STRINGSTRING
ADO48326.1 ADO48326.1 ADO47148.1 ADO47148.1 ADO50029.1 ADO50029.1 proA proA ADO49058.1 ADO49058.1 ADO49026.1 ADO49026.1 ADO49013.1 ADO49013.1 astD astD ADO48677.1 ADO48677.1 ADO48674.1 ADO48674.1 patD patD ADO48543.1 ADO48543.1 ADO48486.1 ADO48486.1 ADO48003.1 ADO48003.1 ADO47966.1 ADO47966.1 ADO47578.1 ADO47578.1 ADO47523.1 ADO47523.1 ADO47030.1 ADO47030.1 ADO50038.1 ADO50038.1
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.
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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:
ADO48326.1PFAM: iron-containing alcohol dehydrogenase; Aldehyde Dehydrogenase; KEGG: enc:ECL_01635 bifunctional acetaldehyde-CoA/alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. (892 aa)
ADO47148.1KEGG: cko:CKO_04008 succinate-semialdehyde dehydrogenase I; TIGRFAM: succinic semialdehyde dehydrogenase; PFAM: Aldehyde Dehydrogenase; Belongs to the aldehyde dehydrogenase family. (482 aa)
ADO50029.1PFAM: Aldehyde Dehydrogenase; KEGG: cro:ROD_25491 putative aldehyde dehydrogenase. (534 aa)
proAGamma-glutamyl phosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family. (417 aa)
ADO49058.1KEGG: kva:Kvar_3367 succinic semialdehyde dehydrogenase; TIGRFAM: succinic semialdehyde dehydrogenase; PFAM: Aldehyde Dehydrogenase; Belongs to the aldehyde dehydrogenase family. (482 aa)
ADO49026.1PFAM: Aldehyde Dehydrogenase; KEGG: spe:Spro_2410 aldehyde dehydrogenase; Belongs to the aldehyde dehydrogenase family. (506 aa)
ADO49013.1Delta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source; Belongs to the aldehyde dehydrogenase family. In the N-terminal section; belongs to the proline dehydrogenase family. (1320 aa)
astDSuccinylglutamic semialdehyde dehydrogenase; Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. (492 aa)
ADO48677.1PFAM: Aldehyde Dehydrogenase; KEGG: eoj:ECO26_1989 phenylacetaldehyde dehydrogenase; Belongs to the aldehyde dehydrogenase family. (499 aa)
ADO48674.1Phenylacetic acid degradation protein paaN; KEGG: enc:ECL_02154 bifunctional aldehyde dehydrogenase/enoyl-CoA hydratase; TIGRFAM: phenylacetic acid degradation protein paaN; PFAM: MaoC domain protein dehydratase; Aldehyde Dehydrogenase. (681 aa)
patD1-pyrroline dehydrogenase; Catalyzes the oxidation 4-aminobutanal (gamma- aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA). This is the second step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate via 4- aminobutanal. Also functions as a 5-aminopentanal dehydrogenase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. (475 aa)
ADO48543.1PFAM: Aldehyde Dehydrogenase; KEGG: kpe:KPK_2744 putative succinate semialdehyde dehydrogenase. (461 aa)
ADO48486.1PFAM: Aldehyde Dehydrogenase; KEGG: kpu:KP1_2509 aldehyde dehydrogenase A; Belongs to the aldehyde dehydrogenase family. (479 aa)
ADO48003.1PFAM: Aldehyde Dehydrogenase; KEGG: cro:ROD_21371 propanediol utilization: CoA-dependent propionaldehyde dehydrogenase. (461 aa)
ADO47966.1PFAM: Aldehyde Dehydrogenase; KEGG: kpu:KP1_2002 gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Belongs to the aldehyde dehydrogenase family. (495 aa)
ADO47578.1PFAM: Aldehyde Dehydrogenase; KEGG: sea:SeAg_B2608 ethanolamine utilization protein EutE. (467 aa)
ADO47523.1KEGG: enc:ECL_03809 methylmalonate-semialdehyde dehydrogenase; TIGRFAM: methylmalonate-semialdehyde dehydrogenase; PFAM: Aldehyde Dehydrogenase. (501 aa)
ADO47030.1PFAM: Aldehyde Dehydrogenase; KEGG: reu:Reut_A1903 aldehyde dehydrogenase; Belongs to the aldehyde dehydrogenase family. (471 aa)
ADO50038.1KEGG: kpu:KP1_0741 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; TIGRFAM: 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; PFAM: Aldehyde Dehydrogenase; Belongs to the aldehyde dehydrogenase family. (488 aa)
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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