STRINGSTRING
patA patA patB patB nifS_1 nifS_1 nifS_2 nifS_2 aspC_1 aspC_1 mdeA_1 mdeA_1 aspC_2 aspC_2 dapL dapL mdeA_2 mdeA_2 ltaE_1 ltaE_1 hisC hisC csd_2 csd_2 glyA glyA norG norG argD argD ltaE_2 ltaE_2 CUN23477.1 CUN23477.1 sufS sufS serC serC iscS iscS hemL hemL csd_1 csd_1 cobD cobD
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.
Node Color
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:
patAPutative aminotransferase A. (393 aa)
patBCystathionine beta-lyase PatB. (389 aa)
nifS_1Cysteine desulfurase. (398 aa)
nifS_2Cysteine desulfurase; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily. (395 aa)
aspC_1Aspartate aminotransferase. (390 aa)
mdeA_1Methionine gamma-lyase. (436 aa)
aspC_2Aspartate aminotransferase. (394 aa)
dapLLL-diaminopimelate aminotransferase; Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL- diaminopimelate. (404 aa)
mdeA_2Methionine gamma-lyase. (427 aa)
ltaE_1Low specificity L-threonine aldolase. (345 aa)
hisCHistidinol-phosphate aminotransferase; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (357 aa)
csd_2Probable cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. (417 aa)
glyAPyridoxal-phosphate-dependent serine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. (414 aa)
norGHTH-type transcriptional regulator norG. (489 aa)
argDAcetylornithine aminotransferase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (397 aa)
ltaE_2Low specificity L-threonine aldolase. (270 aa)
CUN23477.1Putative aminotransferase MSMEG_6286. (430 aa)
sufSCysteine desulfurase. (378 aa)
serCPhosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. (361 aa)
iscSCysteine desulfurase. (387 aa)
hemLGlutamate-1-semialdehyde 2%2C1-aminomutase. (428 aa)
csd_1Probable cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. (408 aa)
cobDThreonine-phosphate decarboxylase. (347 aa)
Your Current Organism:
Eubacterium ramulus
NCBI taxonomy Id: 39490
Other names: ATCC 29099, DSM 3995, E. ramulus
Server load: low (10%) [HD]