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thiH thiH yjjW yjjW yjeK yjeK pflC pflC STM4012 STM4012 hemN hemN STM3966 STM3966 yhcC yhcC ygiR ygiR STM3123 STM3123 yggW yggW ygcF ygcF yfgB yfgB STM1287 STM1287 pflA pflA yliG yliG pflE pflE moaA moaA bioB bioB miaB miaB lipA lipA STM0036 STM0036
Nodes:
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
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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:
thiHThiamin biosynthesis protein, thiazole moiety; Catalyzes the radical-mediated cleavage of tyrosine to 2- iminoacetate and 4-cresol; Belongs to the radical SAM superfamily. ThiH family. (377 aa)
yjjWPyruvate formate lyase activating enzyme; Similar to E. coli putative activating enzyme (AAC77332.1); Blastp hit to AAC77332.1 (287 aa), 81% identity in aa 1 - 287. (287 aa)
yjeKPutative aminomutase; With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3- aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine) (By similarity). (342 aa)
pflCSimilar to E. coli probable pyruvate formate lyase activating enzyme 2 (AAC76934.1); Blastp hit to AAC76934.1 (292 aa), 78% identity in aa 1 - 292. (292 aa)
STM4012Putative coproporphyrinogen III oxidase and related FeS oxidoreductase; Similar to E. coli O2-independent coproporphyrinogen III oxidase (AAC76864.1); Blastp hit to AAC76864.1 (459 aa), 28% identity in aa 14 - 248, 25% identity in aa 319 - 379. (413 aa)
hemNO2-independent coproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX. (457 aa)
STM3966Similar to E. coli putative arylsulfatase regulator (AAC76803.1); Blastp hit to AAC76803.1 (411 aa), 47% identity in aa 11 - 402. (447 aa)
yhcCPutative FeS oxidoreductase; Similar to E. coli orf, hypothetical protein (AAC76243.1); Blastp hit to AAC76243.1 (309 aa), 94% identity in aa 1 - 307. (309 aa)
ygiRPutative Fe-S oxidoreductase family 2; Similar to E. coli orf, hypothetical protein (AAC76051.1); Blastp hit to AAC76051.1 (413 aa), 46% identity in aa 1 - 26. (723 aa)
STM3123Similar to E. coli putative arylsulfatase regulator (AAC76803.1); Blastp hit to AAC76803.1 (411 aa), 36% identity in aa 4 - 248, 34% identity in aa 230 - 387. (394 aa)
yggWPutative 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. (378 aa)
ygcFPutative organic radical activating enzymes; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. (223 aa)
yfgBPutative Fe-S-cluster redox enzyme; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. (388 aa)
STM1287Similar to E. coli putative arylsulfatase regulator (AAC76803.1); Blastp hit to AAC76803.1 (411 aa), 46% identity in aa 10 - 401. (398 aa)
pflAPyruvate formate lyase activating enzyme 1; Activation of pyruvate formate-lyase under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine; Belongs to the organic radical-activating enzymes family. (274 aa)
yliGPutative Fe-S oxidoreductases family 1; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (441 aa)
pflESimilar to E. coli putative pyruvate formate-lyase 2 activating enzyme (AAC73911.1); Blastp hit to AAC73911.1 (308 aa), 87% identity in aa 10 - 308. (299 aa)
moaAMolybdopterin biosynthesis, protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (329 aa)
bioBBiotin synthetase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family. (346 aa)
miaBMethylthiolation of isopentenylated A37 derivatives in rRNA; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. (474 aa)
lipALipoate synthase, an iron-sulfur enzyme; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. (321 aa)
STM0036Similar to E. coli putative arylsulfatase regulator (AAC76803.1); Blastp hit to AAC76803.1 (411 aa), 46% identity in aa 8 - 401. (396 aa)
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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