Tag | Content |
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CPLM ID | CPLM-003788 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase |
Protein Synonyms/Alias | Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase |
Gene Name | hisA |
Gene Synonyms/Alias | b2024; JW2006 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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23 | LHQGDYGKQRDYGND | acetylation | [1] | 55 | LVDLTGAKDPAKRQI | acetylation | [1] | 66 | KRQIPLIKTLVAGVN | acetylation | [1] | 107 | VVGSTAVKSQDMVKG | acetylation | [1] | 113 | VKSQDMVKGWFERFG | acetylation | [1] | 232 | GRALLEGKFTVKEAI | 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 | ACT_SITE 7 7 Proton acceptor (By similarity). ACT_SITE 129 129 Proton donor (By similarity). |
Keyword | Amino-acid biosynthesis; Complete proteome; Cytoplasm; Histidine biosynthesis; Isomerase; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 245 AA |
Protein Sequence | MIIPALDLID GTVVRLHQGD YGKQRDYGND PLPRLQDYAA QGAEVLHLVD LTGAKDPAKR 60 QIPLIKTLVA GVNVPVQVGG GVRSEEDVAA LLEAGVARVV VGSTAVKSQD MVKGWFERFG 120 ADALVLALDV RIDEQGNKQV AVSGWQENSG VSLEQLVETY LPVGLKHVLC TDISRDGTLA 180 GSNVSLYEEV CARYPQVAFQ SSGGIGDIDD VAALRGTGVR GVIVGRALLE GKFTVKEAIA 240 CWQNA 245 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IDA:EcoCyc. GO:0000105; P:histidine biosynthetic process; IDA:EcoCyc. GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki. |
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