STRINGSTRING
sucC sucC ADC69049.1 ADC69049.1 ADC69109.1 ADC69109.1 sucD sucD ADC69627.1 ADC69627.1 ADC69710.1 ADC69710.1
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second shell of interactors
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Your Input:
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. (364 aa)
ADC69049.1KEGG: mja:MJ1294 fumarate hydratase; TIGRFAM: hydro-lyase, Fe-S type, tartrate/fumarate subfamily, alpha subunit; PFAM: Fe-S type hydro-lyase tartrate/fumarate alpha region. (282 aa)
ADC69109.1TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: protein of unknown function DUF224 cysteine-rich region domain protein; ferredoxin; KEGG: mja:MJ0092 succinate dehydrogenase/fumarate reductase iron-sulfur subunit. (489 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. (288 aa)
ADC69627.1PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; KEGG: mfe:Mefer_1238 fumarate reductase/succinate dehydrogenase flavoprotein domain protein. (540 aa)
ADC69710.1KEGG: mja:MJ0617 tartrate dehydratse, subunit beta (TtdB); TIGRFAM: hydro-lyase, Fe-S type, tartrate/fumarate subfamily, beta subunit; PFAM: Fe-S type hydro-lyase tartrate/fumarate beta region. (218 aa)
Your Current Organism:
Methanocaldococcus sp. FS40622
NCBI taxonomy Id: 644281
Other names: M. sp. FS406-22, Methanocaldococcus sp. FS406-22
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