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/ The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat. Struct. Biol. (1072-8368) 2000 imex curation Abramson J., Riistama S., Larsson G., Jasaitis A., Svensson-Ek M., Laakkonen L., Puustinen A., Iwata S., Wikström M. Marten.Wikstrom@Helsinki.Fi,iwata@xray.bmc.uu.se 30-Sept-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro oxidoreduct assay oxidoreductase assay oxidoreduct assay predetermined predetermined participant predetermined Abramson J., Riistama S., Larsson G., Jasaitis A., Svensson-Ek M., Laakkonen L., Puustinen A., Iwata S., Wikström M. "...the enzyme [was] reconstituted in proteoliposomes." (see Text) "Translocation of electrical charge during the reaction was determined by time resolved electrometry" (see Legend of Fig. 8). Ubiquinol oxidase activity was measured at 25 °C using a Clark-type oxygen electrode. Ubiquinone content and steady state reduction level of heme b were measured spectrophotometrically (Table 2). Marten.Wikstrom@Helsinki.Fi,iwata@xray.bmc.uu.se Accepted 2013-SEP-25 by MGT 30-Sept-2013: Contacted by IntAct-Help. Nat. Struct. Biol. (1072-8368) 2000 Only protein-protein interactions imex curation The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat. Struct. Biol. (1072-8368) 2000 imex curation Abramson J., Riistama S., Larsson G., Jasaitis A., Svensson-Ek M., Laakkonen L., Puustinen A., Iwata S., Wikström M. Marten.Wikstrom@Helsinki.Fi,iwata@xray.bmc.uu.se 30-Sept-2013: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Abramson J., Riistama S., Larsson G., Jasaitis A., Svensson-Ek M., Laakkonen L., Puustinen A., Iwata S., Wikström M. Marten.Wikstrom@Helsinki.Fi,iwata@xray.bmc.uu.se Accepted 2013-SEP-25 by MGT 30-Sept-2013: Contacted by IntAct-Help. Nat. Struct. Biol. (1072-8368) 2000 Only protein-protein interactions imex curation cyoa_ecoli Cytochrome bo(3) ubiquinol oxidase subunit 2 Ubiquinol oxidase polypeptide II Cytochrome o ubiquinol oxidase subunit 2 cyoA Cytochrome b562-o complex subunit II Oxidase bo(3) subunit 2 Ubiquinol oxidase chain B Ubiquinol oxidase subunit 2 JW0422 b0432 protein protein ecoli Escherichia coli (strain K12) MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAAFDQWVAKAKQSPNTMSDMAAFEKLAAPSEYNQVEYFSNVKPDLFADVINKFMAHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH 62EC951183B65724 cyod_ecoli Cytochrome bo(3) ubiquinol oxidase subunit 4 Cytochrome o ubiquinol oxidase subunit 4 Oxidase bo(3) subunit 4 Ubiquinol oxidase chain D Ubiquinol oxidase polypeptide IV Ubiquinol oxidase subunit 4 JW0419 b0429 cyoD protein protein ecoli Escherichia coli (strain K12) MSHSTDHSGASHGSVKTYMTGFILSIILTVIPFWMVMTGAASPAVILGTILAMAVVQVLVHLVCFLHMNTKSDEGWNMTAFVFTVLIIAILVVGSIWIMWNLNYNMMMH E2DBE23C893724BA ubiquinol ubiquinol a ubiquinol coenzymes QH2 CoQH2 QH(2) QH2 reduced ubiquinone Ubiquinol ubiquinols small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) TVLSKGDBUQMDPR-UHFFFAOYSA-N TVLSKGDBUQMDPR-UHFFFAOYSA-N cyoc_ecoli Cytochrome bo(3) ubiquinol oxidase subunit 3 Cytochrome o ubiquinol oxidase subunit 3 Oxidase bo(3) subunit 3 Ubiquinol oxidase polypeptide III Ubiquinol oxidase subunit 3 JW0420 b0430 cyoC Ubiquinol oxidase chain C protein protein ecoli Escherichia coli (strain K12) MATDTLTHATAHAHEHGHHDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM F1D6ABF9EB6CB5AD heme b Heme b small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) cyob_ecoli Cytochrome bo(3) ubiquinol oxidase subunit 1 cyoB Ubiquinol oxidase polypeptide I Cytochrome o ubiquinol oxidase subunit 1 Ubiquinol oxidase chain A Cytochrome b562-o complex subunit I Oxidase bo(3) subunit 1 Ubiquinol oxidase subunit 1 JW0421 b0431 protein protein ecoli Escherichia coli (strain K12) MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQFHTMLMIAASGAVLIALGILCLVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN 17357B8D44C7CF84 cyoa-cyob-1 2 8 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) 3 unspecified role unspecified role neutral component neutral component c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role neutral component neutral component ecoli Escherichia coli (strain K12) physical association physical association Fig.s 2, 3, Table 1. 3.5 A cyoa-cyob-3 1 4 ancillary ancillary neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 6 ancillary ancillary neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 8 enzyme enzyme neutral component neutral component P0ABI8:p.Arg71Leu mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain R L Wed May 02 17:47:19 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg71leu' Tue Jun 30 20:19:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg71Leu' P0ABI8:p.Arg71Gln mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain R Q Wed May 02 16:10:12 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg71gln' Tue Jun 30 17:13:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg71Gln' P0ABI8:p.Asp75Asn mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain D N Wed May 02 16:12:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp75asn' Tue Jun 30 15:59:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp75Asn' P0ABI8:p.His98Asn mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate certain certain sequence position certain certain certain sequence position certain H N Wed May 02 19:59:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his98asn' Tue Jun 30 17:26:28 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His98Asn' region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P0ABI8:p.Gln101Asn mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain Q N Wed May 02 19:18:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln101asn' Tue Jun 30 18:33:57 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln101Asn' ecoli Escherichia coli (strain K12) 7 ancillary ancillary unspecified role unspecified role 3 ancillary ancillary neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 5 enzyme target enzyme target substrate substrate neutral component neutral component redox reaction oxidoreductase activity electron transfer reaction redox reaction Fig. 8, Table 2. The reaction with the WT construct was measured in two buffers: Triton-X100 with a kM of 45 uM and DM with a kM of 18 uM.