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
ADZ10487.1Magnesium chelatase; PFAM: von Willebrand factor, type A; ATPase, AAA-5; KEGG: mmg:MTBMA_c09440 cobaltochelatase subunit-like protein; SMART: von Willebrand factor, type A; ATPase, AAA+ type, core. (711 aa)    
Predicted Functional Partners:
ADZ09078.1
PFAM: Flavodoxin/nitric oxide synthase; KEGG: rci:RCIX1909 putative protoporphyrinogen oxidase.
     
  0.900
ADZ09910.1
Geranylgeranylglycerol-phosphate geranylgeranyltransferase; KEGG: rci:LRC477 prenyltransferase; PFAM: UbiA prenyltransferase.
 
  
 0.704
ADZ08768.1
Digeranylgeranylglyceryl phosphate synthase; Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). This reaction is the second ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
 
  
 0.679
ADZ10579.1
Geranylgeranyl reductase; KEGG: mth:MTH725 hypothetical protein; TIGRFAM: Geranylgeranyl reductase, plant/prokaryotic; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase.
 
  
 0.674
hemC
Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
  
  
 0.632
ADZ08723.1
Digeranylgeranylglycerophospholipid reductase; Is involved in the reduction of 2,3- digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3- diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di- O-geranylgeranylglyceryl phosphate (DGGGP) via the hydrogenation of each double bond of the isoprenoid chains.
 
  
 0.629
ADZ10252.1
Digeranylgeranylglycerophospholipid reductase; Is involved in the reduction of 2,3- digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3- diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di- O-geranylgeranylglyceryl phosphate (DGGGP) via the hydrogenation of each double bond of the isoprenoid chains.
 
  
 0.628
cbiA
Cobyrinic acid A,C-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source.
 
   
 0.557
ADZ10488.1
KEGG: mru:mru_1094 hypothetical protein.
       0.508
ADZ10489.1
KEGG: mru:mru_1095 hypothetical protein.
       0.508
Your Current Organism:
Methanobacterium lacus
NCBI taxonomy Id: 877455
Other names: DSM 24406, JCM 17760, M. lacus, Methanobacterium lacus Borrel et al. 2012, Methanobacterium sp. 17A1, Methanobacterium sp. AL-21, strain 17A1
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