STRINGSTRING
Sps_03543 Sps_03543 Sps_03132 Sps_03132 Sps_02853 Sps_02853 Sps_01137 Sps_01137 serC serC Sps_04230 Sps_04230 glyA-2 glyA-2 glyA glyA Sps_00645 Sps_00645 glyA-3 glyA-3 Sps_04805 Sps_04805 Sps_03594 Sps_03594
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:
Sps_03543Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: cysteine synthase A; cysteine synthase; Belongs to the cysteine synthase/cystathionine beta- synthase family. (322 aa)
Sps_03132'PFAM: Serine acetyltransferase, N-terminal; Bacterial transferase hexapeptide (six repeats)'; TIGRFAM: serine O-acetyltransferase. (261 aa)
Sps_02853'PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; ACT domain; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain'. (409 aa)
Sps_01137Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. (353 aa)
serCPhosphoserine aminotransferase apoenzyme; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. (362 aa)
Sps_04230Phosphoserine phosphatase; PFAM: haloacid dehalogenase-like hydrolase; 'TIGRFAM: Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; phosphoserine phosphatase SerB'. (326 aa)
glyA-2Glycine/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. (421 aa)
glyASerine 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. (431 aa)
Sps_00645Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. (296 aa)
glyA-3Serine 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. (418 aa)
Sps_04805PFAM: Pyridoxal-phosphate dependent enzyme; 'TIGRFAM: 2,3-diaminopropionate biosynthesis protein SbnA'. (312 aa)
Sps_03594Serine O-acetyltransferase; PFAM: Bacterial transferase hexapeptide (six repeats); TIGRFAM: serine O-acetyltransferase. (273 aa)
Your Current Organism:
Shewanella psychrophila
NCBI taxonomy Id: 225848
Other names: CGMCC 1.6159, JCM 13876, S. psychrophila, Shewanella psychrophila Xiao et al. 2007 emend. Thorell et al. 2019, Shewanella sp. WP2, strain WP2
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