STRINGSTRING
fadB fadB Sps_00769 Sps_00769 Sps_01408 Sps_01408 Sps_01409 Sps_01409 Sps_01629 Sps_01629 Sps_01630 Sps_01630 Sps_01631 Sps_01631 Sps_01632 Sps_01632 fadJ fadJ fabV fabV Sps_02046 Sps_02046 Sps_02086 Sps_02086 Sps_02087 Sps_02087 Sps_02088 Sps_02088 Sps_02664 Sps_02664 Sps_02823 Sps_02823 Sps_02824 Sps_02824 Sps_03044 Sps_03044 Sps_03047 Sps_03047 Sps_03073 Sps_03073 Sps_03074 Sps_03074 Sps_03075 Sps_03075 Sps_03076 Sps_03076 Sps_03126 Sps_03126 Sps_03127 Sps_03127 Sps_03221 Sps_03221 Sps_03564 Sps_03564 Sps_04082 Sps_04082 Sps_04460 Sps_04460 Sps_04461 Sps_04461 Sps_04462 Sps_04462 Sps_04949 Sps_04949
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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.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
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Your Input:
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_00769Alcohol dehydrogenase AdhE; PFAM: Aldehyde dehydrogenase family; Iron-containing alcohol dehydrogenase; acetaldehyde dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. (866 aa)
Sps_01408Acetolactate synthase, large subunit; 'PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain'; 'TIGRFAM: acetolactate synthase, large subunit, biosynthetic type'. (573 aa)
Sps_01409PFAM: Small subunit of acetolactate synthase; ACT domain; 'TIGRFAM: acetolactate synthase, small subunit'. (164 aa)
Sps_01629Succinate dehydrogenase subunit B; PFAM: 2Fe-2S iron-sulfur cluster binding domain; 4Fe-4S dicluster domain; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (235 aa)
Sps_01630Succinate dehydrogenase subunit A; PFAM: FAD binding domain; Fumarate reductase flavoprotein C-term; 'TIGRFAM: succinate dehydrogenase, flavoprotein subunit, E. coli/mitochondrial subgroup; succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial subgroup'; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (588 aa)
Sps_01631Succinate dehydrogenase subunit D; Membrane-anchoring subunit of succinate dehydrogenase (SDH). (115 aa)
Sps_01632PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit; 'TIGRFAM: succinate dehydrogenase, cytochrome b556 subunit'. (124 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)
fabVPutative paraquat-inducible protein B; Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon- carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP); Belongs to the TER reductase family. (400 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_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_02664PFAM: Aldehyde dehydrogenase family; Belongs to the aldehyde dehydrogenase family. (456 aa)
Sps_02823PFAM: Aminotransferase class-III; 'TIGRFAM: 4-aminobutyrate aminotransferase, prokaryotic type'; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (426 aa)
Sps_02824PFAM: Aldehyde dehydrogenase family; TIGRFAM: succinate-semialdehyde dehydrogenase; Belongs to the aldehyde dehydrogenase family. (494 aa)
Sps_03044poly(R)-hydroxyalkanoic acid synthase, class I; PFAM: Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; alpha/beta hydrolase fold; 'TIGRFAM: poly(R)-hydroxyalkanoic acid synthase, class I'. (590 aa)
Sps_03047PFAM: short chain dehydrogenase; TIGRFAM: acetoacetyl-CoA reductase; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (248 aa)
Sps_03073Succinate dehydrogenase subunit B; PFAM: 2Fe-2S iron-sulfur cluster binding domain; 4Fe-4S dicluster domain; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (247 aa)
Sps_03074Succinate dehydrogenase subunit A; PFAM: FAD binding domain; Fumarate reductase flavoprotein C-term; 'TIGRFAM: succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial subgroup'. (670 aa)
Sps_03075PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit. (242 aa)
Sps_03076PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit. (243 aa)
Sps_03126Acetolactate synthase, small subunit; PFAM: ACT domain. (75 aa)
Sps_03127Acetolactate synthase, large subunit; 'PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain'; 'TIGRFAM: acetolactate synthase, large subunit, biosynthetic type'. (579 aa)
Sps_03221poly(R)-hydroxyalkanoic acid synthase, class I; PFAM: Poly-beta-hydroxybutyrate polymerase (PhaC) N-terminus; alpha/beta hydrolase fold; 'TIGRFAM: poly(R)-hydroxyalkanoic acid synthase, class I'. (591 aa)
Sps_03564Formate acetyltransferase 1; PFAM: Glycine radical; Pyruvate formate lyase; TIGRFAM: formate acetyltransferase 1. (760 aa)
Sps_04082Sodium ion-translocating decarboxylase, beta subunit; Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation; Belongs to the GcdB/MmdB/OadB family. (376 aa)
Sps_04460PFAM: short chain dehydrogenase; TIGRFAM: 3-hydroxybutyrate dehydrogenase. (260 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_04949PFAM: FAD binding domain; Cytochrome c3; TIGRFAM: flavocytochrome c; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (595 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
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