Tag | Content |
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CPLM ID | CPLM-002233 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 3-dehydroquinate dehydratase |
Protein Synonyms/Alias | 3-dehydroquinase; Type I DHQase |
Gene Name | aroD |
Gene Synonyms/Alias | b1693; JW1683 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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31 | AKDIASVKSEALAYR | acetylation | [1] | 66 | ESVMAAAKILRETMP | acetylation | [1] | 137 | YAHAHDVKVVMSNHD | acetylation | [1] | 147 | MSNHDFHKTPEAEEI | 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 46 48 Substrate binding (By similarity). ACT_SITE 143 143 Proton donor/acceptor. ACT_SITE 170 170 Schiff-base intermediate with substrate. BINDING 82 82 Substrate (By similarity). BINDING 213 213 Substrate (By similarity). BINDING 232 232 Substrate (By similarity). BINDING 236 236 Substrate (By similarity). |
Keyword | Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Complete proteome; Direct protein sequencing; Lyase; Reference proteome; Schiff base. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 252 AA |
Protein Sequence | MKTVTVKDLV IGTGAPKIIV SLMAKDIASV KSEALAYREA DFDILEWRVD HYADLSNVES 60 VMAAAKILRE TMPEKPLLFT FRSAKEGGEQ AISTEAYIAL NRAAIDSGLV DMIDLELFTG 120 DDQVKETVAY AHAHDVKVVM SNHDFHKTPE AEEIIARLRK MQSFDADIPK IALMPQSTSD 180 VLTLLAATLE MQEQYADRPI ITMSMAKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVN 240 DLRTVLTILH QA 252 |
Gene Ontology | GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:HAMAP. GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:HAMAP. GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. |
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PRINTS | |