| Tag |
Content |
LipidDB ID |
LipidDB-36329-01244 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
7.99 |
Molecular Weight |
56150.28 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
Inosine-5'-monophosphate dehydrogenase |
Protein Synonyms/Alias |
IMP dehydrogenase; IMPD; IMPDH; 1.1.1.205; |
Gene Name |
|
Gene Synonyms/Alias |
PFI1020c; |
Created Date |
01-MAR-2003 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
255 | Canonical | KNMIDVICIDSSQGN | [1] | S-Palmitoylation | 314 | Canonical | GMGSGSICTTQDVCA | [1] | S-Palmitoylation |
|
Organism |
Plasmodium falciparum (isolate 3D7) |
NCBI Taxa ID |
36329 |
Reference |
[1] Predicted from GPS-Lipid
|
Functional Description |
Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. |
Sequence Annotation |
Domain: 101 160 CBS 1.
Domain: 164 220 CBS 2.
Nucleotide-binding: 257 259 NAD.
Nucleotide-binding: 307 309 NAD.
Region: 347 349 IMP binding.
Region: 370 371 IMP binding.
Region: 394 398 IMP binding.
Active site: 314 314 Thioimidate intermediate.
Metal binding site: 309 309 Potassium; via carbonyl oxygen.
Metal binding site: 311 311 Potassium; via carbonyl oxygen.
Metal binding site: 314 314 Potassium; via carbonyl oxygen.
Binding site: 312 312 IMP.
Binding site: 435 435 IMP.
|
Protein Length |
510 AA. |
Protein Sequence
(Canonical) |
MASGWKADEV FGGVMSYTYD DIICMPGYID FALSDIDLTN NMTDNITLKT PVISSPMDTV 60
TGHKMSIALA LSGGLGVIHN NMSIEKQIEE VKKVKRFENG FIFDPYTFSP EHTVADVLET 120
KNRVGYKSYP ITVDGKVGSK LVGIITGVDY LYLTNKSMKI GDIMTTDVVT GSYPINLSDA 180
NKVLCDEKKS VLPIVNKNNE LIALVCRNDM HKNRIFPHAS KSQNKQLIVG ASISTREHDL 240
ERANQLIKNM IDVICIDSSQ GNSIYQIDTI KKIKSAHPDI PIIGGNVVTS QQAKNLIDAG 300
ADVLRIGMGS GSICTTQDVC AVGRAQGTAV YHVSKYAHTR NIKTIADGGI KNSGNIVKAL 360
SLGADFVMLG NLLAATEESC SEYYFENNVR LKIYRGMGSM EAMYNKGFNS KSRYLVDERK 420
NEYTDENIDE IKVSQGVSAS LVDKGSVLNL IPHLFKAVKH GFQSMGIRNI PELHSKLYSG 480
DIRFDVRSFN TIKEGKVSDN LIFNNKKFTT 510
|
FASTA
(Canonical) |
>LipidDB-36329-01244|Q8I2U5
MASGWKADEVFGGVMSYTYDDIICMPGYIDFALSDIDLTNNMTDNITLKTPVISSPMDTV
TGHKMSIALALSGGLGVIHNNMSIEKQIEEVKKVKRFENGFIFDPYTFSPEHTVADVLET
KNRVGYKSYPITVDGKVGSKLVGIITGVDYLYLTNKSMKIGDIMTTDVVTGSYPINLSDA
NKVLCDEKKSVLPIVNKNNELIALVCRNDMHKNRIFPHASKSQNKQLIVGASISTREHDL
ERANQLIKNMIDVICIDSSQGNSIYQIDTIKKIKSAHPDIPIIGGNVVTSQQAKNLIDAG
ADVLRIGMGSGSICTTQDVCAVGRAQGTAVYHVSKYAHTRNIKTIADGGIKNSGNIVKAL
SLGADFVMLGNLLAATEESCSEYYFENNVRLKIYRGMGSMEAMYNKGFNSKSRYLVDERK
NEYTDENIDEIKVSQGVSASLVDKGSVLNLIPHLFKAVKHGFQSMGIRNIPELHSKLYSG
DIRFDVRSFNTIKEGKVSDNLIFNNKKFTT
|
Gene Ontology |
GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell GO:0030554; F:adenyl nucleotide binding; IEA:InterPro GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-HAMAP GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-HAMAP |
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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