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Protein

6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase

Gene

FKFBP

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Synthesis and degradation of fructose 2,6-bisphosphate. Regulates carbon partitioning between sucrose versus starch during the diurnal cycle.3 Publications

Catalytic activityi

Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.1 Publication
ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.1 Publication

Enzyme regulationi

6-phosphofructo-2-kinase activity is activated by pyruvate. 6-phosphofructo-2-kinase activity is inhibited by PPi, phosphoenolpyruvate and 2-phosphoglycerate. Fructose-2,6-bisphosphatase activity is inhibited by pyruvate, fructose 1,6-bisphosphate and 6-phosphogluconate.1 Publication

Kineticsi

  1. KM=0.5 mM for fructose-6-phosphate for the 6-phosphofructo-2-kinase activity (at pH 6.0 and 25 degrees Celsius)1 Publication
  2. KM=0.19 mM for ATP for the 6-phosphofructo-2-kinase activity (at pH 6.0 and 25 degrees Celsius)1 Publication
  3. KM=0.028 mM for fructose-2,6-bisphosphate for the fructose-2,6-bisphosphatase activity (at pH 6.0 and 25 degrees Celsius)1 Publication
  1. Vmax=180 nmol/min/mg enzyme with fructose-6-phosphate as substrate for the 6-phosphofructo-2-kinase activity (at pH 6.0 and 25 degrees Celsius)1 Publication
  2. Vmax=270 nmol/min/mg enzyme with fructose-2,6-bisphosphate as substrate for the fructose-2,6-bisphosphatase activity (at pH 6.0 and 25 degrees Celsius)1 Publication

Temperature dependencei

Inactivated by mild heat treatment (42 degrees Celsius during 10 minutes).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei382Fructose 6-phosphateBy similarity1
Binding sitei406Fructose 6-phosphateBy similarity1
Active sitei431Sequence analysis1
Binding sitei433Fructose 6-phosphateBy similarity1
Binding sitei439Fructose 6-phosphateBy similarity1
Active sitei460Sequence analysis1
Binding sitei496Fructose 6-phosphateBy similarity1
Binding sitei500Fructose 6-phosphateBy similarity1
Binding sitei557Fructose 2,6-bisphosphateBy similarity1
Sitei557Transition state stabilizerBy similarity1
Active sitei558Tele-phosphohistidine intermediateBy similarity1
Binding sitei564Fructose 2,6-bisphosphateBy similarity1
Sitei564Transition state stabilizerBy similarity1
Binding sitei570Fructose 2,6-bisphosphate; via amide nitrogenBy similarity1
Active sitei630Proton donor/acceptorBy similarity1
Binding sitei641Fructose 2,6-bisphosphateBy similarity1
Binding sitei655Fructose 2,6-bisphosphateBy similarity1
Binding sitei659Fructose 2,6-bisphosphateBy similarity1
Binding sitei670Fructose 2,6-bisphosphateBy similarity1
Sitei696Transition state stabilizerBy similarity1
Binding sitei697Fructose 2,6-bisphosphateBy similarity1
Binding sitei701Fructose 2,6-bisphosphateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi349 – 357ATPBy similarity9
Nucleotide bindingi469 – 474ATPBy similarity6
Nucleotide bindingi652 – 655ATPBy similarity4
Nucleotide bindingi697 – 701ATPBy similarity5

GO - Molecular functioni

GO - Biological processi

  • fructose 2,6-bisphosphate metabolic process Source: UniProtKB
  • fructose 6-phosphate metabolic process Source: UniProtKB
  • fructose metabolic process Source: UniProtKB
  • regulation of carbon utilization Source: UniProtKB

Keywordsi

Molecular functionHydrolase, Kinase, Transferase
Biological processCarbohydrate metabolism
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT1G07110-MONOMER.
BRENDAi2.7.1.105. 399.
3.1.3.46. 399.
ReactomeiR-ATH-70171. Glycolysis.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Short name:
6PF-2-K/Fru-2,6-P2ase
Short name:
AtF2KP
Short name:
PFK/FBPase
Including the following 2 domains:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
Gene namesi
Name:FKFBP
Synonyms:F2KP
Ordered Locus Names:At1g07110
ORF Names:F10K1.19
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

AraportiAT1G07110.
TAIRilocus:2007367. AT1G07110.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00004153192 – 7446-phosphofructo-2-kinase/fructose-2,6-bisphosphataseAdd BLAST743

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine1 Publication1
Modified residuei220Phosphoserine; by CPK3Combined sources1 Publication1
Modified residuei276PhosphoserineCombined sources1
Modified residuei295PhosphoserineCombined sources1
Modified residuei303Phosphoserine; by CPK3Combined sources1 Publication1

Post-translational modificationi

Phosphorylation at Ser-220 and Ser-303 by CPK3 promotes 14-3-3 proteins binding.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiQ9MB58.
PRIDEiQ9MB58.
ProMEXiQ9MB58.

PTM databases

iPTMnetiQ9MB58.

Expressioni

Gene expression databases

ExpressionAtlasiQ9MB58. baseline and differential.
GenevisibleiQ9MB58. AT.

Interactioni

Subunit structurei

Interacts with 14-3-3 proteins; these interactions may regulate both nitrate assimilation and sucrose/starch partitioning in leaves during the diurnal cycle.1 Publication

Protein-protein interaction databases

STRINGi3702.AT1G07110.1.

Structurei

3D structure databases

ProteinModelPortaliQ9MB58.
SMRiQ9MB58.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 122CBM20PROSITE-ProRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni301 – 5496-phosphofructo-2-kinaseAdd BLAST249
Regioni550 – 744Fructose-2,6-bisphosphataseAdd BLAST195

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi320 – 331Poly-AlaAdd BLAST12

Sequence similaritiesi

In the C-terminal section; belongs to the phosphoglycerate mutase family.Curated

Phylogenomic databases

eggNOGiKOG0234. Eukaryota.
COG0406. LUCA.
HOGENOMiHOG000181112.
InParanoidiQ9MB58.
KOiK01103.
OMAiRESTSMW.
OrthoDBiEOG0936039Z.
PhylomeDBiQ9MB58.

Family and domain databases

CDDicd07067. HP_PGM_like. 1 hit.
Gene3Di2.60.40.10. 1 hit.
3.40.50.1240. 1 hit.
InterProiView protein in InterPro
IPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR013783. Ig-like_fold.
IPR027417. P-loop_NTPase.
IPR001345. PG/BPGM_mutase_AS.
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiView protein in Pfam
PF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiView protein in SMART
SM01065. CBM_2. 1 hit.
SM00855. PGAM. 1 hit.
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiView protein in PROSITE
PS51166. CBM20. 1 hit.
PS00175. PG_MUTASE. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9MB58-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSGASKNTE EDDDGSNGGG GQLYVSLKME NSKVEGELTP HVYGSLPLIG
60 70 80 90 100
SWDPSKALPM QRESALMSEL SFVVPPDHET LDFKFLLKPK NRNTPCIVEE
110 120 130 140 150
GENRLLTGGS LQGDARLALF RLEGDVIVEF RVFINADRVS PIDLATSWRA
160 170 180 190 200
YRENLQPSTV RGIPDVSINP DPKSAECPLE SLELDLAHYE VPAPAPSANS
210 220 230 240 250
YLVYAADNAE NPRSLSASGS FRNDSTPKAA QRNSEDSGVT VDGSPSAKEM
260 270 280 290 300
TIVVPDSSNI YSAFGEAESK SVETLSPFQQ KDGQKGLFVD RGVGSPRLVK
310 320 330 340 350
SLSASSFLID TKQIKNSMPA AAGAVAAAAV ADQMLGPKED RHLAIVLVGL
360 370 380 390 400
PARGKTFTAA KLTRYLRWLG HDTKHFNVGK YRRLKHGVNM SADFFRADNP
410 420 430 440 450
EGVEARTEVA ALAMEDMIAW MQEGGQVGIF DATNSTRVRR NMLMKMAEGK
460 470 480 490 500
CKIIFLETLC NDERIIERNI RLKIQQSPDY SEEMDFEAGV RDFRDRLANY
510 520 530 540 550
EKVYEPVEEG SYIKMIDMVS GNGGQIQVNN ISGYLPGRIV FFLVNTHLTP
560 570 580 590 600
RPILLTRHGE SMDNVRGRIG GDSVISDSGK LYAKKLASFV EKRLKSEKAA
610 620 630 640 650
SIWTSTLQRT NLTASSIVGF PKVQWRALDE INAGVCDGMT YEEVKKNMPE
660 670 680 690 700
EYESRKKDKL RYRYPRGESY LDVIQRLEPV IIELERQRAP VVVISHQAVL
710 720 730 740
RALYAYFADR PLKEIPQIEM PLHTIIEIQM GVSGVQEKRY KLMD
Length:744
Mass (Da):82,559
Last modified:October 1, 2000 - v1
Checksum:i61EA630DFA01F38A
GO

Sequence cautioni

The sequence AAF76986 differs from that shown. Reason: Frameshift at positions 278 and 288.Curated
The sequence AAF82210 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti629D → A in AAF04293 (PubMed:10899575).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190739 mRNA. Translation: AAF04293.2.
AF242859 Genomic DNA. Translation: AAF76986.1. Frameshift.
AB035288 mRNA. Translation: BAA96353.1.
AC067971 Genomic DNA. Translation: AAF82210.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28077.1.
AY128346 mRNA. Translation: AAM91549.1.
PIRiH86205.
RefSeqiNP_172191.1. NM_100584.5.
UniGeneiAt.15685.

Genome annotation databases

EnsemblPlantsiAT1G07110.1; AT1G07110.1; AT1G07110.
GeneIDi837221.
GrameneiAT1G07110.1; AT1G07110.1; AT1G07110.
KEGGiath:AT1G07110.

Similar proteinsi

Entry informationi

Entry nameiF26_ARATH
AccessioniPrimary (citable) accession number: Q9MB58
Secondary accession number(s): Q8L7N6
, Q9LL39, Q9LMK3, Q9SP17
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: October 1, 2000
Last modified: September 27, 2017
This is version 109 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families