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
korA2-oxoglutarate ferredoxin oxidoreductase alpha subunit; PMID: 11401501 best DB hits: BLAST: embl:CAC08296.1; (AL392148) putative oxidoreductase [Streptomyces; E=1e-165 embl:CAB60189.1; (AL132824) putative oxidoreductase alpha-subunit; E=1e-164 pir:F70864; probable oxidoreductase alpha subunit - Mycobacterium; E=1e-160 COG: Rv2455c_2; COG0674 Pyruvate:ferredoxin oxidoreductase and related; E=1e-106 Rv2455c_1; COG1014 Pyruvate:ferredoxin oxidoreductase and related; E=2e-46 BH2374_2; COG0674 Pyruvate:ferredoxin oxidoreductase and related; E=2e-40 PFAM: PF01855; Pyruvate flavodoxin/ferredo [...] (627 aa)    
Predicted Functional Partners:
korB
2-oxoglutarate ferredoxin oxidoreductase beta subunit; PMID: 11401501 best DB hits: BLAST: embl:CAC08295.1; (AL392148) putative oxidoreductase [Streptomyces; E=1e-104 embl:CAB60188.1; (AL132824) putative oxidoreductase beta-subunit; E=1e-103 pir:E70864; probable oxidoreductase - Mycobacterium tuberculosis; E=2e-94 COG: Rv2454c; COG1013 Pyruvate:ferredoxin oxidoreductase and related; E=1e-95 PFAM: PF02775; Thiamine pyrophosphate enzyme,; E=0.19.
 0.999
icd
Isocitrate dehydrogenase; PMID: 4149369 best DB hits: BLAST: swissprot:P16100; IDH_AZOVI ISOCITRATE DEHYDROGENASE [NADP]; E=0.0 pir:B81143; isocitrate dehydrogenase NMB0920 [imported] - Neisseria; E=0.0 pir:B82236; isocitrate dehydrogenase VC1141 [imported] - Vibrio; E=0.0 COG: NMB0920; COG2838 Monomeric isocitrate dehydrogenase; E=0.0; Belongs to the monomeric-type IDH family.
  
 
 0.986
ldh
L-lactate dehydrogenase; PMID: 3122782 PMID: 3118900 best DB hits: BLAST: swissprot:P00345; LDH_BACME L-LACTATE DEHYDROGENASE -----pir:; E=3e-49 swissprot:P20619; LDHX_BACPS L-LACTATE DEHYDROGENASE X -----; E=6e-47 swissprot:P16115; LDH_THEMA L-LACTATE DEHYDROGENASE ----- pir:; E=3e-46 COG: TM1867; COG0039 Malate/lactate dehydrogenases; E=2e-47 PFAM: PF00056; lactate/malate dehydrogenase, NA; E=6.7e-46 PF02866; lactate/malate dehydrogenase, al; E=2.4e-36; Belongs to the LDH/MDH superfamily.
  
 
 0.972
ldh-2
L-lactate/malate dehydrogenase; PMID: 8404889 PMID: 3098260 best DB hits: BLAST: swissprot:P16115; LDH_THEMA L-LACTATE DEHYDROGENASE -----pir:; E=2e-51 pdb:1A5Z; Lactate Dehydrogenase From Thermotoga Maritima; E=2e-51 pdb:1LLC; L-Lactate Dehydrogenase (E.C.1.1.1.27) Complex With; E=9e-49 COG: TM1867; COG0039 Malate/lactate dehydrogenases; E=2e-52 PFAM: PF00056; lactate/malate dehydrogenase, NA; E=7.5e-36 PF02866; lactate/malate dehydrogenase, al; E=5e-36; Belongs to the LDH/MDH superfamily.
  
 
 0.972
RB7621
Probable ferredoxin MJ0251-putative Fe-S containing oxidoreductase; Best DB hits: BLAST: swissprot:Q57699; FER5_METJA PUTATIVE FERREDOXIN MJ0251 -----; E=8e-10 pir:B72286; ferredoxin - Thermotoga maritima (strain MSB8) -----; E=9e-09 pir:B72206; ferredoxin - Thermotoga maritima (strain MSB8) -----; E=1e-05 COG: MJ0251; COG1146 Ferredoxin 3; E=7e-11 TM1292; COG1149 MinD superfamily P-loop ATPase containing an; E=0.002 AF0427; COG1146 Ferredoxin 3; E=0.004 PFAM: PF00037; 4Fe-4S binding domain; E=0.0025.
  
 
 0.966
gdhA
Glutamate dehydrogenase A; PMID: 7551585 best DB hits: BLAST: swissprot:O04937; DHEA_NICPL GLUTAMATE DEHYDROGENASE A (GDH A); E=1e-115 swissprot:Q43314; DHE1_ARATH GLUTAMATE DEHYDROGENASE 1 (GDH 1); E=1e-115 pir:T04342; glutamate dehydrogenase (EC 1.4.1.2) - maize -----; E=1e-114 COG: TM1015; COG0334 Glutamate dehydrogenase/leucine dehydrogenase; E=1e-99 PFAM: PF02812; Glu/Leu/Phe/Val dehydrogenase; E=3.1e-56 PF00044; Glyceraldehyde 3-phosphate de; E=0.76 PF02254; KTN NAD-binding domain; E=0.33; Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
  
 
 0.956
pta
Phosphate acetyltransferase; Involved in acetate metabolism. In the N-terminal section; belongs to the CobB/CobQ family.
    
 0.956
sucC
succinyl-CoA synthetase (beta subunit); Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
  
 
 0.951
sucD
Putative succinyl-CoA synthetase alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.
  
 
 0.951
acs
Acetyl-coenzyme A synthetase; Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA; Belongs to the ATP-dependent AMP-binding enzyme family.
  
 
 0.949
Your Current Organism:
Rhodopirellula baltica
NCBI taxonomy Id: 243090
Other names: Pirellula sp. 1, R. baltica SH 1, Rhodopirellula baltica SH 1, Rhodopirellula baltica str. SH 1, Rhodopirellula baltica strain SH 1
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