UniProt ID | THI4_SCHPO | |
---|---|---|
UniProt AC | P40998 | |
Protein Name | Thiamine thiazole synthase {ECO:0000255|HAMAP-Rule:MF_03158} | |
Gene Name | thi2 | |
Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
Sequence Length | 328 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.. | |
Protein Sequence | MAPATAVVTPQTAFKTDLPVEKTAHNTVVKSEMGALSKAYPTYSLDESFSFAPIRESTVSRAMTRRYFSDLDKYAESDIVIVGAGSAGLTAAYYIGTRRPDLKIAIIEASVAPGGGAWLGGQLFSAMVVRKPADLFLNEIGVPYEDEGDYVVVKHAALFTSTVMARTLALPNVKLFNATAVEDLIVKEGKDGKQRIAGVVTNWTLVSLNHGLQSCMDPNTINAHLVVSATGHDGPFGAFCVKRLASAQLVSNLHDMRPLDMNRAEDLIVKGTREVFPGMIVGGMELSEFDGANRMGPTFGGMMFSGIKAAQEALAIFDERKAVNEKYL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
5 | Phosphorylation | ---MAPATAVVTPQT ---CCCCEEEECCCC | 20.94 | 24763107 | |
9 | Phosphorylation | APATAVVTPQTAFKT CCCEEEECCCCCCCC | 11.77 | 24763107 | |
12 | Phosphorylation | TAVVTPQTAFKTDLP EEEECCCCCCCCCCC | 34.95 | 29996109 | |
16 | Phosphorylation | TPQTAFKTDLPVEKT CCCCCCCCCCCCEEC | 35.99 | 25720772 | |
23 | Phosphorylation | TDLPVEKTAHNTVVK CCCCCEECCCCHHHH | 21.46 | 24763107 | |
27 | Phosphorylation | VEKTAHNTVVKSEMG CEECCCCHHHHHHHH | 19.46 | 21712547 | |
31 | Phosphorylation | AHNTVVKSEMGALSK CCCHHHHHHHHHHHH | 22.62 | 29996109 | |
40 | Phosphorylation | MGALSKAYPTYSLDE HHHHHHCCCCCCCCC | 10.39 | 29996109 | |
42 | Phosphorylation | ALSKAYPTYSLDESF HHHHCCCCCCCCCCC | 17.05 | 29996109 | |
43 | Phosphorylation | LSKAYPTYSLDESFS HHHCCCCCCCCCCCC | 11.61 | 29996109 | |
44 | Phosphorylation | SKAYPTYSLDESFSF HHCCCCCCCCCCCCC | 31.64 | 29996109 | |
48 | Phosphorylation | PTYSLDESFSFAPIR CCCCCCCCCCCCCCC | 26.34 | 25720772 | |
57 | Phosphorylation | SFAPIRESTVSRAMT CCCCCCHHHHHHHHH | 25.02 | 29996109 | |
58 | Phosphorylation | FAPIRESTVSRAMTR CCCCCHHHHHHHHHH | 20.11 | 29996109 | |
60 | Phosphorylation | PIRESTVSRAMTRRY CCCHHHHHHHHHHHH | 17.89 | 29996109 | |
69 | Phosphorylation | AMTRRYFSDLDKYAE HHHHHHHCCHHHHCC | 28.47 | 25720772 | |
215 | Other | LNHGLQSCMDPNTIN CCCHHHHCCCCCCCC | 2.01 | - | |
246 | Phosphorylation | FCVKRLASAQLVSNL HHHHHHHHHHHHHCC | 22.57 | 25720772 | |
251 | Phosphorylation | LASAQLVSNLHDMRP HHHHHHHHCCHHCCC | 42.12 | 29996109 | |
287 | Phosphorylation | IVGGMELSEFDGANR EECCEEHHHCCCCCC | 23.94 | 25720772 | |
327 | Phosphorylation | RKAVNEKYL------ HHHHHHHCC------ | 16.09 | 25720772 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of THI4_SCHPO !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of THI4_SCHPO !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of THI4_SCHPO !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
THI4_SCHPO | thi2 | physical | 23695164 | |
THI4_SCHPO | thi2 | physical | 26771498 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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