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/ Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1. Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1. J. Biol. Chem. (0021-9258) 2005 Okada K., Hase T. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species sourceforge request for new CV interaction identification method : bacterial two hybrid using polymerase fusion. The BacterioMatch II two-hybrid was used. The bait fused to the DNA-binding domain of lambda cI is tethered to the lambda operator sequence upstream of the reporter promoter. The target is fused to the RNA polymerase. When the bait and target interact, they recruit and stabilize the binding of RNA polymerase at the promoter and activate the transcription. fig 4,5 okadak@protein.osaka-u.ac.jp in vitro In vitro pull down pull down predetermined predetermined participant predetermined Okada K., Hase T. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species sourceforge request for new CV interaction identification method : bacterial two hybrid using polymerase fusion. The BacterioMatch II two-hybrid was used. The bait fused to the DNA-binding domain of lambda cI is tethered to the lambda operator sequence upstream of the reporter promoter. The target is fused to the RNA polymerase. When the bait and target interact, they recruit and stabilize the binding of RNA polymerase at the promoter and activate the transcription. fig 4,5 okadak@protein.osaka-u.ac.jp Annotation to indicate that this entry has been checked and accepted by a senior curator. J. Biol. Chem. (0021-9258) 2005 Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1. Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1. J. Biol. Chem. (0021-9258) 2005 Okada K., Hase T. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species sourceforge request for new CV interaction identification method : bacterial two hybrid using polymerase fusion. The BacterioMatch II two-hybrid was used. The bait fused to the DNA-binding domain of lambda cI is tethered to the lambda operator sequence upstream of the reporter promoter. The target is fused to the RNA polymerase. When the bait and target interact, they recruit and stabilize the binding of RNA polymerase at the promoter and activate the transcription. fig 4,5 okadak@protein.osaka-u.ac.jp in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Okada K., Hase T. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species sourceforge request for new CV interaction identification method : bacterial two hybrid using polymerase fusion. The BacterioMatch II two-hybrid was used. The bait fused to the DNA-binding domain of lambda cI is tethered to the lambda operator sequence upstream of the reporter promoter. The target is fused to the RNA polymerase. When the bait and target interact, they recruit and stabilize the binding of RNA polymerase at the promoter and activate the transcription. fig 4,5 okadak@protein.osaka-u.ac.jp Annotation to indicate that this entry has been checked and accepted by a senior curator. J. Biol. Chem. (0021-9258) 2005 Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1. Cyanobacterial non-mevalonate pathway: (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase interacts with ferredoxin in Thermosynechococcus elongatus BP-1. J. Biol. Chem. (0021-9258) 2005 Okada K., Hase T. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species sourceforge request for new CV interaction identification method : bacterial two hybrid using polymerase fusion. The BacterioMatch II two-hybrid was used. The bait fused to the DNA-binding domain of lambda cI is tethered to the lambda operator sequence upstream of the reporter promoter. The target is fused to the RNA polymerase. When the bait and target interact, they recruit and stabilize the binding of RNA polymerase at the promoter and activate the transcription. fig 4,5 okadak@protein.osaka-u.ac.jp ecoli Escherichia coli (strain K12) transcription compl transcriptional complementation assay transcription compl predetermined predetermined participant predetermined Okada K., Hase T. Cyanobacteria - Interaction dataset based on Cyanobacteria proteins and related species sourceforge request for new CV interaction identification method : bacterial two hybrid using polymerase fusion. The BacterioMatch II two-hybrid was used. The bait fused to the DNA-binding domain of lambda cI is tethered to the lambda operator sequence upstream of the reporter promoter. The target is fused to the RNA polymerase. When the bait and target interact, they recruit and stabilize the binding of RNA polymerase at the promoter and activate the transcription. fig 4,5 okadak@protein.osaka-u.ac.jp Annotation to indicate that this entry has been checked and accepted by a senior curator. J. Biol. Chem. (0021-9258) 2005 ispg_theeb 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ferredoxin) 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase ispG tlr0996 protein protein theeb Thermosynechococcus elongatus (strain BP-1) MQTLPSPVQATPTETAIVRRKTRPVPIGSVVIGGGHPVAVQSMINEDTLDIEGSVAAIRRLHEIGCEIVRVTVPSLAHAKAMEEIRDRLYKTYKPVPLVADVHHNGMKIALEVAKYVDNVRINPGLYVFEKPKPNRTEYTQAEFDEIGAKIRETLEPLVISLRDQGKSMRIGVNHGSLAERMLFTYGDTPEGMVESALEFIRICESLNFYNLEISLKASRVPVMIAANRLMVKRMDELGMDYPLHLGVTEAGDGEYGRIKSTAGIATLLAEGIGDTIRVSLTEAPEKEIPVCYGILQALGLRRTMVEYVACPSCGRTLFNLEEVLHKVREATKHLTGLNIAVMGCIVNGPGEMADADYGYVGKQPGYISLYRGREEVKKVPEAEGVAALVELIKADGRWVDP 7595FFC940AC60D7 fer_theeb Ferredoxin-1 Ferredoxin I petF1 petF tsl1009 protein protein theeb Thermosynechococcus elongatus (strain BP-1) MATYKVTLVRPDGSETTIDVPEDEYILDVAEEQGLDLPFSCRAGACSTCAGKLLEGEVDQSDQSFLDDDQIEKGFVLTCVAYPRSDCKILTNQEEELY DE8198FFB127C7AF petf-gcpe-1 3 5 unspecified role unspecified role bait bait 4 unspecified role unspecified role prey prey physical association physical association petf-gcpe-2 1 5 unspecified role unspecified role bait bait ecoli Escherichia coli (strain K12) 4 unspecified role unspecified role prey prey n-terminal 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 ecoli Escherichia coli (strain K12) direct interaction direct interaction petf-gcpe-3 2 4 electron acceptor electron acceptor unspecified role unspecified role n-terminal 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 ecoli Escherichia coli (strain K12) 5 electron donor electron donor unspecified role unspecified role region gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction NADH and PetH are required for the reduction