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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
Hhal_1908cob(I)yrinic acid a,c-diamide adenosyltransferase; Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids. (202 aa)    
Predicted Functional Partners:
cobQ
Adenosylcobyric acid synthase (glutamine-hydrolysing); Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.
  
 0.998
Hhal_1853
Adenosylcobinamide kinase; Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
 
  
 0.979
cobD
Adenosylcobinamide-phosphate synthase; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
 
  
 0.979
Hhal_1909
TIGRFAM: cobyrinic acid a,c-diamide synthase; PFAM: Cobyrinic acid a,c-diamide synthase; CobB/CobQ domain protein glutamine amidotransferase; KEGG: abo:ABO_2367 acid--ammonia (or amine) ligases (amide synthases).
 
 
 0.979
cobS
Cobalamin-5'-phosphate synthase; Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate; Belongs to the CobS family.
 
 
 0.970
Hhal_1858
PFAM: aminotransferase, class I and II; KEGG: tbd:Tbd_2715 cobalamin biosynthetic protein CobC.
 
  
 0.969
Hhal_1925
TIGRFAM: ATP--cobalamin adenosyltransferase; PFAM: cobalamin adenosyltransferase; KEGG: xcb:XC_3435 hypothetical protein; Belongs to the Cob(I)alamin adenosyltransferase family.
    
 0.934
Hhal_1963
TIGRFAM: cobyrinic acid a,c-diamide synthase; PFAM: Cobyrinic acid a,c-diamide synthase; CobB/CobQ domain protein glutamine amidotransferase; KEGG: aeh:Mlg_1666 cobyrinic acid a,c-diamide synthase.
 
 
 0.934
Hhal_1348
KEGG: mca:MCA2296 precorrin-6Y C5,15-methyltransferase (decarboxylating); TIGRFAM: precorrin-6y C5,15-methyltransferase (decarboxylating), CbiE subunit; precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; PFAM: Uroporphyrin-III C/tetrapyrrole (Corrin/Porphyrin) methyltransferase.
     
 0.727
cysG1
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.
    
 0.666
Your Current Organism:
Halorhodospira halophila
NCBI taxonomy Id: 349124
Other names: H. halophila SL1, Halorhodospira halophila DSM 244, Halorhodospira halophila SL 1, Halorhodospira halophila SL1, Halorhodospira halophila str. SL1, Halorhodospira halophila strain SL1
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