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
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[Homology]
Score
cysHPhosphoadenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite. Belongs to the PAPS reductase family. CysH subfamily. (243 aa)    
Predicted Functional Partners:
cysC
Adenylylsulfate kinase; Catalyzes the synthesis of activated sulfate.
 0.999
cysI
Sulfite 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.
 
 
 0.999
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
cysN
Sulfate adenylyltransferase subunit 1; 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.
 0.998
cobA
Sirohydrochlorin ferrochelatase; 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.
 
  
 0.979
cysQ
Adenosine-3'(2'),5'-bisphosphate nucleotidase; Converts adenosine-3',5'-bisphosphate (PAP) to AMP. Belongs to the inositol monophosphatase superfamily. CysQ family.
  
 
 0.958
sseA
3-mercaptopyruvate sulfurtransferase; Catalyzes the transfer of a sulfur ion to cyanide or to other thiol compounds; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.953
cysD
Sulfate adenylyltransferase subunit 2; With CysN catalyzes the formation of adenylylsulfate from sulfate and ATP; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
0.946
glpE
Thiosulfate sulfurtransferase; Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
     
 0.942
tauD
Catalyzes the conversion of taurine (2-aminoethanesulfonate) to sulfite and aminoacetaldehyde concurrently with the conversion of alpha-ketoglutarate to succinate and carbon dioxide; non-heme iron oxidase; allows the use of taurine as an alternative sulfur source; forms homodimers; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.942
Your Current Organism:
Erwinia tracheiphila
NCBI taxonomy Id: 65700
Other names: ATCC 33245, Bacillus tracheiphilus, Bacterium tracheiphilus, CFBP 2355, CIP 105205, DSM 21139, E. tracheiphila, Erwinia amylovora var. tracheiphila, ICMP 5845, LMG 2707, LMG 2906, LMG:2707, LMG:2906, NCPPB 2452
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