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
hemEUroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (355 aa)    
Predicted Functional Partners:
hemC
Hydroxymethylbilane synthase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family.
 
 0.985
cpoX
Coproporphyrinogen oxidase; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX.
 
 0.962
hemN
Coproporphyrinogen dehydrogenase; Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX. It can use NAD or NADP, but NAD is preferred; Belongs to the anaerobic coproporphyrinogen-III oxidase family; KEGG: vcy:IX92_00390 oxygen-independent coproporphyrinogen III oxidase.
 
 
 0.949
hemD
Uroporphyrinogen-III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
  
 
 0.940
cobA
Uroporphyrinogen-III C-methyltransferase; 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; In the N-terminal sectio; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family; In the C-terminal sectio; belongs to the precorrin methyltransferase family; KEGG: vcy:IX92_14505 uroporphy [...]
    
 0.920
ANS87297.1
Uroporphyrinogen-III C-methyltransferase; 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; In the N-terminal sectio; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family; In the C-terminal sectio; belongs to the precorrin methyltransferase family; KEGG: vcy:IX92_08050 uroporphy [...]
    
 0.920
hemH
Protoporphyrin ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family.
 
  
 0.913
hemX
KEGG: vpa:VP2990 uroporphyrin-III C-methyltransferase.
    
 0.907
hemB
Porphobilinogen synthase; Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity); Belongs to the ALAD family; KEGG: vch:VC0105 porphobilinogen synthase.
 
 
 0.783
hemL
Glutamate-1-semialdehyde 2,1-aminomutase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily; KEGG: yro:CH64_3351 glutamate-1-semialdehyde 2,1-aminomutase.
 
  
 0.707
Your Current Organism:
Vibrio scophthalmi
NCBI taxonomy Id: 45658
Other names: CAIM 75, CECT 4638, CIP 105211, LMG 19158, LMG:19158, V. scophthalmi, strain A089
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