IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Dimethyl sulfoxide reductase of Escherichia coli: an investigation of function and assembly by use of in vivo complementation. Dimethyl sulfoxide reductase of Escherichia coli: an investigation of function and assembly by use of in vivo complementation. Journal of bacteriology 1991 imex curation Sambasivarao D., Weiner JH. I cannot re-add the "reject" comments at Experiment level (editor appears to save and then loses them) - so have copied at Publication level. pmid:21357619 - Tang 2011 curated by yourself-also has several enzyme assays - but as it would appear they do not use purified enzymes (or no mention that I could find) so I accepted that publication. Only protein-protein interactions in vitro In vitro oxidoreduct assay oxidoreductase assay oxidoreduct assay predetermined predetermined participant predetermined Sambasivarao D., Weiner JH. I cannot re-add the "reject" comments at Experiment level (editor appears to save and then loses them) - so have copied at Publication level. pmid:21357619 - Tang 2011 curated by yourself-also has several enzyme assays - but as it would appear they do not use purified enzymes (or no mention that I could find) so I accepted that publication. The dmsABC proteins were introduced into the cell on a plasmid containing the entire dmsABC operon. Triton X-100 E.coli membrane extracts were cleared by centrifugation then applied to a DE-52 column and extracted by salt gradient. Active fractions were further purified by Sephacryl S-300 HR column chromatography. The enzyme had a specific activity of 736 units/mg using TMAO as substrate column Accepted 2016-JUL-05 AT 10:41 BST AT 10:41 BST by MGT Journal of bacteriology 1991 imex curation Mock publication and experiment for abstract interactions that are not interaction evidences. Mock publication and experiment for abstract interactions that are not interaction evidences. unspecified method Dimethyl sulfoxide reductase of Escherichia coli: an investigation of function and assembly by use of in vivo complementation. Dimethyl sulfoxide reductase of Escherichia coli: an investigation of function and assembly by use of in vivo complementation. Journal of bacteriology 1991 imex curation Sambasivarao D., Weiner JH. I cannot re-add the "reject" comments at Experiment level (editor appears to save and then loses them) - so have copied at Publication level. pmid:21357619 - Tang 2011 curated by yourself-also has several enzyme assays - but as it would appear they do not use purified enzymes (or no mention that I could find) so I accepted that publication. Only protein-protein interactions ecoli Escherichia coli (strain K12) ion exchange chrom ion exchange chromatography IEC IEC ion exchange chrom western blot western blot Immuno blot Immuno blot Sambasivarao D., Weiner JH. I cannot re-add the "reject" comments at Experiment level (editor appears to save and then loses them) - so have copied at Publication level. pmid:21357619 - Tang 2011 curated by yourself-also has several enzyme assays - but as it would appear they do not use purified enzymes (or no mention that I could find) so I accepted that publication. The dmsABC proteins were introduced into the cell on a plasmid containing the entire dmsABC operon. Triton X-100 E.coli membrane extracts were cleared by centrifugation then applied to a DE-52 column and extracted by salt gradient. Active fractions were further purified by Sephacryl S-300 HR column chromatography. The enzyme had a specific activity of 736 units/mg using TMAO as substrate column Accepted 2016-JUL-05 AT 10:41 BST AT 10:41 BST by MGT Journal of bacteriology 1991 imex curation dmsb_ecoli Anaerobic dimethyl sulfoxide reductase chain B DMSO reductase iron-sulfur subunit dmsB b0895 JW0878 protein protein ecoli Escherichia coli (strain K12) MTTQYGFFIDSSRCTGCKTCELACKDYKDLTPEVSFRRIYEYAGGDWQEDNGVWHQNVFAYYLSISCNHCEDPACTKVCPSGAMHKREDGFVVVDEDVCIGCRYCHMACPYGAPQYNETKGHMTKCDGCYDRVAEGKKPICVESCPLRALDFGPIDELRKKHGDLAAVAPLPRAHFTKPNIVIKPNANSRPTGDTTGYLANPKEV 7EC4417EED0809C6 tetra-mu3-sulfido-tetrairon tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) trimethylamine n-oxide trimethylamine N-oxide (CH3)3NO Me3N(+)O(-) Me3N(O) N(CH3)3O TMAO Trimethylamine N-oxide trimethylamine N-oxide trimethylamine oxide Trimethylaminoxid trimethyloxamine N,N-dimethylmethanamine oxide small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) dimethyl sulfoxide dimethyl sulfoxide (CH3)2SO Dimethyl sulfoxide DIMETHYL SULFOXIDE dimethyl sulfoxide dimethyl sulfur oxide dimethyl sulphoxide dimethyli sulfoxidum Dimethylsulfoxid dimethylsulfoxyde dimetil sulfoxido DMSO dmso methylsulfinylmethane S(O)Me2 sulfinylbis(methane) (methanesulfinyl)methane dimethyl sulfoxide small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) dmsc_ecoli Anaerobic dimethyl sulfoxide reductase chain C dmsC DMSO reductase anchor subunit JW0879 b0896 protein protein ecoli Escherichia coli (strain K12) MGSGWHEWPLMIFTVFGQCVAGGFIVLALALLKGDLRAEAQQRVIACMFGLWVLMGIGFIASMLHLGSPMRAFNSLNRVGASALSNEIASGSIFFAVGGIGWLLAMLKKLSPALRTLWLIVTMVLGVIFVWMMVRVYNSIDTVPTWYSIWTPMGFFLTMFMGGPLLGYLLLSLAGVDGWAMRLLPAISVLALVVSGVVSVMQGAELATIHSSVQQAAALVPDYGALMSWRIVLLAVALCLWIAPQLKGYQPAVPLLSVSFILLLAGELIGRGVFYGLHMTVGMAVAS DB6D26ACD2BE0CEB dmsa_ecoli Dimethyl sulfoxide reductase DmsA dmsA b0894 JW5118 protein protein ecoli Escherichia coli (strain K12) MKTKIPDAVLAAEVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSAIPTKSDEKVIWSACTVNCGSRCPLRMHVVDGEIKYVETDNTGDDNYDGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNYGTGTLGGTMTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGGVTYYLEQARQKSNARMIIIDPRYTDTGAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQAFLDKYCVGYDEKTLPASAPKNGHYKAYILGEGPDGVAKTPEWASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWNYAGNCLINQHSEINRTHEILQDDKKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFALDASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYAQSREAIPELPTFEEFRKQGIFKKRDPQGHHVAYKAFREDPQANPLTTPSGKIEIYSQALADIAATWELPEGDVIDPLPIYTPGFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKAACRQEMWINPLDAQKRGIHNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPDAKRVDKGGCINVLTTQRPSPLAKGNPSHTNLVQVEKV DIP protein P18775 original sequence version: 96 B97C830ABAC7C32C mo(=o)-bis(molybdopterin guanine dinucleotide)(4-) Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-) Mo(=O)-bis(molybdopterin guanine dinucleotide) tetraanion Mo-bis(molybdopterin guanine dinucleotide) molybdate-bis(molybdopterin guanine dinucleotide) tetraanion small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) dmsa-dmsb-1 3 4 unspecified role unspecified role neutral component neutral component 9 unspecified role unspecified role neutral component neutral component physical association physical association Fig. 5 dimethyl sulfoxide-dmsabc_ecoli-1 1 7 enzyme target enzyme target substrate substrate unspecified role unspecified role 17 enzyme enzyme unspecified role unspecified role ecoli Escherichia coli (strain K12) redox reaction oxidoreductase activity electron transfer reaction redox reaction Table 3, Table 5, Fig. 6 Relatively weak activity was demonstrated when methyl-violet was the electron donor, stronger activity when DMNH2 was the donor molecule. dmsabc_ecoli-trimethylamine n_oxide-1 1 6 enzyme target enzyme target substrate substrate unspecified role unspecified role 17 enzyme enzyme unspecified role unspecified role ecoli Escherichia coli (strain K12) redox reaction oxidoreductase activity electron transfer reaction redox reaction Table 3, Fig. 6 dmsabc_ecoli DMSOR complex Dimethylsulfoxide reductase complex DmaABC DMSO reductase complex dmsA:dmsB:dmsC 5 cofactor cofactor coenzyme dmsB binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 5 cofactor cofactor coenzyme dmsA binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 8 unspecified role unspecified role dmsB binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 4 unspecified role unspecified role dmsc binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain dmsA binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [4Fe-4S] binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 9 enzyme enzyme dmsB binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [4Fe-4S] binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Mo-bis-MGD binding site binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 10 cofactor cofactor coenzyme dmsA binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 30 22 24 33 28 26 29 32 34 36 physical association physical association ecoli Escherichia coli (strain K12) stable complex stable complex physical interaction evidence used in manual assertion physical interaction evidence used in manual assertion IPI inferred from physical interaction Terminal reductase required for the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS) and that of a broad array of S- and N-oxide compounds during anaerobic growth. Induced in the presence of fumarate. The expression of the enzyme is dependent on molybdenum. Trimeric enzyme localised to the cytoplasmic membrane, with two extrinsic subunits (dmsA and dmsB) and one membrane anchor (dmsC). Heterotrimer Accepted 2016-JAN-14 by BMELDAL