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mhpA mhpA mhpB mhpB mhpC mhpC mhpD mhpD mhpF mhpF mhpE mhpE ybaZ ybaZ ltaE ltaE hcr hcr hcp hcp rutG rutG rutF rutF rutE rutE rutD rutD rutC rutC rutB rutB rutA rutA rutR rutR fnr fnr ogt ogt abgT abgT abgB abgB abgA abgA abgR abgR ydcO ydcO ydfG ydfG ydiH ydiH yeaQ yeaQ yoaG yoaG yeaR yeaR yeaW yeaW yeaX yeaX alkA alkA alkB alkB ada ada hcaE hcaE hcaF hcaF hcaC hcaC hcaB hcaB hcaD hcaD hmp hmp norR norR norV norV norW norW ygbA ygbA yhhM yhhM yhjY yhjY tag tag tdh tdh kbl kbl nsrR nsrR aidB aidB ytfE ytfE yjgZ yjgZ insG insG
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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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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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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)
mhpB2,3-dihydroxyphenylpropionate 1,2-dioxygenase; Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6- ketononatrienedioate, respectively; Belongs to the LigB/MhpB extradiol dioxygenase family. (314 aa)
mhpC2-hydroxy-6-ketonona-2,4-dienedioic acid hydrolase; Catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6- oxononadienedioate and 2-hydroxy-6-oxononatrienedioate, a dienol ring fission product of the bacterial meta-cleavage pathway for degradation of phenylpropionic acid. MhpC shows some selectivity for the carboxylate of the side chain; Belongs to the AB hydrolase superfamily. MhpC family. (288 aa)
mhpD2-keto-4-pentenoate hydratase; Catalyzes the conversion of 2-hydroxypentadienoic acid (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid. Belongs to the hydratase/decarboxylase family. MhpD subfamily. (269 aa)
mhpFacetaldehyde-CoA dehydrogenase II, NAD-binding; Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. (316 aa)
mhpE4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase, class I; Catalyzes the retro-aldol cleavage of 4-hydroxy-2- oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta- cleavage pathway for the degradation of 3-phenylpropanoate. Belongs to the 4-hydroxy-2-oxovalerate aldolase family. (337 aa)
ybaZExcision repair protein, alkyltransferase-like protein ATL; Involved in DNA damage recognition. Binds DNA containing O(6)-methylguanine and larger O(6)-alkylguanine adducts, and to double- stranded DNA that contains an AP (apurinic/apyrimidinic) site. Binds to the damaged base and flips the base out of the DNA duplex into an extrahelical conformation, which allows processing by repair proteins. Works in partnership with the nucleotide excision repair (NER) pathway to enhance the repair of the O(6)- alkylguanine adducts larger than the methyl adduct. Also prevents methyl-directed mismat [...] (129 aa)
ltaEL-allo-threonine aldolase, PLP-dependent; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. L-threo-phenylserine and L-erythro- phenylserine are also good substrates. (333 aa)
hcrHCP oxidoreductase, NADH-dependent; NADH oxidoreductase acting in concert with HCP. (322 aa)
hcpHybrid-cluster [4Fe-2S-2O] subunit of anaerobic terminal reductases; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. Is also able to reduce hydroxylamine analogs such as methylhydroxylamine and hydroxyquinone. Might have a role as a scavenger of potentially toxic by-products of nitrate metabolism. Belongs to the HCP family. (550 aa)
rutGPyrimidine permease; May function as a proton-driven pyrimidine uptake system. (442 aa)
rutFflavin:NADH reductase; Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway. In vitro, the flavin reductase Fre can substitute for the function of RutF, however, RutF is required for uracil utilization in vivo. (164 aa)
rutEPutative malonic semialdehyde reductase; May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. RutE is apparently supplemented by YdfG. Required in vivo, but not in vitro in pyrimidine nitrogen degradation; Belongs to the nitroreductase family. HadB/RutE subfamily. (196 aa)
rutDPutative reactive intermediate detoxifying aminoacrylate hydrolase; May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. (266 aa)
rutCPutative aminoacrylate deaminase, reactive intermediate detoxification; May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. (128 aa)
rutBUreidoacrylate amidohydrolase; In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2. (230 aa)
rutAPyrimidine oxygenase, FMN-dependent; Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. RutA subfamily. (382 aa)
rutRRut operon transcriptional repressor for; Master transcription regulator which represses the degradation of pyrimidines (rutABCDEFG) and purines (gcl operon) for maintenance of metabolic balance between pyrimidines and purines. It also regulates the synthesis of pyrimidine nucleotides and arginine from glutamine (carAB) and the supply of glutamate (gadABWX). (212 aa)
fnrOxygen-sensing anaerobic growth regulon transcriptional regulator FNR; Global transcription factor that controls the expression of over 100 target genes in response to anoxia. It facilitates the adaptation to anaerobic growth conditions by regulating the expression of gene products that are involved in anaerobic energy metabolism. When the terminal electron acceptor, O(2), is no longer available, it represses the synthesis of enzymes involved in aerobic respiration and increases the synthesis of enzymes required for anaerobic respiration. (250 aa)
ogtO-6-alkylguanine-DNA:cysteine-protein methyltransferase; Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. (171 aa)
abgTP-aminobenzoyl-glutamate transporter; Essential for aminobenzoyl-glutamate utilization. It catalyzes the concentration-dependent uptake of p-aminobenzoyl- glutamate (PABA-GLU) into the cell and allows accumulation of PABA-GLU to a concentration enabling AbgAB to catalyze cleavage into p- aminobenzoate and glutamate. It seems also to increase the sensitivity to low levels of aminobenzoyl-glutamate. May actually serve physiologically as a transporter for some other molecule, perhaps a dipeptide, and that it transports p-aminobenzoyl-glutamate as a secondary activity. The physiological ro [...] (508 aa)
abgBP-aminobenzoyl-glutamate hydrolase, B subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified. (481 aa)
abgAP-aminobenzoyl-glutamate hydrolase, A subunit; Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p- aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified; Belongs to the peptidase M20 family. (436 aa)
abgRPutative DNA-binding transcriptional regulator of abgABT operon; Could be the regulator of the abg operon; Belongs to the LysR transcriptional regulatory family. (302 aa)
ydcOBenE family inner membrane putative transporter; Putative membrane transport protein. (391 aa)
ydfGNADP-dependent 3-hydroxy acid dehydrogenase; NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L- allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate. Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimi [...] (248 aa)
ydiHUncharacterized protein. (62 aa)
yeaQUPF0410 family protein. (82 aa)
yoaGUncharacterized protein. (60 aa)
yeaRDUF1971 family protein, nitrate-inducible; Protein involved in xenobiotic metabolic process. (119 aa)
yeaWPutative YeaWX dioxygenase alpha subunit; Converts carnitine to trimethylamine and malic semialdehyde. Can also use gamma-butyrobetaine, choline and betaine as substrates. (374 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)
alkA3-methyl-adenine DNA glycosylase II; Hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions. (282 aa)
alkBOxidative demethylase of N1-methyladenine or N3-methylcytosine DNA lesions; Dioxygenase that repairs alkylated DNA and RNA containing 3- methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and single-stranded substrates. Requires molecular oxygen, alpha- ketoglutarate and iron. Provides extensive resistance to alkylating agents such as MMS and DMS (SN2 agents), but not t [...] (216 aa)
adaFused DNA-binding transcriptional dual regulator/O6-methylguanine-DNA methyltransferase; Involved in the adaptive response to alkylation damage in DNA caused by alkylating agents. Repairs O6-methylguanine (O6-MeG) and O4- methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme (Cys-321). Also specifically repairs the Sp diastereomer of DNA methylphosphotriester lesions by the same mechanism, although the methyl transfer occurs onto a different cysteine residue (Cys-38). Cannot demeth [...] (354 aa)
hcaE3-phenylpropionate dioxygenase, large (alpha) subunit; Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3- phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively. (453 aa)
hcaF3-phenylpropionate dioxygenase, small (beta) subunit; Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3- phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively. (172 aa)
hcaC3-phenylpropionate dioxygenase, ferredoxin 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. This protein seems to be a 2Fe-2S ferredoxin. (106 aa)
hcaB2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Converts 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol) into 3-(2,3- dihydroxylphenyl)propanoic acid (DHPP) and 2,3-dihydroxicinnamic acid (DHCI), respectively; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (270 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)
norRAnaerobic nitric oxide reductase DNA-binding transcriptional activator; Required for the expression of anaerobic nitric oxide (NO) reductase, acts as a transcriptional activator for at least the norVW operon. Activation also requires sigma-54. Not required for induction of the aerobic NO-detoxifying enzyme NO dioxygenase. Binds to the promoter region of norVW, to a consensus target sequence, GT-(N7)-AC, which is highly conserved among proteobacteria. (504 aa)
norVAnaerobic nitric oxide reductase flavorubredoxin; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the reductase at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family. (479 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)
ygbAUncharacterized protein. (117 aa)
yhhMDUF2500 family protein; Putative receptor. (119 aa)
yhjYAutotransporter beta-domain protein; Putative lipase; Protein involved in fatty acid oxidation. (232 aa)
tag3-methyl-adenine DNA glycosylase I, constitutive; Hydrolysis of the deoxyribose N-glycosidic bond to excise 3- methyladenine from the damaged DNA polymer formed by alkylation lesions. (187 aa)
tdhL-threonine 3-dehydrogenase, NAD(P)-binding; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate. To a lesser extent, also catalyzes the oxidation of D-allo-threonine and L-threonine amide, but not that of D-threonine and L-allothreonine. Cannot utilize NADP(+) instead of NAD(+). Belongs to the zinc-containing alcohol dehydrogenase family. (341 aa)
kblGlycine C-acetyltransferase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. (398 aa)
nsrRNitric oxide-sensitive repressor for NO regulon; Nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress, such as ytfE, hmpA and ygbA. May require iron for activity. Does not regulates its own transcription. (141 aa)
aidBDNA alkylation damage repair protein; Part of the adaptive DNA-repair response to alkylating agents. Could prevent alkylation damage by protecting DNA and destroying alkylating agents that have yet to reach their DNA target. Binds to double-stranded DNA with a preference for a DNA region that includes its own promoter. Shows weak isovaleryl-CoA dehydrogenase activity in vitro. (541 aa)
ytfEIron-sulfur cluster repair protein RIC; Di-iron-containing protein involved in the repair of iron- sulfur clusters damaged by oxidative and nitrosative stress conditions. (220 aa)
yjgZUncharacterized protein YjgZ; Pseudogene fragment. (109 aa)
insGIS4 transposase; Involved in the transposition of the insertion sequence IS4. (442 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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