STRINGSTRING
serC serC AEE90473.1 AEE90473.1 AEE90497.1 AEE90497.1 AEE90533.1 AEE90533.1 AEE90634.1 AEE90634.1 pfp pfp cooF cooF cooS cooS acsD acsD acsC acsC pfkA pfkA serA serA ackA ackA pta pta fba fba fbp fbp AEE91886.1 AEE91886.1 mdh mdh eno eno pgm pgm glyA glyA AEE92267.1 AEE92267.1 AEE92268.1 AEE92268.1 porB porB porA porA AEE92324.1 AEE92324.1 porC porC pfp-2 pfp-2 fba-2 fba-2
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:
serCPhosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. (363 aa)
AEE90473.1KEGG: ols:Olsu_0672 tagatose-bisphosphate aldolase; PFAM: Ketose-bisphosphate aldolase, class-II. (277 aa)
AEE90497.1Cobalamin B12-binding domain protein; PFAM: Cobalamin (vitamin B12)-binding; Methionine synthase, cobalamin (vitamin B12)-binding module, cap; KEGG: toc:Toce_0790 cobalamin B12-binding domain protein. (212 aa)
AEE90533.1PFAM: Formylmethanofuran dehydrogenase, subunit E domain; KEGG: clj:CLJU_c38060 formylmethanofuran dehydrogenase subunit E. (176 aa)
AEE90634.1Phosphoglycerate dehydrogenase; KEGG: elm:ELI_0529 hypothetical protein; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain. (343 aa)
pfpDiphosphate--fructose-6-phosphate 1-phosphotransferase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. (394 aa)
cooFPFAM: 4Fe-4S binding domain; KEGG: toc:Toce_0799 iron-sulfur cluster-binding protein CooF. (139 aa)
cooSTIGRFAM: Carbon-monoxide dehydrogenase, catalytic subunit; KEGG: toc:Toce_0800 carbon-monoxide dehydrogenase, catalytic subunit; PFAM: Prismane. (633 aa)
acsDPFAM: CO dehydrogenase/acetyl-CoA synthase delta subunit, TIM barrel; KEGG: toc:Toce_0810 CO dehydrogenase/acetyl-CoA synthase delta subunit, TIM barrel. (312 aa)
acsCPFAM: CO dehydrogenase/acetyl-CoA synthase delta subunit, TIM barrel; Putative Fe-S cluster; KEGG: toc:Toce_0811 acetyl-CoA decarbonylase/synthase gamma subunit. (454 aa)
pfkA6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. (319 aa)
serATIGRFAM: D-3-phosphoglycerate dehydrogenase; KEGG: dau:Daud_0012 D-3-phosphoglycerate dehydrogenase; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain; Amino acid-binding ACT. (523 aa)
ackAAcetate kinase; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction; Belongs to the acetokinase family. (400 aa)
ptaTIGRFAM: Phosphate acetyltransferase; KEGG: toc:Toce_1047 phosphotransacetylase; PFAM: Phosphate acetyl/butaryl transferase. (328 aa)
fbaTIGRFAM: Fructose-1,6-bisphosphate aldolase, class 2; Ketose-bisphosphate aldolase, class-II; KEGG: toc:Toce_1810 fructose-bisphosphate aldolase; PFAM: Ketose-bisphosphate aldolase, class-II. (309 aa)
fbpProtein of unknown function DUF100; Catalyzes two subsequent steps in gluconeogenesis: the aldol condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3- phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the dephosphorylation of FBP to fructose-6-phosphate (F6P). (362 aa)
AEE91886.1Phosphoglycerate dehydrogenase; KEGG: tmt:Tmath_0226 glyoxylate reductase; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain. (310 aa)
mdhMalate dehydrogenase; KEGG: ckr:CKR_2460 hypothetical protein; PFAM: Malate/L-lactate dehydrogenase; Belongs to the LDH2/MDH2 oxidoreductase family. (372 aa)
enoEnolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family. (428 aa)
pgm2,3-bisphosphoglycerate-independent phosphoglycerate mutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. (511 aa)
glyAGlycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. (412 aa)
AEE92267.1TIGRFAM: Ketose-bisphosphate aldolase, class-II; KEGG: ate:Athe_1995 ketose-bisphosphate aldolase; PFAM: Ketose-bisphosphate aldolase, class-II. (279 aa)
AEE92268.1Phosphoglycerate dehydrogenase; KEGG: ate:Athe_1994 D-isomer specific 2-hydroxyacid dehydrogenase; PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain. (365 aa)
porBPyruvate synthase; KEGG: toc:Toce_2138 thiamine pyrophosphate protein domain protein TPP-binding protein; PFAM: Thiamine pyrophosphate enzyme, C-terminal TPP-binding. (315 aa)
porAKEGG: toc:Toce_2139 pyruvate ferredoxin oxidoreductase, alpha subunit; PFAM: Pyruvate flavodoxin/ferredoxin oxidoreductase, N-terminal. (393 aa)
AEE92324.1KEGG: toc:Toce_2140 pyruvate ferredoxin oxidoreductase, delta subunit; TIGRFAM: 2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate; PFAM: 4Fe-4S binding domain. (122 aa)
porCTIGRFAM: 2-oxoacid:acceptor oxidoreductase, gamma subunit, pyruvate/2-ketoisovalerate; KEGG: toc:Toce_2141 pyruvate ferredoxin oxidoreductase, gamma subunit; PFAM: Pyruvate/ketoisovalerate oxidoreductase, catalytic domain. (192 aa)
pfp-2Phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. (393 aa)
fba-2TIGRFAM: Ketose-bisphosphate aldolase, class-II; KEGG: toc:Toce_1875 ketose-bisphosphate aldolase; PFAM: Ketose-bisphosphate aldolase, class-II. (280 aa)
Your Current Organism:
Tepidanaerobacter acetatoxydans
NCBI taxonomy Id: 1209989
Other names: T. acetatoxydans Re1, Tepidanaerobacter acetatoxydans Re1, Tepidanaerobacter acetatoxydans str. Re1, Tepidanaerobacter acetatoxydans strain Re1, Tepidanaerobacter sp. Re1
Server load: low (20%) [HD]