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
cysISulfite reductase subunit beta; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (589 aa)    
Predicted Functional Partners:
cysJ
Sulfite reductase subunit alpha; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. Belongs to the NADPH-dependent sulphite reductase flavoprotein subunit CysJ family. In the N-terminal section; belongs to the flavodoxin family.
 0.999
cysH
Phosphoadenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite. Belongs to the PAPS reductase family. CysH subfamily.
 
 0.998
cysG
Siroheme synthase; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. Belongs to the precorrin methyltransferase family. In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.
 
  
 0.996
CysN
Sulfate adenylyltransferase; May be the GTPase, regulating ATP sulfurylase activity. Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily.
  
  
 0.986
CysD
Sulfate adenylyltransferase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.980
cysK
Cysteine synthase A; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the cysteine synthase/cystathionine beta- synthase family.
  
 
 0.966
cysA
Sulfate ABC transporter ATP-binding protein; Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system.
  
  
 0.943
metZ
O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide.
  
 0.921
CysW
Sulfate ABC transporter permease subunit CysW; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.890
CysU
Sulfate ABC transporter permease subunit CysT; Part of the ABC transporter complex (TC 3.A.1.6.1) involved in sulfate/thiosulfate import; Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.
  
  
 0.680
Your Current Organism:
Neisseria lactamica
NCBI taxonomy Id: 486
Other names: ATCC 23970, CCUG 5853, CIP 72.17, DSM 4691, N. lactamica, NCTC 10617, Neisseria lactamicus
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.