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gpmA gpmA hemA hemA hemD hemD hemL hemL gltB gltB pgi pgi gltS gltS ppc ppc pgk pgk gdh gdh glnA glnA hemN hemN aceA aceA sucD sucD sucC sucC lpdA lpdA gltD gltD gltX gltX sdhCD sdhCD sdhA sdhA sdhB sdhB
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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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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gpmAPHOSPHOGLYCEROMUTASE 1; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. (248 aa)
hemAGLUTAMYL-TRNA REDUCTASE; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (463 aa)
hemDUROPORPHYRINOGEN III SYNTHASE/METHYLTRANSFERASE. (598 aa)
hemLGLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE. (437 aa)
gltBGLUTAMINE 2-OXOGLUTARATE AMINOTRANSFERASE LARGE SU. (1510 aa)
pgiGLUCOSE-6-PHOSPHATE ISOMERASE. (540 aa)
gltSPUTATIVE GLUTAMYL-TRNA SYNTHETASE; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (496 aa)
ppcPHOSPHOENOLPYRUVATE CARBOXYLASE; Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle; Belongs to the PEPCase type 1 family. (919 aa)
pgkPHOSPHOGLYCERATE KINASE; Belongs to the phosphoglycerate kinase family. (405 aa)
gdhNADP-SPECIFIC GLUTAMATE DEHYDROGENASE; Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia. (447 aa)
glnAGLUTAMINE SYNTHETASE I. (477 aa)
hemNPUTATIVE ANAEROBIC COPROPORPHYRINOGEN III OXIDASE; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (380 aa)
aceAISOCITRATE LYASE; Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates. (432 aa)
sucDSUCCINYL-COA SYNTHETASE 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. (294 aa)
sucCSUCCINYL-COA SYNTHETASE 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. (402 aa)
lpdADIHYDROLIPOAMIDE DEHYDROGENASE. (469 aa)
gltDGLUTAMINE 2-OXOGLUTARATE AMINOTRANSFERASE. (506 aa)
gltXGLUTAMYL-TRNA SYNTHETASE-RELATED PROTEIN; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. (293 aa)
sdhCDSuccinate dehydrogenase CD. (257 aa)
sdhASuccinate dehydrogenase A. (673 aa)
sdhBSuccinate dehydrogenase B. (249 aa)
Your Current Organism:
Corynebacterium glutamicum
NCBI taxonomy Id: 196627
Other names: C. glutamicum ATCC 13032, Corynebacterium glutamicum ATCC 13032, Corynebacterium glutamicum str. ATCC 13032, Corynebacterium glutamicum strain ATCC 13032
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