Tag | Content |
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CPLM ID | CPLM-002999 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Aspartate carbamoyltransferase regulatory chain |
Protein Synonyms/Alias | |
Gene Name | pyrI |
Gene Synonyms/Alias | b4244; JW4203 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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6 | **MTHDNKLQVEAIK | acetylation | [1] | 13 | KLQVEAIKRGTVIDH | acetylation | [1] | 28 | IPAQIGFKLLSLFKL | acetylation | [1] | 34 | FKLLSLFKLTETDQR | acetylation | [1] | 94 | DNYEVVGKSRPSLPE | acetylation | [1] | 137 | RANDIALKCKYCEKE | acetylation | [1] | 143 | LKCKYCEKEFSHNVV | 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 | Involved in allosteric regulation of aspartate carbamoyltransferase. |
Sequence Annotation | METAL 109 109 Zinc. METAL 114 114 Zinc. METAL 138 138 Zinc. METAL 141 141 Zinc. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Metal-binding; Pyrimidine biosynthesis; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 153 AA |
Protein Sequence | MTHDNKLQVE AIKRGTVIDH IPAQIGFKLL SLFKLTETDQ RITIGLNLPS GEMGRKDLIK 60 IENTFLSEDQ VDQLALYAPQ ATVNRIDNYE VVGKSRPSLP ERIDNVLVCP NSNCISHAEP 120 VSSSFAVRKR ANDIALKCKY CEKEFSHNVV LAN 153 |
Gene Ontology | GO:0009347; C:aspartate carbamoyltransferase complex; IEA:InterPro. GO:0005737; C:cytoplasm; IDA:UniProtKB. GO:0008270; F:zinc ion binding; IDA:EcoCyc. GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |