STRINGSTRING
gcvH gcvH AFG36520.1 AFG36520.1 AFG36584.1 AFG36584.1 speA speA AFG36853.1 AFG36853.1 AFG37048.1 AFG37048.1 AFG37221.1 AFG37221.1 AFG37272.1 AFG37272.1 dtd dtd pdxT pdxT AFG38502.1 AFG38502.1 AFG38618.1 AFG38618.1 AFG37724.1 AFG37724.1 AFG37817.1 AFG37817.1
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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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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
Others
textmining
co-expression
protein homology
Your Input:
gcvHGlycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. (126 aa)
AFG36520.1Theronine dehydrogenase-like Zn-dependent dehydrogenase; PFAM: Alcohol dehydrogenase GroES-like domain; Zinc-binding dehydrogenase; TIGRFAM: 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase. (338 aa)
AFG36584.1Glycine dehydrogenase, decarboxylating; PFAM: Glycine cleavage T-protein C-terminal barrel domain; Aminomethyltransferase folate-binding domain; Glycine cleavage system P-protein; TIGRFAM: glycine dehydrogenase (decarboxylating); glycine cleavage system T protein; Belongs to the GcvT family. (1340 aa)
speAArginine decarboxylase, biosynthetic; Catalyzes the biosynthesis of agmatine from arginine. (638 aa)
AFG36853.1Phosphopantothenoylcysteine decarboxylase/phosphopantothenate--cysteine ligase; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4- phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family. (417 aa)
AFG37048.1Hypothetical protein; PFAM: SlyX. (67 aa)
AFG37221.1Ornithine carbamoyltransferase; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. (311 aa)
AFG37272.1Arginine deiminase; PFAM: Amidinotransferase. (418 aa)
dtdD-tyrosyl-tRNA(Tyr) deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. (149 aa)
pdxTPyridoxal 5'-phosphate synthase, glutaminase subunit Pdx2; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. (202 aa)
AFG38502.1Putative TIM-barrel fold metal-dependent hydrolase; PFAM: Amidohydrolase family; manually curated. (521 aa)
AFG38618.1acetyl-CoA acetyltransferase; PFAM: Thiolase, C-terminal domain; Thiolase, N-terminal domain; TIGRFAM: acetyl-CoA acetyltransferases; Belongs to the thiolase-like superfamily. Thiolase family. (401 aa)
AFG37724.1KamA family protein; PFAM: Lysine-2,3-aminomutase; Radical SAM superfamily; TIGRFAM: KamA family protein. (330 aa)
AFG37817.1PFAM: Phenylalanine and histidine ammonia-lyase; TIGRFAM: phenylalanine ammonia-lyase. (664 aa)
Your Current Organism:
Spirochaeta africana
NCBI taxonomy Id: 889378
Other names: S. africana DSM 8902, Spirochaeta africana DSM 8902, Spirochaeta africana Z-7692, Spirochaeta africana str. DSM 8902, Spirochaeta africana strain DSM 8902
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