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 Dissection and engineering of the Escherichia coli formate hydrogenlyase complex. Dissection and engineering of the Escherichia coli formate hydrogenlyase complex. FEBS letters 2015 imex curation McDowall JS., Hjersing MC., Palmer T., Sargent F. f.sargent@dundee.ac.uk 19-Jan-2016: Contacted by IntAct-Help. Only protein-protein interactions imex curation ecoli Escherichia coli (strain K12) affinity chrom affinity chromatography technology Affinity purification Affinity purification affinity chrom ms participant Identification by mass spectrometry ms participant McDowall JS., Hjersing MC., Palmer T., Sargent F. f.sargent@dundee.ac.uk Accepted 2015-DEC-21 AT 15:50 GMT AT 15:50 GMT by LUANA FEBS letters 2015 Only protein-protein interactions imex curation imex curation hycf_ecoli Formate hydrogenlyase subunit 6 hycF hevF b2720 JW2690 Hydrogenase-3 component F protein protein ecoli Escherichia coli (strain K12) MFTFIKKVIKTGTATSSYPLEPIAVDKNFRGKPEQNPQQCIGCAACVNACPSNALTVETDLATGELAWEFNLGHCIFCGRCEEVCPTAAIKLSQEYELAVWKKEDFLQQSRFALCNCRVCNRPFAVQKEIDYAIALLKHNGDSRAENHRESFETCPECKRQKCLVPSDRIELTRHMKEAI 284B8C507B47DFDC hycg_ecoli Formate hydrogenlyase subunit 7 Hydrogenase-3 component G hycG hevG b2719 JW2689 protein protein ecoli Escherichia coli (strain K12) MSNLLGPRDANGIPVPMTVDESIASMKASLLKKIKRSAYVYRVDCGGCNGCEIEIFATLSPLFDAERFGIKVVPSPRHADILLFTGAVTRAMRSPALRAWQSAPDPKICISYGACGNSGGIFHDLYCVWGGTDKIVPVDVYIPGCPPTPAATLYGFAMALGLLEQKIHARGPGELDEQPAEILHGDMVQPLRVKVDREARRLAGYRYGRQIADDYLTQLGQGEEQVARWLEAENDPRLNEIVSHLNHVVEEARIR DIP protein P16433 original sequence version: null B24FBAE3C44F3A10 hyce_ecoli Formate hydrogenlyase subunit 5 Hydrogenase-3 component E hycE hevE b2721 JW2691 protein protein ecoli Escherichia coli (strain K12) MSEEKLGQHYLAALNEAFPGVVLDHAWQTKDQLTVTVKVNYLPEVVEFLYYKQGGWLSVLFGNDERKLNGHYAVYYVLSMEKGTKCWITVRVEVDANKPEYPSVTPRVPAAVWGEREVRDMYGLIPVGLPDERRLVLPDDWPDELYPLRKDSMDYRQRPAPTTDAETYEFINELGDKKNNVVPIGPLHVTSDEPGHFRLFVDGENIIDADYRLFYVHRGMEKLAETRMGYNEVTFLSDRVCGICGFAHSTAYTTSVENAMGIQVPERAQMIRAILLEVERLHSHLLNLGLACHFTGFDSGFMQFFRVRETSMKMAEILTGARKTYGLNLIGGIRRDLLKDDMIQTRQLAQQMRREVQELVDVLLSTPNMEQRTVGIGRLDPEIARDFSNVGPMVRASGHARDTRADHPFVGYGLLPMEVHSEQGCDVISRLKVRINEVYTALNMIDYGLDNLPGGPLMVEGFTYIPHRFALGFAEAPRGDDIHWSMTGDNQKLYRWRCRAATYANWPTLRYMLRGNTVSDAPLIIGSLDPCYSCTDRMTVVDVRKKKSKVVPYKELERYSIERKNSPLK DIP protein P16431 original sequence version: null 38A2BCCB01B27463 hycb_ecoli Formate hydrogenlyase subunit 2 hycB hevB b2724 JW2694 Hydrogenase-3 component B protein protein ecoli Escherichia coli (strain K12) MNRFVIADSTLCIGCHTCEAACSETHRQHGLQSMPRLRVMLNEKESAPQLCHHCEDAPCAVVCPVNAITRVDGAVQLNESLCVSCKLCGIACPFGAIEFSGSRPLDIPANANTPKAPPAPPAPARVSTLLDWVPGIRAIAVKCDLCSFDEQGPACVRMCPTKALHLVDNTDIARVSKRKRELTFNTDFGDLTLFQQAQSGEAK 828042E504B00DBD 1-89 1 3 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed cell lysate cell lysate 2 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed cell lysate cell lysate 5 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed cell lysate cell lysate 4 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed cell lysate cell lysate his tag 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 association association f2 these experiments suggests that the most stable, minimal, core of the FHL complex comprises HycB, -E, -F,and -G, and that this 125kDa species may be formed in the absence of FdhF and/or HycC. these experiments suggests that the most stable, minimal, core of the FHL complex comprises HycB, -E, -F, and -G, and that this 125kDa species may be formed in the absence of FdhF and/or HycC.