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ilvA ilvA ilvD ilvD ilvE ilvE ADO50501.1 ADO50501.1 ADO50502.1 ADO50502.1
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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textmining
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Your Input:
ilvAThreonine dehydratase, biosynthetic; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. (514 aa)
ilvDTIGRFAM: dihydroxy-acid dehydratase; KEGG: sbc:SbBS512_E4149 dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. (616 aa)
ilvEBranched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (309 aa)
ADO50501.1KEGG: enc:ECL_05013 acetolactate synthase 2 regulatory subunit. (89 aa)
ADO50502.1Manually curated; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; KEGG: enc:ECL_05014 acetolactate synthase 2 catalytic subunit; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. (548 aa)
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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