dsdA protein (Enterobacter lignolyticus) - STRING 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.

Knowledge-based Evidence

from curated databases

textmining

Assay-based Predictions

experimentally determined

co-expression

Genomic Predictions

gene neighborhood

gene co-occurrence

gene fusions

Your Input:

Neighborhood

Gene fusion

Co-occurrence

Co-expression

Experiments

Databases

Textmining

[Homology]

Score

dsdA

TIGRFAM: D-serine ammonia-lyase; KEGG: enc:ECL_00023 D-serine deaminase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. (434 aa)

Predicted Functional Partners:

ADO46302.1

0.918

ADO46863.1

0.914

ADO47194.1

0.914

ADO48234.1

0.914

ADO46858.1

0.910

ilvA

0.910

ADO47158.1

0.900

ghrB

0.800

ADO48432.1

0.800

ADO48486.1

0.800

Your Current Organism:

Enterobacter lignolyticus

NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1

Export your current network:

... as a bitmap image:

download

file format is 'PNG': portable network graphic

... as a high-resolution bitmap:

download

same PNG format, but at higher resolution

... as a vector graphic:

download

SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc.

... as short tabular text output:

download

TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)

... as tabular text output:

download

TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)

... as an XML summary:

download

structured XML interaction data, according to the 'PSI-MI' data standard

... protein node degrees:

download

node degree of proteins in your network (given the current score cut-off)

... network coordinates:

download

a flat-file format describing the coordinates and colors of nodes in the network

... protein sequences:

download

MFA: multi-fasta format - containing the aminoacid sequences in the network

... protein annotations:

download

a tab-delimited file describing the names, domains and descriptions of proteins in your network

... functional annotations:

download

a tab-delimited file containing all known functional terms of proteins in your network

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ADO46302.1	dsdA	Entcl_0023	Entcl_0022	Gluconate transporter; KEGG: sed:SeD_A4189 permease DsdX; TIGRFAM: gluconate transporter; PFAM: Gluconate transporter.	TIGRFAM: D-serine ammonia-lyase; KEGG: enc:ECL_00023 D-serine deaminase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit.	0.918
ADO46858.1	ADO46863.1	Entcl_0581	Entcl_0586	Pyridoxal-5'-phosphate-dependent protein beta subunit; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	0.936
ADO46858.1	ADO47158.1	Entcl_0581	Entcl_0886	Pyridoxal-5'-phosphate-dependent protein beta subunit; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	Aspartate racemase; KEGG: cro:ROD_28841 putative Asp/Glu/hydantoin racemase; TIGRFAM: aspartate racemase; PFAM: Asp/Glu/hydantoin racemase; Belongs to the aspartate/glutamate racemases family.	0.900
ADO46858.1	ADO47194.1	Entcl_0581	Entcl_0922	Pyridoxal-5'-phosphate-dependent protein beta subunit; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_3250 L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	0.911
ADO46858.1	ADO48234.1	Entcl_0581	Entcl_1979	Pyridoxal-5'-phosphate-dependent protein beta subunit; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_2383 L-serine ammonia-lyase; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	0.917
ADO46858.1	ADO48432.1	Entcl_0581	Entcl_2178	Pyridoxal-5'-phosphate-dependent protein beta subunit; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	TIGRFAM: lactoylglutathione lyase; KEGG: gloA; lactoylglutathione lyase; PFAM: Glyoxalase/bleomycin resistance protein/dioxygenase.	0.807
ADO46858.1	ADO48486.1	Entcl_0581	Entcl_2233	Pyridoxal-5'-phosphate-dependent protein beta subunit; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	PFAM: Aldehyde Dehydrogenase; KEGG: kpu:KP1_2509 aldehyde dehydrogenase A; Belongs to the aldehyde dehydrogenase family.	0.818
ADO46858.1	dsdA	Entcl_0581	Entcl_0022	Pyridoxal-5'-phosphate-dependent protein beta subunit; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	TIGRFAM: D-serine ammonia-lyase; KEGG: enc:ECL_00023 D-serine deaminase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit.	0.910
ADO46858.1	ghrB	Entcl_0581	Entcl_0187	Pyridoxal-5'-phosphate-dependent protein beta subunit; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily.	0.807
ADO46858.1	ilvA	Entcl_0581	Entcl_4265	Pyridoxal-5'-phosphate-dependent protein beta subunit; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	Threonine dehydratase, biosynthetic; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	0.916
ADO46863.1	ADO46858.1	Entcl_0586	Entcl_0581	TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	Pyridoxal-5'-phosphate-dependent protein beta subunit; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	0.936
ADO46863.1	ADO47158.1	Entcl_0586	Entcl_0886	TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	Aspartate racemase; KEGG: cro:ROD_28841 putative Asp/Glu/hydantoin racemase; TIGRFAM: aspartate racemase; PFAM: Asp/Glu/hydantoin racemase; Belongs to the aspartate/glutamate racemases family.	0.900
ADO46863.1	ADO47194.1	Entcl_0586	Entcl_0922	TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_3250 L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	0.901
ADO46863.1	ADO48234.1	Entcl_0586	Entcl_1979	TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_2383 L-serine ammonia-lyase; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	0.901
ADO46863.1	ADO48432.1	Entcl_0586	Entcl_2178	TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	TIGRFAM: lactoylglutathione lyase; KEGG: gloA; lactoylglutathione lyase; PFAM: Glyoxalase/bleomycin resistance protein/dioxygenase.	0.800
ADO46863.1	ADO48486.1	Entcl_0586	Entcl_2233	TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	PFAM: Aldehyde Dehydrogenase; KEGG: kpu:KP1_2509 aldehyde dehydrogenase A; Belongs to the aldehyde dehydrogenase family.	0.800
ADO46863.1	dsdA	Entcl_0586	Entcl_0022	TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	TIGRFAM: D-serine ammonia-lyase; KEGG: enc:ECL_00023 D-serine deaminase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit.	0.914
ADO46863.1	ghrB	Entcl_0586	Entcl_0187	TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily.	0.807
ADO46863.1	ilvA	Entcl_0586	Entcl_4265	TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family.	Threonine dehydratase, biosynthetic; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	0.911
ADO47158.1	ADO46858.1	Entcl_0886	Entcl_0581	Aspartate racemase; KEGG: cro:ROD_28841 putative Asp/Glu/hydantoin racemase; TIGRFAM: aspartate racemase; PFAM: Asp/Glu/hydantoin racemase; Belongs to the aspartate/glutamate racemases family.	Pyridoxal-5'-phosphate-dependent protein beta subunit; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.	0.900

page 1 of 5

Server load: low (26%) [HD]

Permalink

Network

Neighborhood

Experiments

Co-occurrence

Databases

Co-expression

Textmining

Fusion

© STRING Consortium 2026

Credits

Access

Info

About