DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Heme biosynthesis is coupled to electron transport chains for energy generation. Heme biosynthesis is coupled to electron transport chains for energy generation. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Möbius K., Arias-Cartin R., Breckau D., Hännig AL., Riedmann K., Biedendieck R., Schröder S., Becher D., Magalon A., Moser J., Jahn M., Jahn D. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Möbius K., Arias-Cartin R., Breckau D., Hännig AL., Riedmann K., Biedendieck R., Schröder S., Becher D., Magalon A., Moser J., Jahn M., Jahn D. DIP original experiment: DIP-219808X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Heme biosynthesis is coupled to electron transport chains for energy generation. Heme biosynthesis is coupled to electron transport chains for energy generation. Heme biosynthesis is coupled to electron transport chains for energy generation. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Möbius K., Arias-Cartin R., Breckau D., Hännig AL., Riedmann K., Biedendieck R., Schröder S., Becher D., Magalon A., Moser J., Jahn M., Jahn D. Only protein-protein interactions ecolx Escherichia coli ion exchange chrom ion exchange chromatography IEC IEC ion exchange chrom de novo protein sequence de novo protein sequencing by mass spectrometry de novo protein sequence Möbius K., Arias-Cartin R., Breckau D., Hännig AL., Riedmann K., Biedendieck R., Schröder S., Becher D., Magalon A., Moser J., Jahn M., Jahn D. DIP original experiment: DIP-219809X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Heme biosynthesis is coupled to electron transport chains for energy generation. Heme biosynthesis is coupled to electron transport chains for energy generation. Heme biosynthesis is coupled to electron transport chains for energy generation. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Möbius K., Arias-Cartin R., Breckau D., Hännig AL., Riedmann K., Biedendieck R., Schröder S., Becher D., Magalon A., Moser J., Jahn M., Jahn D. Only protein-protein interactions ecolx Escherichia coli pull down pull down de novo protein sequence de novo protein sequencing by mass spectrometry de novo protein sequence Möbius K., Arias-Cartin R., Breckau D., Hännig AL., Riedmann K., Biedendieck R., Schröder S., Becher D., Magalon A., Moser J., Jahn M., Jahn D. DIP original experiment: DIP-219810X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Heme biosynthesis is coupled to electron transport chains for energy generation. frda_ecoli Fumarate reductase flavoprotein subunit frdA Quinol-fumarate reductase flavoprotein subunit JW4115 b4154 protein protein ecoli Escherichia coli (strain K12) MQTFQADLAIVGAGGAGLRAAIAAAQANPNAKIALISKVYPMRSHTVAAEGGSAAVAQDHDSFEYHFHDTVAGGDWLCEQDVVDYFVHHCPTEMTQLELWGCPWSRRPDGSVNVRRFGGMKIERTWFAADKTGFHMLHTLFQTSLQFPQIQRFDEHFVLDILVDDGHVRGLVAMNMMEGTLVQIRANAVVMATGGAGRVYRYNTNGGIVTGDGMGMALSHGVPLRDMEFVQYHPTGLPGSGILMTEGCRGEGGILVNKNGYRYLQDYGMGPETPLGEPKNKYMELGPRDKVSQAFWHEWRKGNTISTPRGDVVYLDLRHLGEKKLHERLPFICELAKAYVGVDPVKEPIPVRPTAHYTMGGIETDQNCETRIKGLFAVGECSSVGLHGANRLGSNSLAELVVFGRLAGEQATERAATAGNGNEAAIEAQAAGVEQRLKDLVNQDGGENWAKIRDEMGLAMEEGCGIYRTPELMQKTIDKLAELQERFKRVRITDTSSVFNTDLLYTIELGHGLNVAECMAHSAMARKESRGAHQRLDEGCTERDDVNFLKHTLAFRDADGTTRLEYSDVKITTLPPAKRVYGGEADAADKAEAANKKEKANG DIP protein P00363 original sequence version: 131 DIP protein P00363 original sequence version: null 3306D7FF6E198AE9 hemg_ecoli Protoporphyrinogen IX dehydrogenase [quinone] Protoporphyrinogen IX dehydrogenase [menaquinone] Protoporphyrinogen IX dehydrogenase [ubiquinone] Protoporphyrinogen oxidase yihB hemG b3850 JW3827 protein protein ecoli Escherichia coli (strain K12) MKTLILFSTRDGQTREIASYLASELKELGIQADVANVHRIEEPQWENYDRVVIGASIRYGHYHSAFQEFVKKHATRLNSMPSAFYSVNLVARKPEKRTPQTNSYARKFLMNSQWRPDRCAVIAGALRYPRYRWYDRFMIKLIMKMSGGETDTRKEVVYTDWEQVANFAREIAHLTDKPTLK DIP protein P0ACB4 original sequence version: 54 BCCB5AE594010026 hemg-1 1 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction frda-hemg-1 2 4 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association hemg-frda-1 3 4 unspecified role unspecified role prey prey ecolx Escherichia coli 5 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association