STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
metZO-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide. (389 aa)    
Predicted Functional Partners:
metX
Homoserine O-acetyltransferase / Aspartokinase / Homoserine dehydrogenase; This enzyme is a modular protein with a homoserine O-acetyltransferase module (N-terminal) that catalyses the homoserine acetylation and belongs to the alpha/beta hydrolase fold family, an aspartate kinase module (central) that catalyzes the phosphorylation of aspartate and belongs to the amino acid kinase family and, in C- terminal part, a homoserine dehydrogenase module that catalyzes the NAD-dependent reduction of aspartate beta- semialdehyde into homoserine. This module is composed of a substrate-binding dom [...]
 
 
 0.982
cysK2
The cysteine synthase is the enzyme responsible for the formation of cysteine from O-acetyl-serine and hydrogen sulfide with the concomitant release of acetic acid; Uses the pyridoxal phosphate as cofactor (vitamin B6) attached to a conserved lysine residue; Belongs to the cysteine synthase/cystathionine beta-synthase family; Localized in the cytoplasm; High confidence in function and specificity.
 0.969
cysK1
The cysteine synthase is the enzyme responsible for the formation of cysteine from O-acetyl-serine and hydrogen sulfide with the concomitant release of acetic acid; Uses the pyridoxal phosphate as cofactor (vitamin B6) attached to a conserved lysine residue; Belongs to the cysteine synthase/cystathionine beta-synthase family; Localized in the cytoplasm; High confidence in function and specificity.
 0.968
metY
Cys/Met metabolism pyridoxal-phosphate-dependent enzymes; Transforms O-acetylhomoserine into L-methionine. Also reacts with other thiols and H2S, producing homocysteine or thioethers; Uses a pyridoxal phosphate group as cofactor, attached to a lysine residue located in the central section of the enzyme; Localized in the cytoplasm; High confidence in function and specificity.
 
 
0.964
metE
5-Methyltetrahydropteroyltriglutamate- homocysteine methyltransferase; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family.
  
 
 0.955
metH-2
Methionine synthase, homocysteine-binding module; Methionine synthase or 5-methyltetrahydrofolate-homocysteine S-methyltransferase catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate; L-homocysteine is bound via the zinc atom; Uses the cobalamin (vitamin B12) and zinc as cofactors; This sequence corresponds to the homocysteine-binding domain (Hcy-binding domain) only; Belongs to the vitamin-B12 dependent methionine synthase family; Localize [...]
  
 
 0.946
thrA
ThrA is a fusion-protein between aspartate kinase I (N-terminal) and homoserine dehydrogenase I (C-terminal) involved in L-Lysine and L-threonine biosynthesis pathways. Aspartate kinase I converts L-aspartate to 4-phospho-L-aspartate and belongs to the amino acid kinase family. Homoserine dehydrogenase I converts the L-homoserine to L-aspartate 4-semialdehyde. Homoserine dehydrogenase I is composed of a substrate-binding domain belonging to Homoserine dehydrogenase family and a NAD-binding domain (Rossman fold). ThrA features also two central regulatory ACT domains; Localized in the cy [...]
 
 
 0.930
metH
Methionine synthase, cobalamin-binding module; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
  
 
 0.924
sirA
Sulfite reductase catalyses the six-electron reduction reactions of sulfite to sulfide; Contains a Fe(4)S(4) cluster coupled to a siroheme through a cysteine bridge; Would contains a C-terminal HEPN domain of unknown function; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family; Localized in the cytoplasm; High confidence in function and specificity.
  
 0.923
ahcY
Adenosylhomocysteinase; May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
 
 0.920
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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