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
fabHUnannotated protein; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids; Belongs to the thiolase-like superfamily. FabH family. (332 aa)    
Predicted Functional Partners:
fabD
Unannotated protein.
 
 0.999
CJ673_06600
Unannotated protein; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
 
 0.997
plsX
Unannotated protein; Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
 
  
 0.997
accD
Unannotated protein; Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA; Belongs to the AccD/PCCB family.
 
 
 0.996
accB
Unannotated protein; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
  
 
 0.989
CJ673_07625
Unannotated protein.
  
 
 0.988
accA
Unannotated protein; Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
 
 
 0.987
CJ673_06610
Unannotated protein; Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. Belongs to the short-chain dehydrogenases/reductases (SDR) family.
 
 0.981
fabZ
Unannotated protein; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
 
  
 0.978
accC
Unannotated protein; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
  
 
 0.978
Your Current Organism:
Arcobacter cryaerophilus
NCBI taxonomy Id: 28198
Other names: A. cryaerophilus, ATCC 43158, Aliiarcobacter cryaerophilus, Arcibacter cryaerophilus, Arcobacter sp. LMG 10210, Arcobacter sp. LMG 10229, Arcobacter sp. LMG 9065, Arcobacter sp. LMG 9861, Arcobacter sp. LMG 9871, Arquibacter cryaerophilus, CCUG 17801, CIP 104014, Campylobacter cryaerophila, Campylobacter cryaerophilus, DSM 7289, LMG 24291, LMG 7536, LMG 9904, LMG:24291, LMG:7536, LMG:9904, NCTC 11885, strain 02766, strain A 169/B, strain A169/B, strain Neill A 169/B, strain Neill A1691B
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.