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caiA caiA fixB fixB fixC fixC ilvI ilvI lpd lpd fadE fadE paoB paoB rclA rclA betA betA mhpA mhpA gcl gcl ahpF ahpF ybeX ybeX ubiF ubiF phr phr sdhA sdhA poxB poxB hcr hcr trxB trxB wrbA wrbA putA putA solA solA ndh ndh bluF bluF cvrA cvrA paaE paaE ydiJ ydiJ ydiO ydiO ydiR ydiR ydiS ydiS yeaX yeaX yoaE yoaE glf glf yegH yegH dld dld dusC dusC mqo mqo glpA glpA mnmC mnmC hcaD hcaD hmp hmp nadB nadB lhgO lhgO norW norW cysJ cysJ ygcQ ygcQ xdhB xdhB ygfM ygfM ubiI ubiI ubiH ubiH glcD glcD mdaB mdaB yqjH yqjH fadH fadH dusB dusB nirB nirB glpD glpD gor gor ilvB ilvB cbrA cbrA mnmG mnmG fpr fpr metF metF sthA sthA murB murB dusA dusA frdA frdA ytfL ytfL yfjD yfjD ygcU ygcU glcE glcE
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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caiACrotonobetaine reductase subunit II, FAD-binding; Catalyzes the reduction of crotonobetainyl-CoA to gamma- butyrobetainyl-CoA. The electron donor could be the FixA/FixB complex. (380 aa)
fixBProtein FixB; Required for anaerobic carnitine reduction. May bring reductant to CaiA; Belongs to the ETF alpha-subunit/FixB family. (313 aa)
fixCPutative oxidoreductase; Could be part of an electron transfer system required for anaerobic carnitine reduction; Belongs to the ETF-QO/FixC family. (428 aa)
ilvIAcetolactate synthase III, valine sensitive, large subunit. (574 aa)
lpdDihydrolipoyl dehydrogenase; Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. (474 aa)
fadEAcyl coenzyme A dehydrogenase; Catalyzes the dehydrogenation of acyl-coenzymes A (acyl-CoAs) to 2-enoyl-CoAs, the first step of the beta-oxidation cycle of fatty acid degradation. Is required for E.coli to utilize dodecanoate or oleate as the sole carbon and energy source for growth. (814 aa)
paoBPaoABC aldehyde oxidoreductase, FAD-containing subunit; Oxidizes aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. It might play a role in the detoxification of aldehydes to avoid cell damage. (318 aa)
rclAReactive chlorine stress species (RCS) resistance protein; Probably involved in reactive chlorine species (RCS) stress resistance. (441 aa)
betACholine dehydrogenase, a flavoprotein; Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. Belongs to the GMC oxidoreductase family. (556 aa)
mhpA3-(3-hydroxyphenyl)propionate hydroxylase; Catalyzes the insertion of one atom of molecular oxygen into position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP) and hydroxycinnamic acid (3HCI). (554 aa)
gclGlyoxylate carboligase; Catalyzes the condensation of two molecules of glyoxylate to give 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). (593 aa)
ahpFAlkyl hydroperoxide reductase, F52a subunit, FAD/NAD(P)-binding; Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. (521 aa)
ybeXPutative ion transport; Plays a role in the transport of magnesium and cobalt ions. (292 aa)
ubiF2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol oxygenase; Catalyzes the hydroxylation of 2-octaprenyl-3-methyl-6- methoxy-1,4-benzoquinol during ubiquinone biosynthesis. (391 aa)
phrDeoxyribodipyrimidine photolyase, FAD-binding; Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. (472 aa)
sdhASuccinate dehydrogenase, flavoprotein subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. (588 aa)
poxBPyruvate dehydrogenase, thiamine triphosphate-binding, FAD-binding; Pyruvate oxidase; Protein involved in carbohydrate catabolic process and pyruvate catabolic process; Belongs to the TPP enzyme family. (572 aa)
hcrHCP oxidoreductase, NADH-dependent; NADH oxidoreductase acting in concert with HCP. (322 aa)
trxBThioredoxin reductase, FAD/NAD(P)-binding; Thioredoxin reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. (321 aa)
wrbANAD(P)H:quinone oxidoreductase; It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide. It prefers NADH over NADPH. (198 aa)
putADelta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon; In the C-terminal section; belongs to the aldehyde dehydrogenase family. (1320 aa)
solAN-methyltryptophan oxidase, FAD-binding; Catalyzes the oxidative demethylation of N-methyl-L- tryptophan. Can also use other N-methyl amino acids, including sarcosine, which, however, is a poor substrate. (372 aa)
ndhRespiratory NADH dehydrogenase 2/cupric reductase; Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Does not couple the redox reaction to proton translocation. (434 aa)
bluFAnti-repressor for YcgE, blue light-responsive; Binds to and releases the BluR repressor from its bound DNA target in a blue light-dependent (470 nm) fashion. A shift to low temperature also triggers a BluF-mediated relief of repression by BluR, suggesting BluF may serve as a thermometer. Blue light may act to increase the affinity of BluF for BluR, allowing it to be released from its operator. The protein has a reversible photocycle, and undergoes structural changes, probably in the EAL domain, in response to light. (403 aa)
cvrAPutative cation/proton antiporter; K(+)/H(+) antiporter that extrudes potassium in exchange for external protons and maintains the internal concentration of potassium under toxic levels (By similarity). Participates in control of cell volume in low-osmolarity conditions; Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. NhaP2 subfamily. (578 aa)
paaERing 1,2-phenylacetyl-CoA epoxidase, NAD(P)H oxidoreductase component; Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA- CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit E is a reductase with a preference for NADPH and FAD, capable of reducing cytochrome c. (356 aa)
ydiJPutative FAD-linked oxidoreductase; Putative oxidase. (1018 aa)
ydiOPutative acyl-CoA dehydrogenase; Putative oxidoreductase; Belongs to the acyl-CoA dehydrogenase family. (383 aa)
ydiRPutative electron transfer flavoprotein, FAD-binding subunit; May play a role in a redox process; Belongs to the ETF alpha-subunit/FixB family. (312 aa)
ydiSPutative oxidoreductase; Probably accepts electrons from YdiQ/YdiR and reduces a quinone; Belongs to the ETF-QO/FixC family. (429 aa)
yeaXPutative YeaWX dioxygenase beta subunit, reductase component; Converts carnitine to trimethylamine and malic semialdehyde. Can also use gamma-butyrobetaine, choline and betaine as substrates. (321 aa)
yoaEPutative transport protein. (518 aa)
glfUDP-galactopyranose mutase, FAD/NAD(P)-binding; Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF); Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase family. (367 aa)
yegHInner membrane protein; Putative transport protein. (527 aa)
dldD-lactate dehydrogenase, FAD-binding, NADH independent; Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane. (571 aa)
dusCtRNA-dihydrouridine synthase C; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. DusC specifically modifies U16 in tRNAs. (315 aa)
mqoMalate dehydrogenase, FAD/NAD(P)-binding domain; Protein involved in tricarboxylic acid cycle. (548 aa)
glpAAnaerobic sn-glycerol-3-phosphate dehydrogenase, large FAD/NAD(P)-binding subunit; Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor. (542 aa)
mnmCtRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC; Catalyzes the last two steps in the biosynthesis of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34; In the N-terminal section; belongs to the methyltransferase superfamily. tRNA (mnm(5)s(2)U34)-methyltransferase family. (668 aa)
hcaDPhenylpropionate dioxygenase, ferredoxin reductase subunit; Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively; Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family. (400 aa)
hmpFused nitric oxide dioxygenase/dihydropteridine reductase 2; Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. Various electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if th [...] (396 aa)
nadBQuinolinate synthase, L-aspartate oxidase (B protein) subunit; Catalyzes the oxidation of L-aspartate to iminoaspartate. (540 aa)
lhgOL-2-hydroxyglutarate oxidase; Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG) to alpha-ketoglutarate and couples to the respiratory chain by feeding electrons from the reaction into the membrane quinone pool. Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. (422 aa)
norWNADH:flavorubredoxin oxidoreductase; One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase; Belongs to the FAD-dependent oxidoreductase family. (377 aa)
cysJSulfite reductase, alpha subunit, flavoprotein; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component; In the N-terminal section; belongs to the flavodoxin family. (599 aa)
ygcQPutative flavoprotein; May play a role in a redox process; Belongs to the ETF alpha-subunit/FixB family. (286 aa)
xdhBXanthine dehydrogenase, FAD-binding subunit; Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism). (292 aa)
ygfMPutative oxidoreductase. (259 aa)
ubiI2-octaprenylphenol hydroxylase, FAD-dependent; FAD-dependent monooxygenase required for the aerobic hydroxylation of 2-octaprenylphenol to 2-octaprenyl-6-hydroxy-phenol, the first hydroxylation step in coenzyme Q (ubiquinone) biosynthesis. (400 aa)
ubiH2-octaprenyl-6-methoxyphenol hydroxylase, FAD/NAD(P)-binding; Is likely an oxygenase that introduces the hydroxyl group at carbon four of 2-octaprenyl-6-methoxyphenol resulting in the formation of 2-octaprenyl-6-methoxy-1,4-benzoquinol. (392 aa)
glcDGlycolate oxidase subunit, FAD-linked; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is required for E.coli to grow on glycolate as a sole source of carbon. Is also able to oxidize D-lactate ((R)-lactate) with a similar rate. Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown ; Belongs to the FAD-binding oxidoreductase/transferase type 4 family. (499 aa)
mdaBNADPH quinone reductase; NADPH-specific quinone reductase. Is most active with quinone derivatives and ferricyanide as electron acceptors. Can use menadione, 1,4-naphthoquinone and 1,4-benzoquinone; Belongs to the oxidoreductase MdaB family. (193 aa)
yqjHPutative siderophore interacting protein; Plays a role in iron homeostasis under excess nickel conditions; Belongs to the SIP oxidoreductase family. (254 aa)
fadH2,4-dienoyl-CoA reductase, NADH and FMN-linked; Functions as an auxiliary enzyme in the beta-oxidation of unsaturated fatty acids with double bonds at even carbon positions. Catalyzes the NADPH-dependent reduction of the C4-C5 double bond of the acyl chain of 2,4-dienoyl-CoA to yield 2-trans-enoyl-CoA. Acts on both isomers, 2-trans,4- cis- and 2-trans,4-trans-decadienoyl-CoA, with almost equal efficiency. Is not active with NADH instead of NADPH. Does not show cis->trans isomerase activity. (672 aa)
dusBtRNA-dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the Dus family. DusB subfamily. (321 aa)
nirBNitrite reductase, large subunit, NAD(P)H-binding; Nitrite reductase (NAD(P)H) subunit; Protein involved in anaerobic respiration; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (847 aa)
glpDSn-glycerol-3-phosphate dehydrogenase, aerobic, FAD/NAD(P)-binding; Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor. (501 aa)
gorGlutathione oxidoreductase; Maintains high levels of reduced glutathione in the cytosol; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (450 aa)
ilvBAcetolactate synthase I,valine-sensitive, large subunit. (562 aa)
cbrAColicin M resistance protein; FAD-binding protein, putative oxidoreductase; Belongs to the CbrA family. (354 aa)
mnmG5-methylaminomethyl-2-thiouridine modification at tRNA U34; NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34. (629 aa)
fprferredoxin-NADP reductase; Transports electrons between flavodoxin or ferredoxin and NADPH. Reduces flavodoxin 1, flavodoxin 2 and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner. Required for the activation of several enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide reductase and cobalamin-dependent methionine synthase. Belongs to the ferredoxin--NADP reductase type 1 family. (248 aa)
metF5,10-methylenetetrahydrofolate reductase; Methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine. (296 aa)
sthAPyridine nucleotide transhydrogenase, soluble; Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation. (466 aa)
murBUDP-N-acetylenolpyruvoylglucosamine reductase, FAD-binding; Cell wall formation; Belongs to the MurB family. (342 aa)
dusAtRNA-dihydrouridine synthase A; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs; Belongs to the Dus family. DusA subfamily. (345 aa)
frdAAnaerobic fumarate reductase catalytic and NAD/flavoprotein subunit; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (602 aa)
ytfLUPF0053 family inner membrane protein; Putative transport protein. (447 aa)
yfjDUPF0053 family inner membrane protein; Putative membrane protein. (428 aa)
ygcUPutative FAD-linked oxidoreductase; Belongs to the FAD-binding oxidoreductase/transferase type 4 family. (484 aa)
glcEGlycolate oxidase FAD binding subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is required for E.coli to grow on glycolate as a sole source of carbon. Is also able to oxidize D-lactate ((R)-lactate) with a similar rate. Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. (350 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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