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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei382 – 3821Fructose 6-phosphateBy similarity
Binding sitei406 – 4061Fructose 6-phosphateBy similarity
Active sitei431 – 4311Sequence analysis
Binding sitei433 – 4331Fructose 6-phosphateBy similarity
Binding sitei439 – 4391Fructose 6-phosphateBy similarity
Active sitei460 – 4601Sequence analysis
Binding sitei496 – 4961Fructose 6-phosphateBy similarity
Binding sitei500 – 5001Fructose 6-phosphateBy similarity
Binding sitei557 – 5571Fructose 2,6-bisphosphateBy similarity
Sitei557 – 5571Transition state stabilizerBy similarity
Active sitei558 – 5581Tele-phosphohistidine intermediateBy similarity
Binding sitei564 – 5641Fructose 2,6-bisphosphateBy similarity
Sitei564 – 5641Transition state stabilizerBy similarity
Binding sitei570 – 5701Fructose 2,6-bisphosphate; via amide nitrogenBy similarity
Active sitei630 – 6301Proton donor/acceptorBy similarity
Binding sitei641 – 6411Fructose 2,6-bisphosphateBy similarity
Binding sitei655 – 6551Fructose 2,6-bisphosphateBy similarity
Binding sitei659 – 6591Fructose 2,6-bisphosphateBy similarity
Binding sitei670 – 6701Fructose 2,6-bisphosphateBy similarity
Sitei696 – 6961Transition state stabilizerBy similarity
Binding sitei697 – 6971Fructose 2,6-bisphosphateBy similarity
Binding sitei701 – 7011Fructose 2,6-bisphosphateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi349 – 3579ATPBy similarity
Nucleotide bindingi469 – 4746ATPBy similarity
Nucleotide bindingi652 – 6554ATPBy similarity
Nucleotide bindingi697 – 7015ATPBy similarity

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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT1G07110-MONOMER.
BRENDAi2.7.1.105. 399.
3.1.3.46. 399.
ReactomeiR-ATH-70171. Glycolysis.
R-ATH-70263. Gluconeogenesis.

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

TAIRiAT1G07110.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 7447436-phosphofructo-2-kinase/fructose-2,6-bisphosphatasePRO_0000415319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei220 – 2201Phosphoserine; by CPK3Combined sources1 Publication
Modified residuei276 – 2761PhosphoserineCombined sources
Modified residuei295 – 2951PhosphoserineCombined sources
Modified residuei303 – 3031Phosphoserine; by CPK3Combined sources1 Publication

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

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. Positions 345-728.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 122106CBM20PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni301 – 5492496-phosphofructo-2-kinaseAdd
BLAST
Regioni550 – 744195Fructose-2,6-bisphosphataseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi320 – 33112Poly-AlaAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the phosphoglycerate mutase family.Curated
Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

Phylogenomic databases

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

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 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.
[Graphical view]
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM01065. CBM_2. 1 hit.
SM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
PS00175. PG_MUTASE. 1 hit.
[Graphical view]

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 AAF76986.1 differs from that shown. Reason: Frameshift at positions 278 and 288. Curated
The sequence AAF82210.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti629 – 6291D → A in AAF04293 (PubMed:10899575).Curated

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_100584.4.
UniGeneiAt.15685.

Genome annotation databases

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

Cross-referencesi

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_100584.4.
UniGeneiAt.15685.

3D structure databases

ProteinModelPortaliQ9MB58.
SMRiQ9MB58. Positions 345-728.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G07110.1.

PTM databases

iPTMnetiQ9MB58.

Proteomic databases

PaxDbiQ9MB58.
PRIDEiQ9MB58.
ProMEXiQ9MB58.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT1G07110.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciARA:AT1G07110-MONOMER.
BRENDAi2.7.1.105. 399.
3.1.3.46. 399.
ReactomeiR-ATH-70171. Glycolysis.
R-ATH-70263. Gluconeogenesis.

Miscellaneous databases

PROiQ9MB58.

Gene expression databases

GenevisibleiQ9MB58. AT.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.40.50.1240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003094. 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.
[Graphical view]
PANTHERiPTHR10606. PTHR10606. 1 hit.
PfamiPF01591. 6PF2K. 1 hit.
PF00300. His_Phos_1. 1 hit.
[Graphical view]
PRINTSiPR00991. 6PFRUCTKNASE.
SMARTiSM01065. CBM_2. 1 hit.
SM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF53254. SSF53254. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
PS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and heterologous expression of a gene encoding fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase from Arabidopsis thaliana."
    Villadsen D., Rung J.H., Draborg H., Nielsen T.H.
    Biochim. Biophys. Acta 1492:406-413(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION.
    Strain: cv. Columbia.
  2. "cDNA cloning of the gene for Fructose-6-phosphate,2-kinase/Fructose-2,6-bisphosphatase from Arabidopsis."
    Furumoto T., Ito M., Akira W.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 355-744.
    Strain: cv. Columbia.
  6. "N-terminal truncation affects the kinetics and structure of fructose-6-phosphate 2-kinase/fructose-2,6-bisphosphatase from Arabidopsis thaliana."
    Villadsen D., Nielsen T.H.
    Biochem. J. 359:591-597(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  7. "Transgenic Arabidopsis plants with decreased activity of fructose-6-phosphate,2-kinase/fructose-2,6-bisphosphatase have altered carbon partitioning."
    Draborg H., Villadsen D., Nielsen T.H.
    Plant Physiol. 126:750-758(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CARBON PARTITIONING.
  8. "Unexpected protein families including cell defense components feature in the N-myristoylome of a higher eukaryote."
    Boisson B., Giglione C., Meinnel T.
    J. Biol. Chem. 278:43418-43429(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  9. "Phosphorylation and 14-3-3 binding of Arabidopsis 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
    Kulma A., Villadsen D., Campbell D.G., Meek S.E.M., Harthill J.E., Nielsen T.H., MacKintosh C.
    Plant J. 37:654-667(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-220 AND SER-303 BY CPK3, INTERACTION WITH 14-3-3 PROTEINS.
  10. Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Root.
  11. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  12. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-276 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiF26_ARATH
AccessioniPrimary (citable) accession number: Q9MB58
Secondary accession number(s): Q8L7N6
, Q9LL39, Q9LMK3, Q9SP17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 102 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.