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Mkms_1952 Mkms_1952 Mkms_1953 Mkms_1953 leuB leuB leuC leuC leuD leuD Mkms_2340 Mkms_2340 Mkms_2617 Mkms_2617 Mkms_2982 Mkms_2982 Mkms_3815 Mkms_3815 sucD sucD sucC sucC Mkms_4483 Mkms_4483
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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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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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Edges represent protein-protein associations
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
Mkms_1952TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: mmc:Mmcs_1906 acetolactate synthase, large subunit, biosynthetic type. (619 aa)
Mkms_1953TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: mmc:Mmcs_1907 acetolactate synthase, small subunit. (172 aa)
leuB3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. (336 aa)
leuC3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (481 aa)
leuD3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. (197 aa)
Mkms_2340PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: mmc:Mmcs_2293 thiamine pyrophosphate enzyme-like TPP binding region; Belongs to the TPP enzyme family. (570 aa)
Mkms_2617PFAM: isocitrate/isopropylmalate dehydrogenase; KEGG: mmc:Mmcs_2572 3-isopropylmalate dehydrogenase. (360 aa)
Mkms_2982PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: mmc:Mmcs_2938 thiamine pyrophosphate enzyme-like TPP-binding protein. (582 aa)
Mkms_3815PFAM: L-carnitine dehydratase/bile acid-inducible protein F; KEGG: mmc:Mmcs_3742 L-carnitine dehydratase/bile acid-inducible protein F; Belongs to the CoA-transferase III family. (402 aa)
sucDsuccinyl-CoA synthetase (ADP-forming) alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. (300 aa)
sucCsuccinyl-CoA synthetase (ADP-forming) beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (387 aa)
Mkms_4483PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: mmc:Mmcs_4396 thiamine pyrophosphate enzyme-like TPP-binding protein; Belongs to the TPP enzyme family. (571 aa)
Your Current Organism:
Mycobacterium sp. KMS
NCBI taxonomy Id: 189918
Other names: M. sp. KMS
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