UniProt UniProt http://www.uniprot.org Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme. Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme. Biochemistry 2008 imex curation Mitra A., Sarma SP. 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro enzymatic study enzymatic study predetermined predetermined participant predetermined Mitra A., Sarma SP. The conversion of pyruvate to acetate and acetolactate was monitored by NMR. Accepted 2018-JUL-10 AT 14:20 BST AT 14:20 BST by LIVIAP Biochemistry 2008 Only protein-protein interactions imex curation imex curation Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme. Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme. Biochemistry 2008 imex curation Mitra A., Sarma SP. 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro cd circular dichroism CD CD cd predetermined predetermined participant predetermined Mitra A., Sarma SP. Accepted 2018-JUL-10 AT 14:20 BST AT 14:20 BST by LIVIAP Biochemistry 2008 Only protein-protein interactions imex curation imex curation Mock publication and experiment for abstract interactions that are not interaction evidences. Mock publication and experiment for abstract interactions that are not interaction evidences. unspecified method Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme. Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme. Biochemistry 2008 imex curation Mitra A., Sarma SP. 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Mitra A., Sarma SP. Accepted 2018-JUL-10 AT 14:20 BST AT 14:20 BST by LIVIAP Biochemistry 2008 Only protein-protein interactions imex curation imex curation fad FAD - Flavin adenine dinucleotide Adenosine 5'-(trihydrogen pyrophosphate), 5'-5'-ester with riboflavine adenosine 5'-[3-(riboflavin-5'-yl) dihydrogen diphosphate] FAD Flavin adenine dinucleotide FLAVIN-ADENINE DINUCLEOTIDE Riboflavin 5'-(trihydrogen diphosphate), 5'-5'-ester with adenosine Riboflavin 5'-adenosine diphosphate adenosine 5'-(3-{D-ribo-5-[7,8-dimethyl-2,4-dioxo-3,4-dihydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl} dihydrogen diphosphate) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) Flavin adenine dinucleotide Flavin adenine dinucleotide ilvn_ecoli Acetolactate synthase isozyme 1 small subunit Acetohydroxy-acid synthase I small subunit ilvN b3670 JW3645 protein protein ecoli Escherichia coli (strain K12) MQNTTHDNVILELTVRNHPGVMTHVCGLFARRAFNVEGILCLPIQDSDKSHIWLLVNDDQRLEQMISQIDKLEDVVKVQRNQSDPTMFNKIAVFFQ 7F37DD421EDD3802 magnesium(2+) Magnesium(2+) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) fad(3-) FAD(3-) FAD FAD trianion small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) IMGVNJNCCGXBHD-UYBVJOGSSA-K IMGVNJNCCGXBHD-UYBVJOGSSA-K ilvb_ecoli Acetolactate synthase isozyme 1 large subunit Acetohydroxy-acid synthase I large subunit ilvB b3671 JW3646 protein protein ecoli Escherichia coli (strain K12) MASSGTTSTRKRFTGAEFIVHFLEQQGIKIVTGIPGGSILPVYDALSQSTQIRHILARHEQGAGFIAQGMARTDGKPAVCMACSGPGATNLVTAIADARLDSIPLICITGQVPASMIGTDAFQEVDTYGISIPITKHNYLVRHIEELPQVMSDAFRIAQSGRPGPVWIDIPKDVQTAVFEIETQPAMAEKAAAPAFSEESIRDAAAMINAAKRPVLYLGGGVINAPARVRELAEKAQLPTTMTLMALGMLPKAHPLSLGMLGMHGVRSTNYILQEADLLIVLGARFDDRAIGKTEQFCPNAKIIHVDIDRAELGKIKQPHVAIQADVDDVLAQLIPLVEAQPRAEWHQLVADLQREFPCPIPKACDPLSHYGLINAVAACVDDNAIITTDVGQHQMWTAQAYPLNRPRQWLTSGGLGTMGFGLPAAIGAALANPDRKVLCFSGDGSLMMNIQEMATASENQLDVKIILMNNEALGLVHQQQSLFYEQGVFAATYPGKINFMQIAAGFGLETCDLNNEADPQASLQEIINRPGPALIHVRIDAEEKVYPMVPPGAANTEMVGE DIP protein P08142 original sequence version: null 70F8A3128031353C thiamine(1+) diphosphate(3-) thiamine(1+) diphosphate(3-) thiamine diphosphate thiamine diphosphate dianion thiamine diphosphate(2-) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) AYEKOFBPNLCAJY-UHFFFAOYSA-L AYEKOFBPNLCAJY-UHFFFAOYSA-L pyruvate pyruvate small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) ilvb-ilvn-1 2 6 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) 9 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Changes in CD spectra indicate that ilvN interacts with ilvBα and ilvBβ domains of the catalytic subunit and not with the ilvBγ domain. Fig. 7 ilvb-ilvn-2 4 6 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) 9 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region 15n label 15n label 15N N15 15N N15 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction NMR chemical shift mapping methods show that ilvN binds close to the FAD binding site in ilvBβ and proximal to the intrasubunit ilvBα/ilvBβ domain interface. Fig. 8 fad-ilvb-1 4 5 unspecified role unspecified role neutral component neutral component 9 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain region 15n label 15n label 15N N15 15N N15 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) direct interaction direct interaction NMR chemical shift mapping methods show that ilvN binds close to the FAD binding site in ilvBβ and proximal to the intrasubunit ilvBα/ilvBβ domain interface. Fig. 5 ilvbn_ecoli-pyruvate-1 1 11 enzyme target enzyme target substrate substrate unspecified role unspecified role 31 enzyme enzyme unspecified role unspecified role purified purified ecoli Escherichia coli (strain K12) enzymatic reaction enzymatic reaction Biochemical reaction Biochemical reaction Fig. 6 ilvbn_ecoli IlvBN complex AHAS I complex Acetolactate synthase I complex 2xilvb:2xilvN Acetohydroxyacid synthase I complex 7 cofactor cofactor coenzyme ilvb binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 10 cofactor cofactor coenzyme ilvb binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 8 cofactor cofactor coenzyme ilvb binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 6 enzyme enzyme ilvb binding region binding region binding-associated region binding region undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 9 enzyme enzyme fad binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ilvn binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain thiamine diphosphate binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain magnesium binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain 44 33 35 43 37 41 39 42 direct interaction direct interaction ecoli Escherichia coli (strain K12) stable complex stable complex physical interaction evidence used in manual assertion physical interaction evidence used in manual assertion IPI inferred from physical interaction Catalyzes the first step that is common to the biosynthesis of branched-chain amino acids. The reaction involves the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate as the first step in the biosynthesis of valine and leucine. or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate as the initial step in the biosynthesis of isoleucine. The AHAS I and AHAS III (CPX-3575) complexes are both sensitive to feedback inhibition by valine, whereas the AHAS II complex (CPX-3570) is not, enabling bacteria expressing this complex to grow in valine-rich conditions. FAD appears to be required to maintain the geometry of the active sites in the central beta‐domain of the ilvB molecule. Heterotetramer Accepted 2018-JUL-16 by LIVIAP