STRINGSTRING
STM4431 STM4431 eutT eutT eutQ eutQ eutP eutP eutS eutS suhB suhB pdxJ pdxJ epd epd STM3083 STM3083 STM3136 STM3136 gatY gatY gatZ gatZ STM3261 STM3261 aroE aroE gph gph glpE glpE mtlD mtlD lldD lldD STM3781 STM3781 eutC eutC eutL eutL eutK eutK eutR eutR pdxK pdxK pdxB pdxB glpB glpB glpA glpA folE folE dld dld thiM thiM thiD thiD pduX pduX pduW pduW pduV pduV pduU pduU pduT pduT pduS pduS pduQ pduQ pduP pduP pduO pduO pduN pduN pduM pduM pduL pduL pduK pduK pduJ pduJ pduH pduH pduG pduG pduE pduE pduD pduD pduC pduC pudB pudB pduA pduA pocR pocR adhE adhE STM1627 STM1627 STM1620 STM1620 ydfI ydfI pdxY pdxY pdxH pdxH gloA gloA ydiJ ydiJ ydiB ydiB aroD aroD STM1269 STM1269 ycfN ycfN hpaE hpaE hpaG hpaG serC serC ybdB ybdB entF entF entD entD thiI thiI dxs dxs thiL thiL gloB gloB uppS uppS pdxA pdxA STM3859 STM3859 yihS yihS tpiA tpiA glpX glpX glpK glpK thiH thiH thiG thiG thiE thiE thiC thiC cysQ cysQ STM4420 STM4420 iolE iolE iolG iolG yjjX yjjX eutB eutB eutA eutA eutH eutH eutG eutG eutJ eutJ eutE eutE eutN eutN eutM eutM eutD eutD
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STM4431Putative thiamine pyrophosphate-requiring enzyme; Similar to E. coli acetolactate synthase I, valine-sensitive, large subunit (AAC76694.1); Blastp hit to AAC76694.1 (562 aa), 27% identity in aa 26 - 326, 34% identity in aa 12 - 126; Belongs to the TPP enzyme family. (646 aa)
eutTPutative ethanolamine utilization cobalamin adenosyltransferase; Converts CNB12 to ADOB12. (267 aa)
eutQEthanolamine utilization protein EUTQ. (SW:EUTQ_SALTY). (229 aa)
eutPEthanolamine utilization protein EUTP. (SW:EUTP_SALTY). (159 aa)
eutSPutative ethanol utilization carboxysome structural protein; May be involved in the formation of a specific microcompartment in the cell in which the metabolism of potentially toxic by-products takes place; Belongs to the EutS/PduU family. (111 aa)
suhBInositol monophosphatase; Similar to E. coli enhances synthesis of sigma32 in mutant; extragenic suppressor, may modulate RNAse III lethal action (AAC75586.1); Blastp hit to AAC75586.1 (267 aa), 97% identity in aa 1 - 267; Belongs to the inositol monophosphatase superfamily. (267 aa)
pdxJCarries out condensation and ring closure step after PdxA in pyridoxine biosynthesis; Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino- 2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. (243 aa)
epdD-erythrose 4-phosphate dehydrogenase; Catalyzes the NAD-dependent conversion of D-erythrose 4- phosphate to 4-phosphoerythronate. (348 aa)
STM3083Putative mannitol dehydrogenase; Similar to E. coli putative oxidoreductase (AAC75233.1); Blastp hit to AAC75233.1 (488 aa), 49% identity in aa 1 - 477; Belongs to the mannitol dehydrogenase family. (490 aa)
STM3136Similar to E. coli D-mannonate oxidoreductase (AAC77279.1); Blastp hit to AAC77279.1 (486 aa), 79% identity in aa 4 - 486; Belongs to the mannitol dehydrogenase family. (490 aa)
gatYPutative fructose/tagatose biphosphate aldolase; Catalytic subunit of the tagatose-1,6-bisphosphate aldolase GatYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires GatZ subunit for full activity and stability. Is involved in the catabolism of galactitol. (284 aa)
gatZPutative tagatose 6-phosphate kinase 1; Component of the tagatose-1,6-bisphosphate aldolase GatYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of GatY. When expressed alone, GatZ does not show any aldolase activity. Is involved in the catabolism of galactitol. (423 aa)
STM3261Similar to E. coli galactitol-1-phosphate dehydrogenase (AAC75152.1); Blastp hit to AAC75152.1 (346 aa), 68% identity in aa 1 - 344. (347 aa)
aroEDehydroshikimate reductase; Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). (272 aa)
gphPhosphoglycolate phosphatase; Specifically catalyzes the dephosphorylation of 2- phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress. Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family. (252 aa)
glpEThiosulfate/cyanide sulfurtransferase; Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. (108 aa)
mtlDSimilar to E. coli mannitol-1-phosphate dehydrogenase (AAC76624.1); Blastp hit to AAC76624.1 (382 aa), 93% identity in aa 1 - 380. (382 aa)
lldDL-lactate dehydrogenase; Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain; Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family. (396 aa)
STM3781Putative sugar (pentulose and hexulose) kinase; Similar to E. coli L-fuculokinase (AAC75845.1); Blastp hit to AAC75845.1 (482 aa), 24% identity in aa 17 - 444. (494 aa)
eutCEthanolamine ammonia-lyase, light chain; Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. (298 aa)
eutLPutative carboxysome structural protein; May be involved in the formation of a specific microcompartment in the cell in which the metabolism of potentially toxic by-products takes place; Belongs to the EutL/PduB family. (219 aa)
eutKPutative carboxysome structural protein; May be involved in the formation of a specific microcompartment in the cell in which the metabolism of potentially toxic by-products takes place; Belongs to the bacterial microcompartments protein family. (164 aa)
eutRPutative regulator ethanolamine operon; Activates the transcription of the eut operon. Also positively regulates its own transcription. Probably binds ethanolamine and vitamin B12 as effectors. (350 aa)
pdxKPyridoxal-pyridoxamine kinase; B6-vitamer kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxine (PN), pyridoxal (PL), and pyridoxamine (PM), forming their respective 5'-phosphorylated esters, i.e. PNP, PLP and PMP. Belongs to the pyridoxine kinase family. PdxK subfamily. (288 aa)
pdxBErythronate-4-phosphate dehydrogenase; Catalyzes the oxidation of erythronate-4-phosphate to 3- hydroxy-2-oxo-4-phosphonooxybutanoate. (378 aa)
glpBSn-glycerol-3-phosphate dehydrogenase (anaerobic), membrane anchor subunit; Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor; Belongs to the anaerobic G-3-P dehydrogenase subunit B family. (419 aa)
glpASimilar to E. coli sn-glycerol-3-phosphate dehydrogenase (anaerobic), large subunit (AAC75301.1); Blastp hit to AAC75301.1 (542 aa), 92% identity in aa 1 - 542; Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family. (542 aa)
folESimilar to E. coli GTP cyclohydrolase I (AAC75214.1); Blastp hit to AAC75214.1 (222 aa), 96% identity in aa 1 - 221. (222 aa)
dldNADH independent D-lactate dehydrogenase; Catalyzes the oxidation of D-lactate to pyruvate. Belongs to the quinone-dependent D-lactate dehydrogenase family. (576 aa)
thiMHydoxyethylthiazole kinase (THZ kinase); Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ); Belongs to the Thz kinase family. (265 aa)
thiDHydroxy-phosphomethylpyrimidine kinase (HMP-P kinase); Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Belongs to the ThiD family. (266 aa)
pduXPropanediol utilization protein; L-threonine kinase that catalyzes the conversion of L- threonine to L-threonine-O-3-phosphate. Involved in the de novo synthesis of adenosylcobalamin (coenzyme B12) and the assimilation of cobyric acid. Uses ATP; the activity with CTP, GTP or UTP is 6, 11, and 3% of the activity with ATP, respectively. (300 aa)
pduWProbable propionate kinase. (SW:PDUW_SALTY); Belongs to the acetokinase family. PduW subfamily. (404 aa)
pduVPropanediol utilization protein PDUV. (SW:PDUV_SALTY). (150 aa)
pduUPolyhedral bodies; propanediol utilization protein PDUU. (SW:PDUU_SALTY). (116 aa)
pduTPropanediol utilization protein; Polyhedral bodies; similar to E. coli detox protein (AAC75510.1); Blastp hit to AAC75510.1 (111 aa), 41% identity in aa 16 - 93, 31% identity in aa 16 - 90. (184 aa)
pduSPropanediol utilization protein; Polyhedral bodies; similar to E. coli putative membrane protein (AAC74701.1); Blastp hit to AAC74701.1 (740 aa), 33% identity in aa 131 - 448, 37% identity in aa 33 - 93. (451 aa)
pduQPropanediol utilization propanol dehydrogenase; Similar to E. coli CoA-linked acetaldehyde dehydrogenase and iron-dependent alcohol dehydrogenase; pyruvate-formate-lyase deactivase (AAC74323.1); Blastp hit to AAC74323.1 (891 aa), 40% identity in aa 574 - 860, 35% identity in aa 456 - 556. (370 aa)
pduPPropanediol utilization CoA-dependent propionaldehyde dehydrogenase; Similar to E. coli ethanolamine utilization; similar to acetaldehyde dehydrogenase (AAC75508.1); Blastp hit to AAC75508.1 (467 aa), 45% identity in aa 1 - 466. (464 aa)
pduOPropanediol utilization B12 related protein; Belongs to the Cob(I)alamin adenosyltransferase family. (336 aa)
pduNPropanediol utilization protein; Polyhedral bodies; similar to E. coli detox protein (AAC75509.1); Blastp hit to AAC75509.1 (95 aa), 43% identity in aa 1 - 83. (91 aa)
pduMPropanediol utilization protein. (163 aa)
pduLPropanediol utilization protein; Involved in 1,2-propanediol (1,2-PD) degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate. Is also able to catalyze the reverse reaction. To a lesser extent, also displays phosphate acetyltransferase activity. Belongs to the PduL family. (210 aa)
pduKPropanediol utilization protein; Polyhedral bodies; similar to E. coli detox protein (AAC75510.1); Blastp hit to AAC75510.1 (111 aa), 35% identity in aa 9 - 92. (160 aa)
pduJPropanediol utilization protein; Polyhedral bodies; similar to E. coli detox protein (AAC75510.1); Blastp hit to AAC75510.1 (111 aa), 64% identity in aa 17 - 101. (91 aa)
pduHPropanediol utilization diol dehydratase reactivation protein. (116 aa)
pduGPropanediol utilization diol dehydratase reactivation protein. (610 aa)
pduEPropanediol utilization dehydratase, small subunit; Part of the PduCDE complex that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. Is required for S.typhimurium growth on 1,2-propanediol as the sole carbon and energy source; Belongs to the diol/glycerol dehydratase small subunit family. (173 aa)
pduDPropanediol utilization dehydratase, medium subunit; Part of the PduCDE complex that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. Is required for S.typhimurium growth on 1,2-propanediol as the sole carbon and energy source. (224 aa)
pduCPropanediol utilization dehydratase, large subunit; Part of the PduCDE complex that catalyzes the dehydration of 1,2-propanediol to propionaldehyde. Is required for S.typhimurium growth on 1,2-propanediol as the sole carbon and energy source. (554 aa)
pudBPolyhedral bodies; propanediol utilization protein PDUB. (SW:PDUB_SALTY). (233 aa)
pduAPolyhedral bodies; propanediol utilization protein PDUA. (SW:PDUA_SALTY). (94 aa)
pocRPropanediol utilization protein; Positive regulatory protein of pdu and cob operons. (303 aa)
adhESimilar to E. coli CoA-linked acetaldehyde dehydrogenase and iron-dependent alcohol dehydrogenase; pyruvate-formate-lyase deactivase (AAC74323.1); Blastp hit to AAC74323.1 (891 aa), 97% identity in aa 1 - 891; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. (892 aa)
STM1627Similar to E. coli alcohol dehydrogenase class III; formaldehyde dehydrogenase, glutathione-dependent (AAC73459.1); Blastp hit to AAC73459.1 (369 aa), 80% identity in aa 1 - 369; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. (372 aa)
STM1620Putative oxidase; Similar to E. coli L-lactate dehydrogenase (AAC76629.1); Blastp hit to AAC76629.1 (396 aa), 38% identity in aa 212 - 384, 33% identity in aa 22 - 175. (400 aa)
ydfIPutative mannitol dehydrogenase; Similar to E. coli putative oxidoreductase (AAC74615.1); Blastp hit to AAC74615.1 (486 aa), 81% identity in aa 1 - 484; Belongs to the mannitol dehydrogenase family. (488 aa)
pdxYPyridoxal kinase 2; Pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP. (286 aa)
pdxHPyridoxine 5'-phosphate oxidase; Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP). (218 aa)
gloAGlyoxalase I; Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. (135 aa)
ydiJSimilar to E. coli putative oxidase (AAC74757.1); Blastp hit to AAC74757.1 (1018 aa), 88% identity in aa 1 - 1017. (1018 aa)
ydiBPutative shikimate 5-dehydrogenase; The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD. (288 aa)
aroD3-dehydroquinate dehydratase; Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis- dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsylon-amino group of a lys-170 at the active site. Belongs to the type-I 3-dehydroquinase family. (252 aa)
STM1269Putative chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. (181 aa)
ycfNPutative cytoplasmic protein; Catalyzes the phosphorylation of thiamine to thiamine phosphate. (274 aa)
hpaE4-hydroxyphenylacetate catabolism protein; Similar to E. coli aldehyde dehydrogenase, prefers NADP over NAD (AAC74382.1); Blastp hit to AAC74382.1 (495 aa), 39% identity in aa 23 - 493. (488 aa)
hpaG4-hydroxyphenylacetate catabolism protein; Similar to E. coli putative isomerase (AAC74264.1); Blastp hit to AAC74264.1 (219 aa), 38% identity in aa 22 - 219, 29% identity in aa 35 - 211. (429 aa)
serC3-phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. (362 aa)
ybdBPutative protein PaaI, possibly involved in aromatic compounds catabolism; Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules. Belongs to the thioesterase PaaI family. (137 aa)
entFEnterobactin synthetase, component F (nonribosomal peptide synthetase); Similar to E. coli ATP-dependent serine activating enzyme (may be part of enterobactin synthase as component F) (AAC73687.1); Blastp hit to AAC73687.1 (1293 aa), 79% identity in aa 1 - 1293. (1294 aa)
entDEnterochelin synthetase, component D (phoshpantetheinyltransferase); Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo- domains of both EntB (ArCP domain) and EntF (PC [...] (234 aa)
thiISulfur transfer protein (from cys to ThiS and from IscS to U8-tRNA); Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. (482 aa)
dxs1-deoxyxylulose-5-phosphate synthase; Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D- xylulose-5-phosphate (DXP); Belongs to the transketolase family. DXPS subfamily. (620 aa)
thiLThiamin-monophosphate kinase; Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. (325 aa)
gloBHydroxyacylglutathione hydrolase; Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl- glutathione to form glutathione and D-lactic acid. (251 aa)
uppSUndecaprenyl pyrophosphate synthetase (di-trans, poly-cis-decaprenylcistransferase); Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di- trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide. (252 aa)
pdxANAD-dependent dehydrogenase/carboxylase; Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L- threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). (329 aa)
STM3859Similar to E. coli dehydroshikimate reductase (AAC76306.1); Blastp hit to AAC76306.1 (272 aa), 26% identity in aa 20 - 258; quinate 5-dehydrogenase. (272 aa)
yihSPutative isomerase; Catalyzes the isomerization of sulfoquinovose (SQ) to 6- deoxy-6-sulfo-D-fructose (SF) (By similarity). In vitro, can also catalyze the interconversion of mannose, fructose and glucose, but has extremely low activity with glucose. Belongs to the N-acylglucosamine 2-epimerase family. (413 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)
glpXSimilar to E. coli unknown function in glycerol metabolism (AAC76907.1); Blastp hit to AAC76907.1 (336 aa), 94% identity in aa 1 - 336. (336 aa)
glpKGlycerol kinase; Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. (502 aa)
thiHThiamin biosynthesis protein, thiazole moiety; Catalyzes the radical-mediated cleavage of tyrosine to 2- iminoacetate and 4-cresol; Belongs to the radical SAM superfamily. ThiH family. (377 aa)
thiGThiamin biosynthesis protein, thiazole moiety; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. (256 aa)
thiEThiamin phosphate synthase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Belongs to the thiamine-phosphate synthase family. (211 aa)
thiC5'-phosphoryl-5-aminoimidazole; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. (631 aa)
cysQCysQ protein; Converts adenosine-3',5'-bisphosphate (PAP) to AMP. (246 aa)
STM4420Putative inner membrane protein. (269 aa)
iolEPutative endonuclease; Catalyzes the dehydration of inosose (2-keto-myo-inositol, 2KMI or 2,4,6/3,5-pentahydroxycyclohexanone) to 3D-(3,5/4)- trihydroxycyclohexane-1,2-dione (D-2,3-diketo-4-deoxy-epi-inositol). Belongs to the IolE/MocC family. (306 aa)
iolGPutative dehydrogenase; Involved in the oxidation of myo-inositol (MI) to 2-keto-myo- inositol (2KMI or 2-inosose). (336 aa)
yjjXPutative cytoplasmic protein; Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. (171 aa)
eutBEthanolamine ammonia-lyase, heavy chain; Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. (453 aa)
eutACPPZ-55 prophage protein; May protect the EutBC lyase from inhibition. (467 aa)
eutHPutative transport protein; Possibly involved in the transport of ethanolamine from the periplasm to the cytoplasm. (408 aa)
eutGPutative transport protein in ethanolamine utilization; May act on the acetaldehyde produced from the degradation of ethanolamine; Belongs to the iron-containing alcohol dehydrogenase family. (395 aa)
eutJPutative heatshock protein (Hsp70); Ethanolamine utilization protein EUTJ. (SW:EUTJ_SALTY). (279 aa)
eutEPutative aldehyde oxidoreductase in ethanolamine utilization; May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. (467 aa)
eutNPutative detox protein in ethanolamine utilization; May be involved in the formation of a specific microcompartment in the cell in which the metabolism of potentially toxic by-products takes place; To cyanobacterial carbon dioxide concentrating mechanism protein CcmL. (99 aa)
eutMPutative detox protein in ethanolamine utilization; May be involved in the formation of a specific microcompartment in the cell in which the metabolism of potentially toxic by-products takes place; Belongs to the bacterial microcompartments protein family. (96 aa)
eutDEthanolamine utilization protein EUTD. (SW:EUTD_SALTY). (338 aa)
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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