STRINGSTRING
dapB dapB yabF yabF pdxA pdxA leuB leuB lpdA lpdA pdxA2 pdxA2 STM0564 STM0564 nuoJ nuoJ nuoA nuoA nuoB nuoB nuoC nuoC nuoE nuoE nuoF nuoF nuoG nuoG nuoH nuoH nuoI nuoI nuoK nuoK nuoN nuoN yfbG yfbG yeiA yeiA preT preT rfbB rfbB rfbD rfbD rfbG rfbG udg udg hisD hisD cbiJ cbiJ STM1795 STM1795 fabI fabI acpD acpD STM1627 STM1627 ydcW ydcW sfcA sfcA yneI yneI ydfI ydfI pntB pntB pntA pntA ydiB ydiB celF celF nadE nadE astD astD gapA gapA cobB cobB ycdW ycdW putA putA wraB wraB hpaC hpaC galE galE pnuC pnuC nadD nadD ahpF ahpF ybdH ybdH nfnB nfnB pdxB pdxB yfcX yfcX lig lig eutG eutG guaB guaB asrB asrB asrC asrC hmpA hmpA tyrA tyrA yfjB yfjB ygbD ygbD epd epd STM3083 STM3083 STM3136 STM3136 yghA yghA garR garR mdh mdh trkA trkA yheR yheR nirD nirD cysG cysG nadR nadR iolG iolG yjeF yjeF dsbD dsbD melA melA yjaD yjaD udhA udhA gldA gldA metF metF yihU yihU fadB fadB ubiB ubiB wecC wecC gidA gidA yicF yicF tdh tdh gpsA gpsA mtlD mtlD yiaK yiaK yiaE yiaE gor gor STM3529 STM3529 aroB aroB
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dapBDihydrodipicolinate reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate; Belongs to the DapB family. (273 aa)
yabFPutative NAD(P)H oxidoreductase; Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefC. Shows redox enzymatic activity, but this enzymatic activity is not required for activation of KefC; Belongs to the NAD(P)H dehydrogenase (quinone) family. KefF subfamily. (176 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)
leuB3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. (363 aa)
lpdALipoamide dehydrogenase (NADH); Component of 2-oxodehydrogenase and pyruvate complexes; L protein of glycine cleavage complex second part; similar to E. coli lipoamide dehydrogenase (NADH); component of 2-oxodehydrogenase and pyruvate complexes; L-protein of glycine cleavage complex (AAC73227.1); Blastp hit to AAC73227.1 (474 aa), 98% identity in aa 1 - 474. (474 aa)
pdxA2Pyridoxine phosphate biosynthetic protein; Catalyzes the NAD-dependent oxidation and subsequent decarboxylation of D-threonate 4-phosphate to produce dihydroxyacetone phosphate (DHAP). Can also use 4-hydroxy-L-threonine 4-phosphate as substrate. Belongs to the PdxA family. PdxA2 subfamily. (327 aa)
STM0564Similar to E. coli putative oxidoreductase (AAC73407.1); Blastp hit to AAC73407.1 (450 aa), 74% identity in aa 10 - 450. (441 aa)
nuoJNADH dehydrogenase I chain J; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (184 aa)
nuoANADH dehydrogenase I chain A; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 3 family. (147 aa)
nuoBNADH dehydrogenase I chain B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (220 aa)
nuoCNADH dehydrogenase I chain C,D; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (600 aa)
nuoENADH dehydrogenase I chain E; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity); Belongs to the complex I 24 kDa subunit family. (166 aa)
nuoFNADH dehydrogenase I chain F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). (445 aa)
nuoGNADH dehydrogenase I chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). (910 aa)
nuoHNADH dehydrogenase I chain H; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. (325 aa)
nuoINADH dehydrogenase I chain I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (180 aa)
nuoKNADH dehydrogenase I chain K; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4L family. (100 aa)
nuoNNADH dehydrogenase I chain N; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 2 family. (425 aa)
yfbGPutative transformylase; Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto- arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4- amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido- arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (By similarity); In the N-terminal section; belongs to the Fmt family. UDP- L-Ara4N formyltransferase subfamily. (660 aa)
yeiAPutative dihydropyrimidine dehydrogenase; Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT) (By similarity). (411 aa)
preTPutative NADPH-dependent glutamate synthase beta chain or related oxidoreductase; Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT) (By similarity). (413 aa)
rfbBdTDP-glucose 4,6 dehydratase; Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6- deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction; Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily. (361 aa)
rfbDTDP-rhamnose synthetase; Involved in the biosynthesis of the dTDP-L-rhamnose which is an important component of lipopolysaccharide (LPS). Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. RmlD uses NADH and NADPH nearly equally well. (299 aa)
rfbGLPS side chain defect; CDP-glucose 4,6-dehydratase. (SW:RFBG_SALTY); Belongs to the NAD(P)-dependent epimerase/dehydratase family. (359 aa)
udgUDP-glucose 6-dehydrogenase. (SW:UDG_SALTY). (388 aa)
hisDHistidinal dehydrogenase; Catalyzes the sequential NAD-dependent oxidations of L- histidinol to L-histidinaldehyde and then to L-histidine. (434 aa)
cbiJSynthesis of vitamin B12 adenosyl cobalamide precursor; Catalyzes the reduction of the macrocycle of cobalt- precorrin-6A to cobalt-precorrin-6B. (263 aa)
STM1795Putative homolog of glutamic dehydrogenase; Similar to E. coli NADP-specific glutamate dehydrogenase (AAC74831.1); Blastp hit to AAC74831.1 (447 aa), 32% identity in aa 33 - 408; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. (441 aa)
fabIEnoyl-[acyl-carrier-protein] reductase (NADH); Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis (By similarity). Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily. (262 aa)
acpDAcyl carrier protein phosphodiesterase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (201 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)
ydcWPutative aldehyde dehydrogenase; Catalyzes the oxidation 4-aminobutanal (gamma- aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA). This is the second step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate via 4- aminobutanal. Also functions as a 5-aminopentanal dehydrogenase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. (481 aa)
sfcASimilar to E. coli NAD-linked malate dehydrogenase (malic enzyme) (AAC74552.1); Blastp hit to AAC74552.1 (574 aa), 92% identity in aa 10 - 574; Belongs to the malic enzymes family. (565 aa)
yneISimilar to E. coli putative aldehyde dehydrogenase (AAC74598.1); Blastp hit to AAC74598.1 (470 aa), 81% identity in aa 9 - 470. (462 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)
pntBPyridine nucleotide transhydrogenase, beta subunit; The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane; Belongs to the PNT beta subunit family. (462 aa)
pntAPyridine nucleotide transhydrogenase, alpha subunit; The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane; Belongs to the AlaDH/PNT family. (509 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)
celFSimilar to E. coli phospho-beta-glucosidase; cryptic (AAC74804.1); Blastp hit to AAC74804.1 (450 aa), 90% identity in aa 1 - 450; cellobiose-6-phosphate hydrolase. (451 aa)
nadENAD synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. (275 aa)
astDSuccinylglutamic semialdehyde dehydrogenase; Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate; Belongs to the aldehyde dehydrogenase family. AstD subfamily. (492 aa)
gapAGlyceraldehyde-3-phosphate dehydrogenase A; Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. (331 aa)
cobBPutative nicotinate-nucleotide dimethylbenzimidazolephosphoribosltransferase; NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form (By similarity). Activates the enzyme acetyl-CoA synthetase by deacetylating 'Lys-609' in the inactive, acetylated form of the enzyme. May also modulate the activity of other propionyl-adenosine monophosphate (AMP)-forming enzymes. Overexpression compensates for a cobT deletion, suggesting it may have [...] (273 aa)
ycdWPutative oxidoreductase; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. (312 aa)
putAPlasma membrane proline 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)
wraBSimilar to E. coli trp repressor binding protein; affects association of trp repressor and operator (AAC74089.1); Blastp hit to AAC74089.1 (198 aa), 94% identity in aa 1 - 198. (198 aa)
hpaC4-hydroxyphenylacetate catabolism protein; Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the large HpaB component or to other electron acceptors such as cytochrome c and Fe(3+) ion (By similarity); Belongs to the non-flavoprotein flavin reductase family. HpaC subfamily. (170 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 (By similarity). (338 aa)
pnuCNMN family, nucleoside/purine/pyrimidine transporter; Required for nicotinamide riboside transport across the inner membrane. (239 aa)
nadDPutative nicotinic acid mononucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). (213 aa)
ahpFAlkyl hydroperoxide reductase, F52a subunit; 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)
ybdHPutative glycerol dehydrogenase; Similar to E. coli putative oxidoreductase (AAC73700.1); Blastp hit to AAC73700.1 (362 aa), 81% identity in aa 1 - 361. (362 aa)
nfnBDihydropteridine reductase; Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone (By similarity). (217 aa)
pdxBErythronate-4-phosphate dehydrogenase; Catalyzes the oxidation of erythronate-4-phosphate to 3- hydroxy-2-oxo-4-phosphonooxybutanoate. (378 aa)
yfcXPutative 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; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (715 aa)
ligDNA ligase; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. (671 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)
guaBIMP dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family. (488 aa)
asrBAnaerobic sulfide reductase; This enzyme catalyzes the hydrogen sulfide production from sulfite. It is strictly anaerobic. It is regulated by electron acceptors rather than by cysteine. (272 aa)
asrCAnaerobic sulfide reductase; This enzyme catalyzes the hydrogen sulfide production from sulfite. It is strictly anaerobic. It is regulated by electron acceptors rather than by cysteine; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (337 aa)
hmpADihydropteridine 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. Belongs to the globin family. Two-domain flavohemoproteins subfamily. (396 aa)
tyrAChorismate mutase T; Bifuctional; similar to E. coli chorismate mutase-T and prephenate dehydrogenase (AAC75649.1); Blastp hit to AAC75649.1 (373 aa), 95% identity in aa 1 - 372. (373 aa)
yfjBPutative kinase; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates as a source of phosphorus. NADH cannot replace NAD as a substrate. (292 aa)
ygbDPutative oxidoreductase; One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase. (377 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)
yghASimilar to E. coli putative oxidoreductase (AAC76039.1); Blastp hit to AAC76039.1 (294 aa), 93% identity in aa 1 - 294. (294 aa)
garRTartronate semialdehyde reductase (TSAR); Catalyzes the reduction of tatronate semialdehyde to D- glycerate; Belongs to the HIBADH-related family. 2-hydroxy-3- oxopropionate reductase subfamily. (296 aa)
mdhMalate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa)
trkATrk system transport of potassium protein; Part of the constitutive potassium transport systems TrkG and TrkH. May regulate the transport activity of TrkG and TrkH systems. Binds to NAD(+) and NADH. In Salmonella it is required for resistance to antimicrobial peptides. (458 aa)
yheRPutative NAD(P)H oxidoreductase; Regulatory subunit of a potassium efflux system that confers protection against electrophiles. Required for full activity of KefB. (183 aa)
nirDNitrite reductase small subunit; Required for activity of the reductase. (108 aa)
cysGSiroheme synthase; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. (457 aa)
nadRTrifunctional protein; This enzyme has three activities: DNA binding, nicotinamide mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN) kinase. The DNA-binding domain binds to the nadB operator sequence in an NAD- and ATP-dependent manner. As NAD levels increase within the cell, the affinity of NadR for the nadB operator regions of nadA, nadB, and pncB increases, repressing the transcription of these genes. The RN kinase activity catalyzes the phosphorylation of RN to form nicotinamide ribonucleotide. The NMN adenylyltransferase activity catalyzes the transfer of the A [...] (410 aa)
iolGPutative dehydrogenase; Involved in the oxidation of myo-inositol (MI) to 2-keto-myo- inositol (2KMI or 2-inosose). (336 aa)
yjeFPutative sugar kinase; 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. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both ep [...] (515 aa)
dsbDThiol:disulfide interchange protein; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. (567 aa)
melAAlpha-galactosidase. (SW:AGAL_SALTY); Belongs to the glycosyl hydrolase 4 family. (451 aa)
yjaDPutative NTP pyrophosphohydrolases containing a Zn-finger; Probably nucleic-acid-binding; NADH pyrophosphatase. (SW:NUDC_SALTY). (257 aa)
udhASoluble pyridine nucleotide transhydrogenase; Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation. (466 aa)
gldASimilar to E. coli glycerol dehydrogenase, (NAD) (AAC76927.1); Blastp hit to AAC76927.1 (380 aa), 91% identity in aa 14 - 380. (367 aa)
metF5,10-methylenetetrahydrofolate reductase. (SW:METF_SALTY); Belongs to the methylenetetrahydrofolate reductase family. (296 aa)
yihUPutative oxidoreductase; Reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1- sulfonate (DHPS); Belongs to the HIBADH-related family. 3-sulfolactaldehyde reductase subfamily. (298 aa)
fadB3-hydroxyacyl-coA dehydrogenase of 4-enzyme FadB protein; 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)
ubiBFMN reductase; Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides; Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein oxidoreductase family. (233 aa)
wecCUDP-N-acetyl-D-mannosaminuronic acid dehydrogenase; Catalyzes the four-electron oxidation of UDP-N-acetyl-D- mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N- acetylmannosaminuronic acid (UDP-ManNAcA); Belongs to the UDP-glucose/GDP-mannose dehydrogenase family. WecC subfamily. (420 aa)
gidAAssociated with glucose-inhibited division; 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; Belongs to the MnmG family. (629 aa)
yicFPutative DNA ligase; Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. Belongs to the NAD-dependent DNA ligase family. LigB subfamily. (561 aa)
tdhThreonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. (341 aa)
gpsAGlycerol-3-phosphate dehydrogenase [NAD+]. (SW:GPDA_SALTY); Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family. (339 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)
yiaKPutative malate dehydrogenase; Catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH, to form 3-keto-L-gulonate. (332 aa)
yiaE2-keto-D-gluconate reductase; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily. (324 aa)
gorSimilar to E. coli glutathione oxidoreductase (AAC76525.1); Blastp hit to AAC76525.1 (450 aa), 94% identity in aa 1 - 450. (450 aa)
STM3529Similar to E. coli glycerol dehydrogenase, (NAD) (AAC76927.1); Blastp hit to AAC76927.1 (380 aa), 49% identity in aa 21 - 373. (369 aa)
aroBDehydroquinate synthase; Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ); Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family. (362 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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