#ID(s) interactor A	ID(s) interactor B	Alt. ID(s) interactor A	Alt. ID(s) interactor B	Alias(es) interactor A	Alias(es) interactor B	Interaction detection method(s)	Publication 1st author(s)	Publication Identifier(s)	Taxid interactor A	Taxid interactor B	Interaction type(s)	Source database(s)	Interaction identifier(s)	Confidence value(s)	Expansion method(s)	Biological role(s) interactor A	Biological role(s) interactor B	Experimental role(s) interactor A	Experimental role(s) interactor B	Type(s) interactor A	Type(s) interactor B	Xref(s) interactor A	Xref(s) interactor B	Interaction Xref(s)	Annotation(s) interactor A	Annotation(s) interactor B	Interaction annotation(s)	Host organism(s)	Interaction parameter(s)	Creation date	Update date	Checksum(s) interactor A	Checksum(s) interactor B	Interaction Checksum(s)	Negative	Feature(s) interactor A	Feature(s) interactor B	Stoichiometry(s) interactor A	Stoichiometry(s) interactor B	Identification method participant A	Identification method participant B
uniprotkb:P0ADF8	uniprotkb:P08142	intact:EBI-1133508|uniprotkb:P08143|uniprotkb:Q2M7Y3|ensemblbacteria:AAC76693|ensemblbacteria:BAE77623	intact:EBI-552948|uniprotkb:Q2M7Y4|ensemblbacteria:AAC76694|ensemblbacteria:BAE77622	psi-mi:ilvn_ecoli(display_long)|uniprotkb:Acetohydroxy-acid synthase I small subunit(gene name synonym)|uniprotkb:ilvN(gene name)|psi-mi:ilvN(display_short)|uniprotkb:b3670(locus name)|uniprotkb:JW3645(locus name)	psi-mi:ilvb_ecoli(display_long)|uniprotkb:Acetohydroxy-acid synthase I large subunit(gene name synonym)|uniprotkb:ilvB(gene name)|psi-mi:ilvB(display_short)|uniprotkb:b3671(locus name)|uniprotkb:JW3646(locus name)	psi-mi:"MI:0016"(circular dichroism)	Mitra et al. (2008)	pubmed:18193896|imex:IM-26465	taxid:83333(ecoli)|taxid:83333("Escherichia coli (strain K12)")	taxid:83333(ecoli)|taxid:83333("Escherichia coli (strain K12)")	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0486"(UniProt)	intact:EBI-20591346|imex:IM-26465-1	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_418126.1|interpro:IPR002912(Amino acid-binding ACT)|interpro:IPR039557|rcsb pdb:5YPP|rcsb pdb:5YPY|rcsb pdb:5YUM|refseq:WP_001181706.1|ensemblbacteria:AAC76693(transcript)|ensemblbacteria:b3670(gene)|ensemblbacteria:BAE77623(gene)|ensemblbacteria:BAE77623(transcript)|go:"GO:0003984"(acetolactate synthase activity)|go:"GO:0005948"(acetolactate synthase complex)|go:"GO:0009097"(isoleucine biosynthetic process)|go:"GO:0009099"(valine biosynthetic process)|go:"GO:1990610"(acetolactate synthase regulator activity)|rcsb pdb:6LPI|rcsb pdb:2LVW|interpro:IPR004789(Acetolactate synthase, small subunit)	refseq:NP_418127.1|refseq:WP_000168475.1|dip:DIP-10019N|ensemblbacteria:AAC76694(transcript)|ensemblbacteria:b3671(gene)|ensemblbacteria:BAE77622(gene)|ensemblbacteria:BAE77622(transcript)|go:"GO:0000287"(magnesium ion binding)|go:"GO:0003984"(acetolactate synthase activity)|go:"GO:0005948"(acetolactate synthase complex)|go:"GO:0009097"(isoleucine biosynthetic process)|go:"GO:0009099"(valine biosynthetic process)|go:"GO:0050660"(flavin adenine dinucleotide binding)|interpro:IPR000399(TPP-binding enzymes, conserved site)|interpro:IPR011766(Thiamine pyrophosphate enzyme, C-terminal TPP-binding)|interpro:IPR012000(Thiamine pyrophosphate enzyme, central region)|interpro:IPR012001(Thiamine pyrophosphate enzyme, N-terminal TPP binding region)|interpro:IPR012846(Acetolactate synthase, large subunit, biosynthetic)|interpro:IPR029035|interpro:IPR029061|interpro:IPR039368|rcsb pdb:6LPI|go:"GO:0030976"(thiamine pyrophosphate binding)	-	-	-	figure legend:Fig. 7|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2018/06/13	2018/06/15	rogid:pE06BSx/JIVmWxreeOcXVrxHvRA83333	rogid:qrMPzs9Nt9/AAwiQ4PYGCUN4Uh883333	rigid:KR3r4fR6A6VHkr8aNw6Ex9sWNZ0	false	-	sufficient binding region:1-186(IPR029061)|sufficient binding region:187-359(IPR012000)	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
uniprotkb:P0ADF8	uniprotkb:P08142	intact:EBI-1133508|uniprotkb:P08143|uniprotkb:Q2M7Y3|ensemblbacteria:AAC76693|ensemblbacteria:BAE77623	intact:EBI-552948|uniprotkb:Q2M7Y4|ensemblbacteria:AAC76694|ensemblbacteria:BAE77622	psi-mi:ilvn_ecoli(display_long)|uniprotkb:Acetohydroxy-acid synthase I small subunit(gene name synonym)|uniprotkb:ilvN(gene name)|psi-mi:ilvN(display_short)|uniprotkb:b3670(locus name)|uniprotkb:JW3645(locus name)	psi-mi:ilvb_ecoli(display_long)|uniprotkb:Acetohydroxy-acid synthase I large subunit(gene name synonym)|uniprotkb:ilvB(gene name)|psi-mi:ilvB(display_short)|uniprotkb:b3671(locus name)|uniprotkb:JW3646(locus name)	psi-mi:"MI:0077"(nuclear magnetic resonance)	Mitra et al. (2008)	pubmed:18193896|imex:IM-26465	taxid:83333(ecoli)|taxid:83333("Escherichia coli (strain K12)")	taxid:83333(ecoli)|taxid:83333("Escherichia coli (strain K12)")	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0486"(UniProt)	intact:EBI-20591406|imex:IM-26465-3	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_418126.1|interpro:IPR002912(Amino acid-binding ACT)|interpro:IPR039557|rcsb pdb:5YPP|rcsb pdb:5YPY|rcsb pdb:5YUM|refseq:WP_001181706.1|ensemblbacteria:AAC76693(transcript)|ensemblbacteria:b3670(gene)|ensemblbacteria:BAE77623(gene)|ensemblbacteria:BAE77623(transcript)|go:"GO:0003984"(acetolactate synthase activity)|go:"GO:0005948"(acetolactate synthase complex)|go:"GO:0009097"(isoleucine biosynthetic process)|go:"GO:0009099"(valine biosynthetic process)|go:"GO:1990610"(acetolactate synthase regulator activity)|rcsb pdb:6LPI|rcsb pdb:2LVW|interpro:IPR004789(Acetolactate synthase, small subunit)	refseq:NP_418127.1|refseq:WP_000168475.1|dip:DIP-10019N|ensemblbacteria:AAC76694(transcript)|ensemblbacteria:b3671(gene)|ensemblbacteria:BAE77622(gene)|ensemblbacteria:BAE77622(transcript)|go:"GO:0000287"(magnesium ion binding)|go:"GO:0003984"(acetolactate synthase activity)|go:"GO:0005948"(acetolactate synthase complex)|go:"GO:0009097"(isoleucine biosynthetic process)|go:"GO:0009099"(valine biosynthetic process)|go:"GO:0050660"(flavin adenine dinucleotide binding)|interpro:IPR000399(TPP-binding enzymes, conserved site)|interpro:IPR011766(Thiamine pyrophosphate enzyme, C-terminal TPP-binding)|interpro:IPR012000(Thiamine pyrophosphate enzyme, central region)|interpro:IPR012001(Thiamine pyrophosphate enzyme, N-terminal TPP binding region)|interpro:IPR012846(Acetolactate synthase, large subunit, biosynthetic)|interpro:IPR029035|interpro:IPR029061|interpro:IPR039368|rcsb pdb:6LPI|go:"GO:0030976"(thiamine pyrophosphate binding)	-	-	-	figure legend:Fig. 8|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2018/06/13	2018/06/15	rogid:pE06BSx/JIVmWxreeOcXVrxHvRA83333	rogid:qrMPzs9Nt9/AAwiQ4PYGCUN4Uh883333	rigid:KR3r4fR6A6VHkr8aNw6Ex9sWNZ0	false	-	sufficient binding region:1-186(IPR029061)|sufficient binding region:187-359(IPR012000)|15n label:?-?	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
chebi:"CHEBI:16238"	uniprotkb:P08142	intact:EBI-1225105|chebi:"CHEBI:42388"|chebi:"CHEBI:4956"|chebi:"CHEBI:13315"|chebi:"CHEBI:21125"	intact:EBI-552948|uniprotkb:Q2M7Y4|ensemblbacteria:AAC76694|ensemblbacteria:BAE77622	psi-mi:fad(display_short)|psi-mi:"CHEBI:16238"(display_long)|intact:"Adenosine 5'-(trihydrogen pyrophosphate), 5'-5'-ester with riboflavine"(synonym)|intact:"adenosine 5'-[3-(riboflavin-5'-yl) dihydrogen diphosphate]"(synonym)|intact:FAD(synonym)|intact:Flavin adenine dinucleotide(synonym)|intact:FLAVIN-ADENINE DINUCLEOTIDE(synonym)|intact:"Riboflavin 5'-(trihydrogen diphosphate), 5'-5'-ester with adenosine"(synonym)|intact:Riboflavin 5'-adenosine diphosphate(synonym)|intact:"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)"(iupac name)	psi-mi:ilvb_ecoli(display_long)|uniprotkb:Acetohydroxy-acid synthase I large subunit(gene name synonym)|uniprotkb:ilvB(gene name)|psi-mi:ilvB(display_short)|uniprotkb:b3671(locus name)|uniprotkb:JW3646(locus name)	psi-mi:"MI:0077"(nuclear magnetic resonance)	Mitra et al. (2008)	pubmed:18193896|imex:IM-26465	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:83333(ecoli)|taxid:83333("Escherichia coli (strain K12)")	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0486"(UniProt)	intact:EBI-20591420|imex:IM-26465-4	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0497"(neutral component)	psi-mi:"MI:0328"(small molecule)	psi-mi:"MI:0326"(protein)	-	refseq:NP_418127.1|refseq:WP_000168475.1|dip:DIP-10019N|ensemblbacteria:AAC76694(transcript)|ensemblbacteria:b3671(gene)|ensemblbacteria:BAE77622(gene)|ensemblbacteria:BAE77622(transcript)|go:"GO:0000287"(magnesium ion binding)|go:"GO:0003984"(acetolactate synthase activity)|go:"GO:0005948"(acetolactate synthase complex)|go:"GO:0009097"(isoleucine biosynthetic process)|go:"GO:0009099"(valine biosynthetic process)|go:"GO:0050660"(flavin adenine dinucleotide binding)|interpro:IPR000399(TPP-binding enzymes, conserved site)|interpro:IPR011766(Thiamine pyrophosphate enzyme, C-terminal TPP-binding)|interpro:IPR012000(Thiamine pyrophosphate enzyme, central region)|interpro:IPR012001(Thiamine pyrophosphate enzyme, N-terminal TPP binding region)|interpro:IPR012846(Acetolactate synthase, large subunit, biosynthetic)|interpro:IPR029035|interpro:IPR029061|interpro:IPR039368|rcsb pdb:6LPI|go:"GO:0030976"(thiamine pyrophosphate binding)	-	comment:Flavin adenine dinucleotide	-	figure legend:Fig. 5|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2018/06/13	2018/07/10	-	rogid:qrMPzs9Nt9/AAwiQ4PYGCUN4Uh883333	-	false	-	sufficient binding region:187-359(IPR012000)|15n label:?-?	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)
chebi:"CHEBI:15361"	intenz:2.2.1.6	intact:EBI-6621808	intact:EBI-20591435	psi-mi:pyruvate(display_short)|psi-mi:"CHEBI:15361"(display_long)	psi-mi:ilvbn_ecoli(display_short)|psi-mi:2.2.1.6(display_long)|intact:IlvBN complex(complex synonym)|intact:AHAS I complex(complex synonym)|intact:Acetolactate synthase I complex(complex recommended name)|intact:"2xilvb:2xilvN"(complex systematic name)|intact:Acetohydroxyacid synthase I complex(complex synonym)	psi-mi:"MI:0415"(enzymatic study)	Mitra et al. (2008)	pubmed:18193896|imex:IM-26465	taxid:-2(chemical synthesis)|taxid:-2("Chemical synthesis (Chemical synthesis)")	taxid:83333(ecoli)|taxid:83333("Escherichia coli (strain K12)")	psi-mi:"MI:0414"(enzymatic reaction)	psi-mi:"MI:0486"(UniProt)	intact:EBI-20591524|imex:IM-26465-6	-	-	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0328"(small molecule)	psi-mi:"MI:1302"(stable complex)	-	evidence ontology:"ECO:0000353"|intact:EBI-20591346(exp-evidence)|complex portal:CPX-3573(complex-primary)|go:"GO:0003984"(acetolactate synthase activity)|go:"GO:0009082"(branched-chain amino acid biosynthetic process)|go:"GO:0005948"(acetolactate synthase complex)	-	-	curated-complex:"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."|complex-properties:FAD appears to be required to maintain the geometry of the active sites in the central beta‐domain of the ilvB molecule.|complex-assembly:Heterotetramer	figure legend:Fig. 6|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2018/06/13	2018/06/15	-	-	-	false	-	-	-	-	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)