STRINGSTRING
fadA fadA fadB fadB Sps_00540 Sps_00540 Sps_00789 Sps_00789 Sps_00790 Sps_00790 Sps_00791 Sps_00791 fadJ fadJ fadI fadI Sps_02041 Sps_02041 Sps_02045 Sps_02045 Sps_02046 Sps_02046 Sps_02081 Sps_02081 Sps_02082 Sps_02082 Sps_02083 Sps_02083 Sps_02084 Sps_02084 Sps_02086 Sps_02086 Sps_02087 Sps_02087 Sps_02088 Sps_02088 Sps_02565 Sps_02565 Sps_02566 Sps_02566 Sps_02823 Sps_02823 ilvE ilvE Sps_03227 Sps_03227 Sps_04461 Sps_04461 Sps_04462 Sps_04462 Sps_04622 Sps_04622 Sps_05377 Sps_05377
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:
fadA3-ketoacyl-CoA thiolase; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. (387 aa)
fadBFatty oxidation complex, alpha subunit FadB; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (717 aa)
Sps_00540'PFAM: Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; Glu/Leu/Phe/Val dehydrogenase, dimerisation domain'. (344 aa)
Sps_00789Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase component alpha subunit; PFAM: Dehydrogenase E1 component. (392 aa)
Sps_00790Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase component beta subunit; 'PFAM: Transketolase, C-terminal domain; Transketolase, pyrimidine binding domain'. (320 aa)
Sps_00791Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase component; PFAM: 2-oxoacid dehydrogenases acyltransferase (catalytic domain); e3 binding domain; Biotin-requiring enzyme. (536 aa)
fadJFatty oxidation complex, alpha subunit FadJ; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (708 aa)
fadI3-ketoacyl-CoA thiolase; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. (436 aa)
Sps_02041PFAM: NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; NAD binding domain of 6-phosphogluconate dehydrogenase; TIGRFAM: 3-hydroxyisobutyrate dehydrogenase; Belongs to the HIBADH-related family. (312 aa)
Sps_02045Methylmalonate-semialdehyde dehydrogenase (acylating); PFAM: Aldehyde dehydrogenase family; TIGRFAM: methylmalonic acid semialdehyde dehydrogenase. (501 aa)
Sps_02046acetyl-CoA acetyltransferase; 'PFAM: Thiolase, C-terminal domain; Thiolase, N-terminal domain'; TIGRFAM: acetyl-CoA acetyltransferases; Belongs to the thiolase-like superfamily. Thiolase family. (396 aa)
Sps_02081'PFAM: Acyl-CoA dehydrogenase, C-terminal domain; Acyl-CoA dehydrogenase, middle domain; Acyl-CoA dehydrogenase, N-terminal domain'. (389 aa)
Sps_02082acetyl-CoA carboxylase, carboxyltransferase component (subunits alpha and beta); PFAM: Carboxyl transferase domain. (535 aa)
Sps_02083PFAM: Enoyl-CoA hydratase/isomerase family. (291 aa)
Sps_020843-methylcrotonoyl-CoA carboxylase, alpha subunit; 'PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Biotin carboxylase C-terminal domain; Carbamoyl-phosphate synthase L chain, N-terminal domain; Biotin-requiring enzyme'; 'TIGRFAM: acetyl-CoA carboxylase, biotin carboxylase subunit'. (701 aa)
Sps_02086hydroxymethylglutaryl-CoA lyase; PFAM: HMGL-like. (296 aa)
Sps_02087PFAM: Coenzyme A transferase; 'TIGRFAM: 3-oxoacid CoA-transferase, A subunit'. (237 aa)
Sps_02088PFAM: Coenzyme A transferase; 'TIGRFAM: 3-oxoacid CoA-transferase, B subunit'. (218 aa)
Sps_02565PFAM: Aminotransferase class-III; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (445 aa)
Sps_02566Methylmalonate-semialdehyde dehydrogenase (acylating); PFAM: Aldehyde dehydrogenase family; TIGRFAM: methylmalonic acid semialdehyde dehydrogenase. (501 aa)
Sps_02823PFAM: Aminotransferase class-III; 'TIGRFAM: 4-aminobutyrate aminotransferase, prokaryotic type'; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (426 aa)
ilvEBranched chain amino acid aminotransferase apoenzyme; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (307 aa)
Sps_03227PFAM: Aminotransferase class IV; 'TIGRFAM: branched-chain amino acid aminotransferase, group II'. (362 aa)
Sps_04461PFAM: Coenzyme A transferase; 'TIGRFAM: 3-oxoacid CoA-transferase, A subunit'. (149 aa)
Sps_04462PFAM: Coenzyme A transferase; 'TIGRFAM: 3-oxoacid CoA-transferase, B subunit'. (220 aa)
Sps_04622'PFAM: Dehydrogenase E1 component; Transketolase, C-terminal domain; Transketolase, pyrimidine binding domain'. (747 aa)
Sps_05377Dihydrolipoamide dehydrogenase; 'PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain'; TIGRFAM: dihydrolipoamide dehydrogenase. (476 aa)
Your Current Organism:
Shewanella psychrophila
NCBI taxonomy Id: 225848
Other names: CGMCC 1.6159, JCM 13876, S. psychrophila, Shewanella psychrophila Xiao et al. 2007 emend. Thorell et al. 2019, Shewanella sp. WP2, strain WP2
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.