| Tag |
Content |
LipidDB ID |
LipidDB-3702-00086 |
Entry Name |
|
UniProt Accession |
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Theoretical PI |
5.94 |
Molecular Weight |
82558.84 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Fructose-2,6-bisphosphatase |
Protein Synonyms/Alias |
6PF-2-K/Fru-2,6-P2ase; AtF2KP; PFK/FBPase; 2.7.1.105; 3.1.3.46; |
Gene Name |
FKFBP |
Gene Synonyms/Alias |
F2KP; At1g07110; F10K1.19; |
Created Date |
25-JAN-2012 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGSGASKNT | [1] | N-Myristoylation |
|
Organism |
Arabidopsis thaliana (Mouse-ear cress) |
NCBI Taxa ID |
3702 |
Reference |
[1] Boisson B, Giglione C, Meinnel T. Unexpected protein families including celldefense components feature in the N-myristoylome of a higher eukaryote. J BiolChem. 2003 Oct 31;278(44):43418-29. Epub 2003 Aug 11.[ PMID:12912986]
|
Functional Description |
Synthesis and degradation of fructose 2,6-bisphosphate. Regulates carbon partitioning between sucrose versus starch during the diurnal cycle. |
Sequence Annotation |
Domain: 17 122 CBM20.
Nucleotide-binding: 349 356 ATP.
Region: 301 549 6-phosphofructo-2-kinase.
Region: 550 744 Fructose-2,6-bisphosphatase.
Active site: 431 431
Active site: 460 460
Active site: 558 558 Tele-phosphohistidine intermediate.
Active site: 630 630
Active site: 696 696 Proton donor.
Binding site: 406 406 Fructose-6-phosphate.
Binding site: 496 496 Fructose-6-phosphate.
Modified residue: 220 220 Phosphoserine; by CPK3.
Modified residue: 276 276 Phosphoserine.
Modified residue: 295 295 Phosphoserine.
Modified residue: 303 303 Phosphoserine; by CPK3.
|
Protein Length |
744 AA. |
Protein Sequence
(Canonical) |
MGSGASKNTE EDDDGSNGGG GQLYVSLKME NSKVEGELTP HVYGSLPLIG SWDPSKALPM 60
QRESALMSEL SFVVPPDHET LDFKFLLKPK NRNTPCIVEE GENRLLTGGS LQGDARLALF 120
RLEGDVIVEF RVFINADRVS PIDLATSWRA YRENLQPSTV RGIPDVSINP DPKSAECPLE 180
SLELDLAHYE VPAPAPSANS YLVYAADNAE NPRSLSASGS FRNDSTPKAA QRNSEDSGVT 240
VDGSPSAKEM TIVVPDSSNI YSAFGEAESK SVETLSPFQQ KDGQKGLFVD RGVGSPRLVK 300
SLSASSFLID TKQIKNSMPA AAGAVAAAAV ADQMLGPKED RHLAIVLVGL PARGKTFTAA 360
KLTRYLRWLG HDTKHFNVGK YRRLKHGVNM SADFFRADNP EGVEARTEVA ALAMEDMIAW 420
MQEGGQVGIF DATNSTRVRR NMLMKMAEGK CKIIFLETLC NDERIIERNI RLKIQQSPDY 480
SEEMDFEAGV RDFRDRLANY EKVYEPVEEG SYIKMIDMVS GNGGQIQVNN ISGYLPGRIV 540
FFLVNTHLTP RPILLTRHGE SMDNVRGRIG GDSVISDSGK LYAKKLASFV EKRLKSEKAA 600
SIWTSTLQRT NLTASSIVGF PKVQWRALDE INAGVCDGMT YEEVKKNMPE EYESRKKDKL 660
RYRYPRGESY LDVIQRLEPV IIELERQRAP VVVISHQAVL RALYAYFADR PLKEIPQIEM 720
PLHTIIEIQM GVSGVQEKRY KLMD 744
|
FASTA
(Canonical) |
>LipidDB-3702-00086|Q9MB58
MGSGASKNTEEDDDGSNGGGGQLYVSLKMENSKVEGELTPHVYGSLPLIGSWDPSKALPM
QRESALMSELSFVVPPDHETLDFKFLLKPKNRNTPCIVEEGENRLLTGGSLQGDARLALF
RLEGDVIVEFRVFINADRVSPIDLATSWRAYRENLQPSTVRGIPDVSINPDPKSAECPLE
SLELDLAHYEVPAPAPSANSYLVYAADNAENPRSLSASGSFRNDSTPKAAQRNSEDSGVT
VDGSPSAKEMTIVVPDSSNIYSAFGEAESKSVETLSPFQQKDGQKGLFVDRGVGSPRLVK
SLSASSFLIDTKQIKNSMPAAAGAVAAAAVADQMLGPKEDRHLAIVLVGLPARGKTFTAA
KLTRYLRWLGHDTKHFNVGKYRRLKHGVNMSADFFRADNPEGVEARTEVAALAMEDMIAW
MQEGGQVGIFDATNSTRVRRNMLMKMAEGKCKIIFLETLCNDERIIERNIRLKIQQSPDY
SEEMDFEAGVRDFRDRLANYEKVYEPVEEGSYIKMIDMVSGNGGQIQVNNISGYLPGRIV
FFLVNTHLTPRPILLTRHGESMDNVRGRIGGDSVISDSGKLYAKKLASFVEKRLKSEKAA
SIWTSTLQRTNLTASSIVGFPKVQWRALDEINAGVCDGMTYEEVKKNMPEEYESRKKDKL
RYRYPRGESYLDVIQRLEPVIIELERQRAPVVVISHQAVLRALYAYFADRPLKEIPQIEM
PLHTIIEIQMGVSGVQEKRYKLMD
|
Gene Ontology |
GO:0005829; C:cytosol; IDA:TAIR GO:0005886; C:plasma membrane; IDA:TAIR GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:UniProtKB-EC GO:0005524; F:ATP binding; IEA:UniProtKB-KW GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IEA:UniProtKB-EC GO:2001070; F:starch binding; IEA:InterPro GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IDA:UniProtKB GO:0006002; P:fructose 6-phosphate metabolic process; IDA:UniProtKB GO:0006000; P:fructose metabolic process; IDA:UniProtKB GO:0043609; P:regulation of carbon utilization; IMP:UniProtKB |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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