MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint tokumoto-2002-1 Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli. in vivo in vivo imaging technique imaging technique microscopy predetermined predetermined participant predetermined Tokumoto U., Nomura S., Minami Y., Mihara H., Kato S., Kurihara T., Esaki N., Kanazawa H., Matsubara H., Takahashi Y. J. Biochem. (0021-924X) 2002 tokumoto-2002-2 Network of protein-protein interactions among iron-sulfur cluster assembly proteins in Escherichia coli. in vivo in vivo 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Tokumoto U., Nomura S., Minami Y., Mihara H., Kato S., Kurihara T., Esaki N., Kanazawa H., Matsubara H., Takahashi Y. J. Biochem. (0021-924X) 2002 iscs_shifl Cysteine desulfurase IscS iscS SF2577 S2749 protein protein shifl Shigella flexneri MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIEWAHH mint Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine. Functions as a sulfur delivery protein for NAD, biotin and Fe-S cluster synthesis. Transfers sulfur on 'Cys-456' of thiI in a transpersulfidation reaction. Functions also as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate fer_eco57 2Fe-2S ferredoxin fdx ECs3391 Z3792 protein protein eco57 Escherichia coli O157:H7 MPKIVILPHQDLCPDGAVLEANSGETILDAALRNGIEIEHACEKSCACTTCHCIVREGFDSLPESSEQEDDMLDKAWGLEPESRLSCQARVTDEDLVVEIPRYTINHAREH mint Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins hsca_eco57 Chaperone protein HscA hscA ECs3392 Z3793 Hsc66 protein protein eco57 Escherichia coli O157:H7 MALLQISEPGLSAAPHQRRLAAGIDLGTTNSLVATVRSGQAETLADHEGRHLLPSVVHYQQQGHSVGYDARTNAALDTANTISSVKRLMGRSLADIQQRYPHLPYQFQASENGLPMIETAAGLLNPVRVSADILKALAARATEALAGELDGVVITVPAYFDDAQRQGTKDAARLAGLHVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSRGVFEVLATGGDSALGGDDFDHLLADYIREQAGIPDRSDNRVQRELLDAAIAAKIALSDADSVTVNVAGWQGEISREQFNELIAPLVKRTLLACRRALKDAGVEADEVLEVVMVGGSTRVPLVRERVGEFFGRPPLTSIDPDKVVAIGAAIQADILVGNKPDSEMLLLDVIPLSLGLETMGGLVEKVIPRNTTIPVARAQDFTTFKDGQTAMSIHVMQGERELVQDCRSLARFALRGIPALPAGGAHIRVTFQVDADGLLSVTAMEKSTGVEASIQVKPSYGLTDSEIASMIKDSMSYAEQDVKARMLAEQKVEAARVLESLHGALAADAALLSAAERQVIDDAAAHLSEVAQGDDVDAIEQAIKNVDKQTQDFAARRMDQSVRRALKGHSVDEV mint Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by hscB. Involved in the maturation of iscU hscb_eco57 Co-chaperone protein HscB hscB ECs3393 Z3794 Hsc20 protein protein eco57 Escherichia coli O157:H7 MDYFTLFGLPARYQLDTQALSLRFQDLQRQYHPDKFASGSQAEQLAAVQQSATINQAWQTLRHPLMRAEYLLSLHGFDLASEQHTVRDTAFLMEQLELREELDEIEQAKDEARLESFIKRVKKMFDTRHQLMVEQLDNETWDAAADTVRKLRFLDKLRSSAEQLEEKLLDF mint Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward hscA fdx-iscs 9856 iscs_shifl 9858 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed Stoichiometry: 1.0 fer_eco57 9859 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed Stoichiometry: 1.0 physical association physical association false false false mint fdx-hsca 9856 hsca_eco57 9860 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed Stoichiometry: 1.0 fer_eco57 9859 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed Stoichiometry: 1.0 physical association physical association false false false mint hsca-hscb 9857 hsca_eco57 9860 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role bait bait over-expressed over expressed level over-expressed tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 hscb_eco57 9861 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence unspecified role unspecified role prey prey over-expressed over expressed level over-expressed tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 1.0 physical association physical association false false false mint