Tag | Content |
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CPLM ID | CPLM-003086 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Uracil phosphoribosyltransferase |
Protein Synonyms/Alias | UMP pyrophosphorylase; UPRTase |
Gene Name | upp |
Gene Synonyms/Alias | uraP; b2498; JW2483 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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2 | ******MKIVEVKHP | acetylation | [1] | 7 | *MKIVEVKHPLVKHK | acetylation | [1] | 67 | PVEIDQIKGKKITVV | acetylation | [1] | 69 | EIDQIKGKKITVVPI | acetylation | [1] | 70 | IDQIKGKKITVVPIL | acetylation | [1] | 116 | EPVPYFQKLVSNIDE | acetylation | [1] | 203 | GLGDAGDKIFGTK** | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Catalyzes the conversion of uracil and 5-phospho-alpha- D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. |
Sequence Annotation | REGION 130 138 5-phospho-alpha-D-ribose 1-diphosphate REGION 198 200 Uracil binding (By similarity). BINDING 78 78 5-phospho-alpha-D-ribose 1-diphosphate BINDING 103 103 5-phospho-alpha-D-ribose 1-diphosphate BINDING 193 193 Uracil; via amide nitrogen (By BINDING 199 199 5-phospho-alpha-D-ribose 1-diphosphate |
Keyword | 3D-structure; Allosteric enzyme; Complete proteome; Direct protein sequencing; Glycosyltransferase; GTP-binding; Magnesium; Nucleotide-binding; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 208 AA |
Protein Sequence | MKIVEVKHPL VKHKLGLMRE QDISTKRFRE LASEVGSLLT YEATADLETE KVTIEGWNGP 60 VEIDQIKGKK ITVVPILRAG LGMMDGVLEN VPSARISVVG MYRNEETLEP VPYFQKLVSN 120 IDERMALIVD PMLATGGSVI ATIDLLKKAG CSSIKVLVLV AAPEGIAALE KAHPDVELYT 180 ASIDQGLNEH GYIIPGLGDA GDKIFGTK 208 |
Gene Ontology | |
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