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
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Textmining
[Homology]
Score
qhpBProbable quinohemoprotein amine dehydrogenase,alpha subunit. Homology to qhpB of P.putida of 50% (gi|34809688|pdb|1PBY|B(PDB (RCSB))). Quinoproteins are a class of amine-oxidising enzymes that catalyse the oxidation of biological amines, using quinone as a redox cofactor to store reducing equivalents. Quinohemoprotein amine dehydrogenase (QH-AmDH) from bacteria represents a new class of quinoproteins that contains both quinone and one or two hemes as redox active groups. The presence of extra redox active groups allows for intramolecular electron transfer. QH-AmDH is a heterotrimeric e [...] (381 aa)    
Predicted Functional Partners:
qhpC
Probable quinohemoprotein amine dehydrogenase,gamma subunit. Homology to qhnDH of P. putida of 54% (sprot|QADG_PSEPK(SRS). Quinoproteins are a class of amine-oxidising enzymes that catalyse the oxidation of biological amines, using quinone as a redox cofactor to store reducing equivalents. Quinohemoprotein amine dehydrogenase (QH-AmDH) from bacteria represents a new class of quinoproteins that contains both quinone and one or two hemes as redox active groups. The presence of extra redox active groups allows for intramolecular electron transfer. QH-AmDH is a heterotrimeric enzyme contai [...]
 
 
   0.991
qhpA
Probable quinohemoprotein amine dehydrogenase,alpha subunit. Homology to qhpA of P.putida of 50% (gi|18655859|pdb|1JMZ|A(PDB (RCSB))). Quinoproteins are a class of amine-oxidising enzymes that catalyse the oxidation of biological amines, using quinone as a redox cofactor to store reducing equivalents. Quinohemoprotein amine dehydrogenase (QH-AmDH) from bacteria represents a new class of quinoproteins that contains both quinone and one or two hemes as redox active groups. The presence of extra redox active groups allows for intramolecular electron transfer. QH-AmDH is a heterotrimeric e [...]
 
 
  0.990
qhpX
Conserved hypothetical qinohemoprotein amine dehydrogenase, unknown subunit. Homology to P. putida of 71% (gi|16950513|dbj|BAB72009.1|(NBCI ENTREZ)). InterPro:IPR000385; MoaA_NifB_PqqE. IPR007197; Radical_SAM. Pfam:PF04055; Radical_SAM. No signal peptide. No TMHs; Family membership.
 
     0.942
mauA
Probable methylamine dehydrogenase. Homology to mauD of P. denifrificans of 45% (CAA67190) carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. InterPro: Methylamine dehydrogenase L subunit (IPR004229) Pfam: Methylamine dehydrogenase, L chain signal peptide no TMHs; High confidence in function and specificity.
   
  0.899
gltB
Ferredoxin-dependent glutamate synthase,; Specificity unclear.
    
  0.889
exaA4
Quinoprotein ethanol dehydrogenase precursor (QEDH). Oxidizes primary alcohols and also acts on secondary alcohol, but not highly active on methanol. 37% Bac_PQQ.IPR002372; Bac_PQQ_repeat. Pfam:PF01011; PQQ; 2. Signal peptide:present; High confidence in function and specificity.
 
 0.820
norB
Nitric-oxide reductase subunit B (EC 1.7.99.7) (Nitric oxide reductase cytochrome b subunit). 69% similarity to the P.stutzeri NorB protein. COMPONENT OF THE ANAEROBIC RESPIRATORY CHAIN THAT TRANSFORMS NITRATE TO DINITROGEN (DENITRIFICATION). NorB IS THE CATALYTIC SUBUNIT OF THE ENZYME COMPLEX. SHOWS PROTON PUMP ACTIVITY ACROSS THE MEMBRANE IN DENITRIFYING BACTERIAL CELLS. THE MONONITROGEN REDUCTION IS PROBABLY COUPLED TO ELECTRON TRANSPORT PHOSPHORYLATION.Belongs to the heme-copper respiratory oxidase family. Swiss Prot: Q59647. IPR000883; COX1. PF00115; COX1; 1. TMHMM:predicted trans [...]
  
 0.790
azo1238
Conserved hypothetical secreted protein. Homology to ebA2217 of Azoarcus sp. EbN1 of 32% (gnl|keqq|eba:ebA2217(KEGG)). C-terminus is not homolog to COG0644. signal peptide present. no TMHS; Conserved hypothetical protein.
 
     0.774
subC
Subtilisin Savinase precursor, 36% identity to SwissProt; P29600. Has PF00082, Subtilase family;IPR000209, Pept_S8_S53;Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see Trypsin). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567. PROSITE;) PS00136; SUBTILASE_ASP; 1. PS00137; SUBTILASE_HIS; 1. PS00138; SUBTILASE_SER; 1.
 
     0.767
azo1236
ATP-binding cassette (ABC) transporters form a large family of proteins responsible for translocation of a variety of compounds across biological membranes. They are composed of two transmembrane domains responsible for binding and transport and two nucleotide-binding domains responsible for coupling the energy of ATP hydrolysis to conformational changes in the TMDs. Similar to TREMBL:Q88H94 (52% identity); TREMBL:Q9RXZ1 (29% identity); SWISSPROT:Q9WYC4 (25% identity). Pfam (PF00664): ABC transporter transmembrane region. Pfam (PF00005): ABC transporter. TMHMM reporting six transmembra [...]
  
     0.750
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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