| Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Thiamine-monophosphate kinase |
Protein Synonyms/Alias | TMP kinase; Thiamine-phosphate kinase |
Gene Name | thiL |
Gene Synonyms/Alias | SYNPCC7002_A1254 |
Created Date | 3-June-2014 |
Organism | Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) |
NCBI Taxa ID | 32049 |
Phosphorylation | Position | Peptide | Code | Type | References | | 133 | LTRSPVKTIGITAFG | T | HTP | [1] | | 143 | ITAFGVVSPHRAIQR | S | HTP | [1] | | 129 | VGGDLTRSPVKTIGI | S | HTP | [1] | |
Reference | [1]Global phosphoproteomic analysis reveals diverse functions of serine/threonine/tyrosine phosphorylation in the model cyanobacterium Synechococcus sp. strain PCC 7002. Yang MK,Qiao ZX,Zhang WY,Xiong Q,Zhang J,Li T,Ge F,Zhao JD J. Proteome Res. 2013, Apr, 5;12(4):1909-23. [ PMID:23461524] |
Functional Description From UniProt | FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1 (By similarity) |
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| ATP-binding; Completeproteome; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Thiaminebiosynthesis; Transferase |
Protein Sequence | MTAGKCLKDF GEAEILQRLQ RFCPAEIIGD DGAVLTFPPG QNLVVTTDVL VDGVHFGDRT 60
MPPEKVGWRA VAANLSDLAA MGATPIGITV GLSLPPETPI LWLDQLYQGL AACLGRYGTP 120
LVGGDLTRSP VKTIGITAFG VVSPHRAIQR SSAKVGDVIL VTGCHGDSRA GLELLLHTNA 180
RSQTLSIGDR QALIRAHQTP QPRLDVLPHL NSSDSPPAGM DSSDGLADAV LQICQRSGVG 240
AVVEAEKIPL SPALRRYQDP ETALRWALYG GEDFELVLCL PPMAAERLLA KLPGQGAIIG 300
QITAEQTVAI ANGAGQTMPL SQTQTFQHFA 330 |
| GO:0005524 F:ATP binding IEA:UniProtKB-HAMAP GO:0000287 F:magnesium ion binding IEA:UniProtKB-HAMAP GO:0009030 F:thiamine-phosphate kinase activity IEA:UniProtKB-HAMAP GO:0009228 P:thiamine biosynthetic process IEA:UniProtKB-KW GO:0009229 P:thiamine diphosphate biosynthetic process IEA:UniProtKB-HAMAP |
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