Gene Ontology annotation through association of InterPro records with GO terms
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Automatic Gene Ontology annotation based on Rhea mapping
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
UniProtKB entry Q88FB2 for Pseudomonas putida KT2440 sucC
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UniProt records the exact ADP-forming succinate-CoA ligase reaction for Q88FB2.
"Reaction=succinate + ATP + CoA = succinyl-CoA + ADP + phosphate;"
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UniProt also records a GTP/GDP-forming succinate-CoA ligase reaction for Q88FB2.
"Reaction=GTP + succinate + CoA = succinyl-CoA + GDP + phosphate;"
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UniProt records Mg2+ as a cofactor and one bound Mg2+ ion per SucC subunit.
"Note=Binds 1 Mg(2+) ion per subunit."
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UniProt places SucC in the heterotetrameric succinate-CoA ligase complex.
"Heterotetramer of two alpha and two beta subunits."
OpenScientist deep research report for sucC
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The report summarizes the SucC/SucD division of labor in the heterotetrameric SCS complex.
"SucC contributes the nucleotide chemistry and the dicarboxylate specificity, while SucD carries the catalytic histidine and part of the CoA/succinate site."
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The report records the absence of direct purified Q88FB2 kinetics or structure.
"All catalytic, kinetic, and structural conclusions are transferred by homology from *E. coli*, *T. aquaticus*, and mammalian SCS. There is no published crystal structure, purified-enzyme kinetics, or Km/kcat measurement specifically for Q88FB2."
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The report supports cytosolic localization for the bacterial enzyme.
"whereas the bacterial homolog Q88FB2 lacks such a signal and therefore functions as a **soluble cytoplasmic enzyme**"
Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440.
Succinyl coenzyme A synthetase of Pseudomonas aeruginosa with a broad specificity for nucleoside triphosphate (NTP) synthesis modulates specificity for NTP synthesis by the 12-kilodalton form of nucleoside diphosphate kinase.
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P. aeruginosa succinyl-CoA synthetase makes ATP and GTP in about equal amounts when given both nucleoside diphosphates.
"Scs synthesizes essentially an equimolar amount of ATP and GTP"
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The enzyme copurifies with nucleoside diphosphate kinase, so the result is not a clean measure of intrinsic nucleotide specificity.
"Scs was previously shown to copurify with Ndk, presumably as a complex."