Tag | Content |
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CPLM ID | CPLM-002417 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Histidine biosynthesis bifunctional protein HisIE |
Protein Synonyms/Alias | Phosphoribosyl-AMP cyclohydrolase; PRA-CH; Phosphoribosyl-ATP pyrophosphatase; PRA-PH |
Gene Name | hisI |
Gene Synonyms/Alias | hisIE; b2026; JW2008 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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50 | DKTLESGKVTFFSRT | acetylation | [1] | 137 | PETSYTAKLYASGTK | acetylation | [1] | 149 | GTKRIAQKVGEEGVE | 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 | |
Sequence Annotation | REGION 1 114 Phosphoribosyl-AMP cyclohydrolase. REGION 115 203 Phosphoribosyl-ATP pyrophosphohydrolase. |
Keyword | Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; Histidine biosynthesis; Hydrolase; Multifunctional enzyme; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 203 AA |
Protein Sequence | MLTEQQRREL DWEKTDGLMP VIVQHAVSGE VLMLGYMNPE ALDKTLESGK VTFFSRTKQR 60 LWTKGETSGN FLNVVSIAPD CDNDTLLVLA NPIGPTCHKG TSSCFGDTAH QWLFLYQLEQ 120 LLAERKSADP ETSYTAKLYA SGTKRIAQKV GEEGVETALA ATVHDRFELT NEASDLMYHL 180 LVLLQDQGLD LTTVIENLRK RHQ 203 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; ISS:EcoCyc. GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IGI:EcoCyc. GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway. |
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PRINTS | |