGSCGYVL EDVPHLSDYL PGLPTYPNPL QDNPAYSVVK QYFVDADDSV
     PQKIVVHKDG PRGIHFRRAG PRQKVYFESD EVHACIVTCG GLCPGLNTVI REIVSSLSYM
     YGVKRILGID GGYRGFYAKN TVSLDSKVVN DIHKRGGTIL GTSRGGHDTT KIVDSIQDRG
     INQVYIIGGD GTQRGASVIF EEIRRRGLKV AVIGIPKTID NDIPVIDKSF GFDTAVEEAQ
     RAINAAHVEA ESIENGIGVV KLMGRYSGFI AMYATLASRD VDCCLIPESP FYLEGEGGLF
     EYIEKRLKES GHMVLVIAEG AGQDLMSKSM ESMTLKDASG NKLLKDVGLW LSQSIKDHFN
     QKKMVMNLKY IDPTYMIRAV PSNASDNVYC TLLAQSAVHG AMAGYTGYIS GLVNGRQTYI
     PFYRITEKQN HVVITDRMWA RLLSSTNQPS FLGPKDVFDN KEKPMSALLD DGNCNGVVDV
     PPVTKEITK
//

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