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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
cobA1Uroporphyrinogen-III C-methyltransferase; This enzyme catalyzes two sequential methylation reactions, forming precorrin-1 and precorrin-2 by methylations at C-2 and C-7 of uroporphyrinogen III respectively; It is the first enzyme specific to the cobalamin (vitamin B12) pathway and precorrin-2 is a common intermediate in the biosynthesis of corrinoids such as vitamin B12, siroheme and coenzyme F430; Belongs to the precorrin methyltransferase family; Localized in the cytoplasm; High confidence in function and specificity. (265 aa)    
Predicted Functional Partners:
sirC
Precorrin-2 dehydrogenase; This protein Catalyzes the dehydrogenation of precorrin-2 into siroheme that is the second step of the siroheme biosynthesis; This reaction consists of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin used as precursor in siroheme biosynthesis; Putatively also catalized the third step that is the conversion of sirohydrochlorin into siroheme; High confidence in function and specificity.
 
 0.998
hemCD
Porphobilinogen deaminase / Uroporphyrinogen-III synthase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family.
  
 0.988
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.
 
  
 0.976
hemD
Uroporphyrinogen-III synthase is the fourth enzyme in the heme biosynthesis pathway. It catalyzes the reaction: hydroxymethylbilane = uroporphyrinogen III + H2O. Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.918
hemE
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
    
 0.917
cobA2
Uroporphyrin-III C-methyltransferase; This enzyme catalyzes two sequential methylation reactions, forming precorrin-1 and precorrin-2 by methylations at C-2 and C-7 of uroporphyrinogen III respectively; It is the first enzyme specific to the cobalamin (vitamin B12) pathway and precorrin-2 is a common intermediate in the biosynthesis of corrinoids such as vitamin B12, siroheme and coenzyme F430; Belongs to the precorrin methyltransferase family; Localized in the cytoplasm; High confidence in function and specificity.
  
  
 
0.907
hemB
Delta-aminolevulinic acid dehydratase catalyzes the second step in the biosynthesis of heme, the condensation of two molecules of 5-aminolevulinate to form porphobilinogen. The enzyme is an oligomer composed of eight identical subunits. Each of the subunits binds a zinc ion. A lysine has been implicated in the catalytic mechanism. Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ALAD family.
 
  
 0.858
cysH
The 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase called also PAPS sulfotransferase catalyses the reduction of activated sulfate into sulfite; The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP); Belongs to the PAPS reductase family; Localized in the cytoplasm; High confidence in function and specificity.
 
  
 0.806
trxB3
Thioredoxin reductase; The active site of this enzyme is a redox-active disulfide bond. TrxB uses the FAD to shuttle reducing equivalents from NAD(P)H to a Cys residue that is usually a part of a redox-active disulphide bridge. In a second step, the reduced disulphide reduces the substrate; Acts as an homodimer and binds one FAD molecule per subunit; Belongs to the class 2 of the pyridine nucleotide- disulphide reductases (PNDR); Localized in the cytoplasm; High confidence in function and specificity.
     
 0.791
cysD
The sulfate adenylyltransferase (ATP sulfurylase) catalyses the activation of sulfate with ATP to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. ATP sulfurylase is a heterodimer composed of cysD, the smaller subunit, and cysN; Belongs to the PAPS reductase family; Localized in the cytoplasm; High confidence in function and specificity.
 
  
 0.786
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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