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scpA scpA parC parC parE parE folB folB uxaC uxaC truB truB glmM glmM kdsD kdsD nanE nanE fkpA fkpA slyD slyD ppiA ppiA rpe rpe xylA xylA sgbU sgbU sgbE sgbE gpmM gpmM hldD hldD gyrB gyrB rbsD rbsD ppiC ppiC wecB wecB dapF dapF fadB fadB yihS yihS rhaM rhaM rhaA rhaA tpiA tpiA murI murI rluF rluF pgi pgi alr alr alsE alsE rpiB rpiB epmB epmB nnr nnr ulaE ulaE ulaF ulaF fklB fklB sgcE sgcE nanM nanM deoB deoB ytjC ytjC frlC frlC rpiA rpiA idi idi kduI kduI ygeA ygeA fucU fucU fucI fucI truC truC truD truD ygbM ygbM srlQ srlQ tyrA tyrA pheA pheA rluD rluD fadJ fadJ truA truA folX folX menF menF gyrA gyrA rsuA rsuA wcaG wcaG cpsG cpsG rfbC rfbC glf glf hisA hisA yeaD yeaD topB topB manA manA fumA fumA lsrG lsrG yddE yddE pptA pptA paaG paaG ycjG ycjG ycjU ycjU ycjR ycjR topA topA rluB rluB trpC trpC dadX dadX rluE rluE rluC rluC fabA fabA ybhH ybhH galE galE galM galM gpmA gpmA pgm pgm entC entC ppiB ppiB purE purE hyi hyi ppiD ppiD tig tig gmhA gmhA hemL hemL araA araA araD araD rluA rluA surA surA fkpB fkpB
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scpAmethylmalonyl-CoA mutase; Catalyzes the interconversion of succinyl-CoA and methylmalonyl-CoA. Could be part of a pathway that converts succinate to propionate. (714 aa)
parCDNA topoisomerase IV, subunit A; Topoisomerase IV is essential for chromosome segregation; it is the principal protein responsible for decatenating newly replicated chromosomes. It relaxes supercoiled DNA. MukB stimulates the relaxation activity of topoisomerase IV and also has a modest effect on decatenation. Belongs to the type II topoisomerase GyrA/ParC subunit family. ParC type 1 subfamily. (752 aa)
parEDNA topoisomerase IV, subunit B; Topoisomerase IV is essential for chromosome segregation; it is the principal protein responsible for decatenating newly replicated chromosomes. It relaxes supercoiled DNA. MukB stimulates the relaxation activity of topoisomerase IV and also has a modest effect on decatenation. Belongs to the type II topoisomerase family. ParE type 1 subfamily. (630 aa)
folBDihydroneopterin aldolase and dihydroneopterin triphosphate 2'-epimerase; Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6- hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin to dihydromonapterin at appreciable velocity; Belongs to the DHNA family. (122 aa)
uxaCUronate isomerase; Protein involved in carbohydrate catabolic process; Belongs to the metallo-dependent hydrolases superfamily. Uronate isomerase family. (470 aa)
truBtRNA pseudouridine synthase B; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily. (314 aa)
glmMPhosphoglucosamine mutase; Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. Can also catalyze the formation of glucose-6-P from glucose-1-P, although at a 1400-fold lower rate. (445 aa)
kdsDD-arabinose 5-phosphate isomerase; Involved in the biosynthesis of 3-deoxy-D-manno-octulosonate (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs). KdsD is not essential in the KDO biosynthesis and can be substituted by GutQ. Catalyzes the reversible aldol-ketol isomerization between D- ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P). (328 aa)
nanEPutative N-acetylmannosamine-6-P epimerase; Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N- acetylglucosamine-6-phosphate (GlcNAc-6-P). (229 aa)
fkpAFKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (270 aa)
slyDFKBP-type peptidyl prolyl cis-trans isomerase (rotamase); Folding helper with both chaperone and peptidyl-prolyl cis- trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa- Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in [...] (196 aa)
ppiAPeptidyl-prolyl cis-trans isomerase A (rotamase A); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (190 aa)
rpeD-ribulose-5-phosphate 3-epimerase; Catalyzes the reversible epimerization of D-ribulose 5- phosphate to D-xylulose 5-phosphate. (225 aa)
xylAD-xylose isomerase; Protein involved in carbohydrate catabolic process and glucose metabolic process; Belongs to the xylose isomerase family. (440 aa)
sgbUPutative L-xylulose 5-phosphate 3-epimerase; Catalyzes the isomerization of L-xylulose-5-phosphate to L- ribulose-5-phosphate (Potential). May be involved in the utilization of 2,3-diketo-L-gulonate; Belongs to the L-ribulose-5-phosphate 3-epimerase family. (286 aa)
sgbEL-ribulose-5-phosphate 4-epimerase; Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-carbon bond cleavage analogous to a class II aldolase reaction). May be involved in the utilization of 2,3-diketo-L-gulonate. (231 aa)
gpmMPhosphoglycero mutase III, cofactor-independent; Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA). (514 aa)
hldDADP-L-glycero-D-mannoheptose-6-epimerase, NAD(P)-binding; Catalyzes the interconversion between ADP-D-glycero-beta-D- manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose; Belongs to the NAD(P)-dependent epimerase/dehydratase family. HldD subfamily. (310 aa)
gyrBDNA gyrase, subunit B; DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at compa [...] (804 aa)
rbsDD-ribose pyranase; Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. It also catalyzes the conversion between beta- allofuranose and beta-allopyranose; Belongs to the RbsD / FucU family. RbsD subfamily. (139 aa)
ppiCPeptidyl-prolyl cis-trans isomerase C (rotamase C); PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates; Belongs to the PpiC/parvulin rotamase family. (93 aa)
wecBUDP-N-acetyl glucosamine-2-epimerase; Catalyzes the reversible epimerization at C-2 of UDP-N- acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP- N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues. Also involved in bacteriophage N4 adsorption. (376 aa)
dapFDiaminopimelate epimerase; Involved in the succinylase branch of the L-lysine biosynthesis and in the biosynthesis of the pentapeptide incorporated in the peptidoglycan moiety. Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso- diaminoheptanedioate (meso-DAP). (274 aa)
fadBEnoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (729 aa)
yihSSulphoquinovose isomerase; Catalyzes the isomerization of sulfoquinovose (SQ) to 6- deoxy-6-sulfo-D-fructose (SF). In vitro, can also catalyze the interconversion of mannose, fructose and glucose, or lyxose and xylulose, but has extremely low activity with glucose. (413 aa)
rhaML-rhamnose mutarotase; Involved in the anomeric conversion of L-rhamnose. (104 aa)
rhaAL-rhamnose isomerase; Protein involved in carbohydrate catabolic process. (419 aa)
tpiATriosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (255 aa)
murIGlutamate racemase; Provides the (R)-glutamate required for cell wall biosynthesis. Belongs to the aspartate/glutamate racemases family. (285 aa)
rluF23S rRNA pseudouridine(2604) synthase; Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-2604 in 23S ribosomal RNA and from uracil-35 in the anticodon of tRNA(Tyr). Can, to a small extent, also react with uracil-2605. Belongs to the pseudouridine synthase RsuA family. (290 aa)
pgiGlucosephosphate isomerase; Protein involved in glycolysis and gluconeogenesis; Belongs to the GPI family. (549 aa)
alrAlanine racemase, biosynthetic, PLP-binding; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. (359 aa)
alsEAllulose-6-phosphate 3-epimerase; Catalyzes the reversible epimerization of D-allulose 6- phosphate to D-fructose 6-phosphate. Can also catalyze with lower efficiency the reversible epimerization of D-ribulose 5-phosphate to D- xylulose 5-phosphate. (231 aa)
rpiBRibose 5-phosphate isomerase B/allose 6-phosphate isomerase; Catalyzes the interconversion of ribulose-5-P and ribose-5-P. It probably also has activity on D-allose 6-phosphate. (149 aa)
epmBEF-P-Lys34 lysylation protein; With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3- aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine). Cannot use (S)-ornithine or (R)-alpha-lysine as a substrate; Belongs to the radical SAM superfamily. KamA family. (342 aa)
nnrBifunctional NAD(P)H-hydrate repair enzyme; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. In the N-terminal section; belongs to the NnrE/AIBP family. (515 aa)
ulaEL-xylulose 5-phosphate 3-epimerase; Catalyzes the isomerization of L-xylulose-5-phosphate to L- ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization; Belongs to the L-ribulose-5-phosphate 3-epimerase family. (284 aa)
ulaFL-ribulose 5-phosphate 4-epimerase; Catalyzes the isomerization of L-ribulose 5-phosphate to D- xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization; Belongs to the aldolase class II family. AraD/FucA subfamily. (228 aa)
fklBFKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (206 aa)
sgcEPutative epimerase; Probable pentose-5-phosphate 3-epimerase. (210 aa)
nanMN-acetylneuraminic acid mutarotase; Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta- anomer, accelerating the equilibrium between the alpha- and beta- anomers. Probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses; Belongs to the NanM family. (368 aa)
deoBPhosphopentomutase; Phosphotransfer between the C1 and C5 carbon atoms of pentose; Belongs to the phosphopentomutase family. (407 aa)
ytjCPhosphatase; Phosphoglyceromutase 2; Protein involved in glycolysis and gluconeogenesis; Belongs to the phosphoglycerate mutase family. GpmB subfamily. (215 aa)
frlCFructoselysine 3-epimerase; Catalyzes the reversible interconversion of fructoselysine with its C-3 epimer, psicoselysine. Allows E.coli to utilize psicoselysine for growth. Does not act on psicose or fructoselysine 6- phosphate. (276 aa)
rpiARibose 5-phosphate isomerase, constitutive; Involved in the first step of the non-oxidative branch of the pentose phosphate pathway. It catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. Can also act on D-ribose-5- diphosphate and D-ribose-5-triphosphate as substrate. (219 aa)
idiIsopentenyl diphosphate isomerase; Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). (182 aa)
kduIHexuronate isomerase; Catalyzes the isomerization of 5-dehydro-4-deoxy-D- glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate (By similarity). Plays a role in the catabolism of hexuronates under osmotic stress conditions, likely substituting for the regular hexuronate degrading enzyme UxaC whose expression is repressed in these conditions ; Belongs to the KduI family. (278 aa)
ygeAAsp/Glu_racemase family protein; Amino-acid racemase able to utilize a broad range of substrates. Highest activity is observed with L-homoserine and D- homoserine. Has tenfold lower activity against L-methionine, L-leucine, L-valine and L-histidine. Has low activity with L-norvaline, L- asparagine, D-methionine, L-aminobutyric acid, L-isoleucine, L-serine, L-norleucine, L-alanine, L-glutamine, LL-diaminopimelic acid and L- phenylalanine. Has no activity against ten L-amino acids (Thr, Glu, Asp, Arg, Lys, Tyr, Trp, Orn, Cit and Aad). D-amino acids might be used as components of peptidog [...] (230 aa)
fucUL-fucose mutarotase; Involved in the anomeric conversion of L-fucose. Catalyzes also the interconversion of beta-pyran and beta-furan forms of D- ribose; Belongs to the RbsD / FucU family. FucU mutarotase subfamily. (140 aa)
fucIL-fucose isomerase; Converts the aldose L-fucose into the corresponding ketose L- fuculose. Is also able to convert D-arabinose into D-ribulose, but this isomerase has a higher affinity for fucose and fuculose than for arabinose and ribulose, respectively. (591 aa)
truCtRNA(Ile1,Asp) pseudouridine(65) synthase; Responsible for synthesis of pseudouridine from uracil-65 in transfer RNAs; Belongs to the pseudouridine synthase RluA family. (260 aa)
truDtRNA(Glu) pseudouridine(13) synthase; Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. (349 aa)
ygbMPutative hydroxypyruvate isomerase; Catalyzes the isomerization of 2-oxo-tetronate to 3-oxo- tetronate. (258 aa)
srlQD-arabinose 5-phosphate isomerase; Catalyzes the reversible aldol-ketol isomerization between D- ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P). It appears that the physiological function of G-API may be to synthesize the regulatory molecule A5P, which in turn participates in the induction of the gut operon through an unknown mechanism. It is also able of sustaining the biosynthetic pathway of 3-deoxy-D-manno- octulosonate (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs); Belongs to the SIS family. GutQ/KpsF subfamily. (321 aa)
tyrAChorismate mutase-T and prephenate dehydrogenase; Protein involved in L-phenylalanine biosynthetic process and tyrosine biosynthetic process. (373 aa)
pheAChorismate mutase and prephenate dehydratase, P-protein; Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. (386 aa)
rluD23S rRNA pseudouridine(1911,1915,1917) synthase; Responsible for synthesis of pseudouridine from uracil at positions 1911, 1915 and 1917 in 23S ribosomal RNA. Isomerization occurs as a late step during the assembly of the large ribosomal subunit. (326 aa)
fadJenoyl-CoA hydratase/epimerase and isomerase/3-hydroxyacyl-CoA dehydrogenase; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (714 aa)
truAtRNA pseudouridine(38-40) synthase; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. (270 aa)
folXD-erythro-7,8-dihydroneopterin triphosphate 2'-epimerase and dihydroneopterin aldolase; Catalyzes the epimerization of carbon 2' of the side chain of 7,8-dihydroneopterin triphosphate (H2NTP) to form 7,8-dihydromonapterin triphosphate (H2MTP). Is required for tetrahydromonapterin biosynthesis, a major pterin in E.coli. (120 aa)
menFIsochorismate synthase 2; Catalyzes the conversion of chorismate to isochorismate. Can also catalyze the reverse reaction, but with a lower efficiency. (431 aa)
gyrADNA gyrase (type II topoisomerase), subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase IV (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of dsDNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than many other bac [...] (875 aa)
rsuA16S rRNA pseudouridine(516) synthase; Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA; Belongs to the pseudouridine synthase RsuA family. (231 aa)
wcaGGDP-L-fucose synthase; Catalyzes the two-step NADP-dependent conversion of GDP-4- dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction. Belongs to the NAD(P)-dependent epimerase/dehydratase family. Fucose synthase subfamily. (321 aa)
cpsGPhosphomannomutase; Involved in the biosynthesis of the capsular polysaccharide colanic acid; Belongs to the phosphohexose mutase family. (456 aa)
rfbCdTDP-4-deoxyrhamnose-3,5-epimerase; Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family. (185 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)
hisAN-(5'-phospho-L-ribosyl-formimino)-5-amino-1- (5'-phosphoribosyl)-4-imidazolecarboxamide isomerase; Protein involved in histidine biosynthetic process; Belongs to the HisA/HisF family. (245 aa)
yeaDD-hexose-6-phosphate epimerase-like protein; Belongs to the glucose-6-phosphate 1-epimerase family. (294 aa)
topBDNA topoisomerase III; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA su [...] (653 aa)
manAMannose-6-phosphate isomerase; Involved in the conversion of glucose to GDP-L-fucose, which can be converted to L-fucose, a capsular polysaccharide. (391 aa)
fumAFumarate hydratase (fumarase A), aerobic Class I; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate. (548 aa)
lsrGAutoinducer-2 (AI-2) degrading protein LsrG; Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the conversion of (4S)-4-hydroxy-5- phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5- phosphonooxypentane-2,4-dione (P-HPD). (96 aa)
yddEPhzC-PhzF family protein. (297 aa)
pptA4-oxalocrotonate tautomerase; Can use enol isomers of phenylpyruvate, 2-hydroxy-2,4- pentadienoate and (p-hydroxyphenyl)pyruvate as substrates. Belongs to the 4-oxalocrotonate tautomerase family. PptA subfamily. (77 aa)
paaG1,2-epoxyphenylacetyl-CoA isomerase, oxepin-CoA-forming; Catalyzes the reversible conversion of the epoxide to 2- oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA). (262 aa)
ycjGL-Ala-D/L-Glu epimerase; Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has a role in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of all the L-Ala-X dipeptides, except L-Ala-L-Arg, L-Ala- L-Lys and L-Ala-L-Pro. Is also active with L-Gly-L-Glu, L-Phe-L-Glu, and L-Ser-L-Glu, but not with L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L- Lys-L-Ala, or D-Ala-D-Ala; Belongs to the mandelate racemase/muconate lactonizing enzyme family. (321 aa)
ycjUBeta-phosphoglucomutase; Catalyzes the conversion of beta D-glucose 1-phosphate (G1P) to D-glucose 6-phosphate (G6P), forming beta-D-glucose 1,6- (bis)phosphate (beta-G16P) as an intermediate (Probable). Phosphatase activity with the reaction intermediate beta-G16P has been measured. In vitro interconverts beta D-glucose 1-phosphate, beta-D-allose 1-phosphate, beta-D-galactose 1-phosphate and beta-D-mannose 1-phosphate to their corresponding sugar 6-phosphate product. The beta-D-glucose 1-phosphate substrate may be furnished by YcjT (AC P77154), the apparent upstream enzyme in the put [...] (219 aa)
ycjRPutative TIM alpha/beta barrel enzyme; Catalyzes the epimerization at C4 of 3-dehydro-D-gulosides leading to 3-dehydro-D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. Cannot act on D- psicose, D-fructose, D-tagatose, D-sorbose, L-xylulose, or L-ribulose. Belongs to the hyi family. (262 aa)
topADNA topoisomerase I, omega subunit; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus re [...] (865 aa)
rluB23S rRNA pseudouridine(2605) synthase; Responsible for synthesis of pseudouridine from uracil-2605 in 23S ribosomal RNA. (291 aa)
trpCIndole-3-glycerolphosphate synthetase and N-(5-phosphoribosyl)anthranilate isomerase; Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain. (453 aa)
dadXAlanine racemase, catabolic, PLP-binding; Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. (356 aa)
rluE23S rRNA pseudouridine(2457) synthase; Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA; Belongs to the pseudouridine synthase RsuA family. (217 aa)
rluC23S rRNA pseudouridine(955,2504,2580) synthase; Responsible for synthesis of pseudouridine from uracil at positions 955, 2504 and 2580 in 23S ribosomal RNA. (319 aa)
fabABeta-hydroxydecanoyl thioester dehydrase; Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E- (2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. Is inactive in the dehydration of long chain unsaturated beta-hydroxyacyl-ACP. (172 aa)
ybhHPutative PrpF family isomerase; Belongs to the PrpF family. (350 aa)
galEUDP-galactose-4-epimerase; Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD. It is only active on UDP-galactose and UDP-glucose. (338 aa)
galMAldose 1-epimerase; Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose. (346 aa)
gpmAPhosphoglyceromutase 1; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate; Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily. (250 aa)
pgmPhosphoglucomutase; This enzyme participates in both the breakdown and synthesis of glucose; Belongs to the phosphohexose mutase family. (546 aa)
entCIsochorismate synthase 1; Involved in the biosynthesis of the siderophore enterobactin (macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine). Catalyzes the reversible conversion of chorismate to isochorismate. (391 aa)
ppiBPeptidyl-prolyl cis-trans isomerase B (rotamase B); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (164 aa)
purEN5-carboxyaminoimidazole ribonucleotide mutase; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR); Belongs to the AIR carboxylase family. Class I subfamily. (169 aa)
hyiHydroxypyruvate isomerase; Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). Does not catalyze the isomerization of D-fructose to D- glucose or that of D-xylulose to D-xylose. Also does not catalyze racemization of serine, alanine, glycerate or lactate. (258 aa)
ppiDPeriplasmic folding chaperone, has an inactive PPIase domain; PPIases accelerate the folding of proteins. Seems to be involved in the folding of outer membrane proteins. Its preference at the P1 position of the peptide substrate is Glu > Leu > Ala > His > Val > Phe > Ile > Gly > Lys > Thr. (623 aa)
tigPeptidyl-prolyl cis/trans isomerase (trigger factor); Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates. Binds to nascent polypeptide chains via ribosomal protein L23. Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity. Belongs to the FKBP-type PPIase family. Tig subfamily. (432 aa)
gmhAD-sedoheptulose 7-phosphate isomerase; Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate; Belongs to the SIS family. GmhA subfamily. (192 aa)
hemLGlutamate-1-semialdehyde aminotransferase (aminomutase). (426 aa)
araAL-arabinose isomerase; Catalyzes the conversion of L-arabinose to L-ribulose. (500 aa)
araDL-ribulose-5-phosphate 4-epimerase; Involved in the degradation of L-arabinose. Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D- xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon- carbon bond cleavage analogous to a class II aldolase reaction). (231 aa)
rluADual-specificity RNA pseudouridine synthase RluA; Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-746 in 23S ribosomal RNA and from uracil-32 in the anticodon stem and loop of transfer RNAs. (219 aa)
surAPeptidyl-prolyl cis-trans isomerase (PPIase); Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane- associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis. (428 aa)
fkpBFKBP-type peptidyl-prolyl cis-trans isomerase (rotamase); PPIases accelerate the folding of proteins. Substrate specificity investigated with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide' where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln. (149 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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