STRINGSTRING
fdoH fdoH hemN hemN STM3966 STM3966 ilvD ilvD yhgI yhgI yhgG yhgG nirB nirB bfd bfd tdcG tdcG ygiR ygiR hypO hypO STM3123 STM3123 mutY mutY yggW yggW sdaB sdaB ygcA ygcA ygcF ygcF STM0036 STM0036 lytB lytB fixX fixX leuC leuC acnB acnB yadR yadR leuC2 leuC2 STM0611 STM0611 lipA lipA miaB miaB citB citB sdhB sdhB nadA nadA bioB bioB moaA moaA dinG dinG yliG yliG STM0858 STM0858 ybjF ybjF hcr hcr hcp hcp dmsA dmsA pflA pflA STM1287 STM1287 ydiT ydiT ttrA ttrA ttrB ttrB ydhD ydhD nth nth rsxC rsxC ydgM ydgM fumA fumA STM1498 STM1498 STM1499 STM1499 STM1539 STM1539 fdnH fdnH fdnG fdnG narZ narZ nifJ nifJ ydaO ydaO fnr fnr acnA acnA narG narG STM1786 STM1786 sdaA sdaA edd edd pduS pduS phsB phsB phsA phsA rfbI-2 rfbI-2 mrp mrp yeiA yeiA STM2196 STM2196 napA napA napF napF nuoI nuoI nuoG nuoG nuoF nuoF nuoE nuoE nuoB nuoB gcpE gcpE yfgB yfgB STM2530 STM2530 nifS nifS yfhP yfhP asrA asrA asrB asrB cysI cysI asrC asrC nrdG nrdG yjeB yjeB yjeS yjeS frdB frdB yjeK yjeK STM4305 STM4305 fumB fumB fdhF fdhF soxR soxR thiC thiC thiH thiH fdoG fdoG
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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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fdoHFormate dehydrogenase-O, Fe-S subunit; The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. (300 aa)
hemNO2-independent coproporphyrinogen III oxidase; Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX. (457 aa)
STM3966Similar to E. coli putative arylsulfatase regulator (AAC76803.1); Blastp hit to AAC76803.1 (411 aa), 47% identity in aa 11 - 402. (447 aa)
ilvDDihydroxy-acid dehydratase. (SW:ILVD_SALTY); Belongs to the IlvD/Edd family. (616 aa)
yhgIPutative thioredoxin-like proteins and domain protein; Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins. (191 aa)
yhgGPutative cytoplasmic protein; May function as a transcriptional regulator that controls feoABC expression. (78 aa)
nirBSimilar to E. coli nitrite reductase (NAD(P)H) subunit (AAC76390.1); Blastp hit to AAC76390.1 (847 aa), 95% identity in aa 1 - 847; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (847 aa)
bfdRegulatory or redox component complexing with Bfr; Seems to associate with BFR; could be a general redox and/or regulatory component participating in the iron storage mobilization functions of BFR. Could participate in the release or the delivery of iron from/to bacterioferritin (or other iron complexes) (By similarity). (64 aa)
tdcGSimilar to E. coli L-serine dehydratase (deaminase), L-SD2 (AAC75839.1); Blastp hit to AAC75839.1 (455 aa), 74% identity in aa 1 - 452; Belongs to the iron-sulfur dependent L-serine dehydratase family. (454 aa)
ygiRPutative Fe-S oxidoreductase family 2; Similar to E. coli orf, hypothetical protein (AAC76051.1); Blastp hit to AAC76051.1 (413 aa), 46% identity in aa 1 - 26. (723 aa)
hypOPutative Ni/Fe hydrogenases, small subunit; Similar to E. coli putative hydrogenase subunit (AAC76033.1); Blastp hit to AAC76033.1 (372 aa), 96% identity in aa 1 - 372. (372 aa)
STM3123Similar to E. coli putative arylsulfatase regulator (AAC76803.1); Blastp hit to AAC76803.1 (411 aa), 36% identity in aa 4 - 248, 34% identity in aa 230 - 387. (394 aa)
mutYAdenine DNA glycosylase; Adenine glycosylase active on G-A mispairs. MutY also corrects error-prone DNA synthesis past GO lesions which are due to the oxidatively damaged form of guanine: 7,8-dihydro-8-oxoguanine (8-oxo- dGTP); Belongs to the Nth/MutY family. (350 aa)
yggWPutative oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (378 aa)
sdaBSimilar to E. coli L-serine dehydratase (deaminase), L-SD2 (AAC75839.1); Blastp hit to AAC75839.1 (455 aa), 94% identity in aa 1 - 455; L-threonine deaminase 2; Belongs to the iron-sulfur dependent L-serine dehydratase family. (455 aa)
ygcAPutative RNA methyltransferase; Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmD subfamily. (431 aa)
ygcFPutative organic radical activating enzymes; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. (223 aa)
STM0036Similar to E. coli putative arylsulfatase regulator (AAC76803.1); Blastp hit to AAC76803.1 (411 aa), 46% identity in aa 8 - 401. (396 aa)
lytBRegulates the activity of guanosine 3',5'-bispyrophosphate synthetase I (RelA); Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. (316 aa)
fixXPutative ferredoxin; Could be part of an electron transfer system required for anaerobic carnitine reduction. Could be a 3Fe-4S cluster-containing protein (By similarity). (95 aa)
leuC3-isopropylmalate isomerase (dehydratase), subunit with LeuD; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (466 aa)
acnBAconitate hydratase 2; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2- methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA- binding regulatory protein which regulates FliC synthesis via interaction with the ftsH transcript to decrease the intracellular levels of FtsH. The lower levels of Fts [...] (865 aa)
yadRPutative HesB-like domain protein; Required for insertion of 4Fe-4S clusters for at least IspG. (129 aa)
leuC2Putative 3-isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (473 aa)
STM0611Similar to E. coli putative oxidoreductase, major subunit (AAC74659.1); Blastp hit to AAC74659.1 (808 aa), 31% identity in aa 10 - 314, 26% identity in aa 298 - 673, 36% identity in aa 636 - 765, 34% identity in aa 489 - 517; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (759 aa)
lipALipoate synthase, an iron-sulfur enzyme; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. (321 aa)
miaBMethylthiolation of isopentenylated A37 derivatives in rRNA; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. (474 aa)
citBCitrate utilization protein B. (SW:CIT2_SALTY). (379 aa)
sdhBSuccinate dehydrogenase, Fe-S protein; Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. (239 aa)
nadAQuinolinate synthetase, A protein; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. (347 aa)
bioBBiotin synthetase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family. (346 aa)
moaAMolybdopterin biosynthesis, protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (329 aa)
dinGLexA regulated (SOS) repair enzyme; DNA-dependent ATPase and 5'-3' DNA helicase. (714 aa)
yliGPutative Fe-S oxidoreductases family 1; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (441 aa)
STM0858Putative dehydrogenase (flavoproteins); Accepts electrons from ETF and reduces ubiquinone. (561 aa)
ybjFPutative tRNA (uracil-5-)-methyltransferase; Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmC subfamily. (376 aa)
hcrNADH oxidoreductase for hcp gene product; Similar to E. coli putative enzyme (AAC73959.1); Blastp hit to AAC73959.1 (322 aa), 90% identity in aa 1 - 322. (323 aa)
hcpHybrid cluster protein; Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O. (550 aa)
dmsASimilar to E. coli anaerobic dimethyl sulfoxide reductase subunit A (AAC73980.1); Blastp hit to AAC73980.1 (785 aa), 93% identity in aa 1 - 784; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (814 aa)
pflAPyruvate formate lyase activating enzyme 1; Activation of pyruvate formate-lyase under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine; Belongs to the organic radical-activating enzymes family. (274 aa)
STM1287Similar to E. coli putative arylsulfatase regulator (AAC76803.1); Blastp hit to AAC76803.1 (411 aa), 46% identity in aa 10 - 401. (398 aa)
ydiTPutative ferredoxin; Could be a 3Fe-4S cluster-containing protein. (97 aa)
ttrATetrathionate reductase complex, subunit A; Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrA is the catalytic subunit. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1020 aa)
ttrBTetrathionate reductase complex, subunit B; Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrB is probably involved in transfer of electrons from TtrC to TtrA. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut. (250 aa)
ydhDPutative glutaredoxin protein; Similar to E. coli orf, hypothetical protein (AAC74726.1); Blastp hit to AAC74726.1 (115 aa), 97% identity in aa 1 - 115; Belongs to the glutaredoxin family. Monothiol subfamily. (115 aa)
nthEndonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. (211 aa)
rsxCPutative respiratory-chain NADH dehydrogenase; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR; Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily. (735 aa)
ydgMPutative alternative beta subunit of Na+-transporting NADH:ubiquinone oxidoreductase; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR; Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily. (192 aa)
fumAFumarase A; 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)
STM1498Similar to E. coli putative oxidoreductase, major subunit (AAC74660.1); Blastp hit to AAC74660.1 (808 aa), 91% identity in aa 2 - 807; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (811 aa)
STM1499Putative dimethyl sulphoxide reductase, chain A1; Similar to E. coli putative oxidoreductase, major subunit (AAC74659.1); Blastp hit to AAC74659.1 (808 aa), 86% identity in aa 1 - 808; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (813 aa)
STM1539Similar to E. coli hydrogenase-1 small subunit (AAC74057.1); Blastp hit to AAC74057.1 (372 aa), 72% identity in aa 1 - 371. (367 aa)
fdnHFormate dehydrogenase-N, Fe-S beta subunit; The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. (294 aa)
fdnGPutative molybdopterin oxidoreductases; Similar to E. coli formate dehydrogenase-N, nitrate-inducible, alpha subunit (AAD13438.1); Blastp hit to AAD13438.1 (1015 aa), 93% identity in aa 1 - 1015; contains selenocysteine tRNA suppressible codon. (1015 aa)
narZSimilar to E. coli cryptic nitrate reductase 2, alpha subunit (AAC74550.1); Blastp hit to AAC74550.1 (1246 aa), 90% identity in aa 1 - 1246; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1246 aa)
nifJSimilar to E. coli putative oxidoreductase, Fe-S subunit (AAC74460.1); Blastp hit to AAC74460.1 (1174 aa), 92% identity in aa 1 - 1174. (1174 aa)
ydaOPutative ATPase; Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. Belongs to the TtcA family. (311 aa)
fnrTranscriptional regulator; 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 (By similarity). (264 aa)
acnAAconitate hydratase 1; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2- methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The (2S,3S)-2-methylcitrate (2-MC) is a very poor substrate. The apo form of AcnA functions as a RNA-binding regulatory protein (By similarity). Belongs to the aconitase/IPM isomerase family. (891 aa)
narGSimilar to E. coli nitrate reductase 1, alpha subunit (AAC74308.1); Blastp hit to AAC74308.1 (1247 aa), 95% identity in aa 1 - 1247; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1247 aa)
STM1786Similar to E. coli hydrogenase-1 small subunit (AAC74057.1); Blastp hit to AAC74057.1 (372 aa), 92% identity in aa 1 - 372. (372 aa)
sdaASimilar to E. coli L-serine deaminase (AAC74884.1); Blastp hit to AAC74884.1 (454 aa), 94% identity in aa 1 - 454; Belongs to the iron-sulfur dependent L-serine dehydratase family. (454 aa)
edd6-phosphogluconate dehydratase; Catalyzes the dehydration of 6-phospho-D-gluconate to 2- dehydro-3-deoxy-6-phospho-D-gluconate; Belongs to the IlvD/Edd family. (603 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)
phsBHydrogen sulfide production iron-sulfur subunit; Component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor. Proton motive force (PMF) is required to drive transmembrane electron transfer within the reductase. The PhsB subunit transfers electrons between PhsC and PhsA. (192 aa)
phsAHydrogen sulfide production membrane anchoring protein; Component of the PhsABC thiosulfate reductase that catalyzes the reduction of thiosulfate to sulfite and hydrogen sulfide, with menaquinol as the sole electron donor. Proton motive force (PMF) is required to drive transmembrane electron transfer within the reductase. The PhsA subunit contains the active site molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor. (758 aa)
rfbI-2CDP-6-deoxy-delta3,4-glucoseen reductase; LPS side chain defect; RFBI protein. (SW:RFBI_SALTY). (330 aa)
mrpPutative ATP-binding protein; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP. Both activities are required for function in vivo, but the ability to hydrolyze ATP is not necessary for Fe-S cluster transfer. (369 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)
STM2196Putative D-serine dehydratase; Similar to E. coli L-serine deaminase (AAC74884.1); Blastp hit to AAC74884.1 (454 aa), 48% identity in aa 1 - 452; Belongs to the iron-sulfur dependent L-serine dehydratase family. (455 aa)
napAPeriplasmic large subunit nitrate reductase; Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite. (828 aa)
napFFerredoxin-type protein; Could be involved in the maturation of NapA, the catalytic subunit of the periplasmic nitrate reductase, before its export into the periplasm; Belongs to the NapF family. (163 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)
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)
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)
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)
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)
gcpEPutative protein; Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME- 2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Belongs to the IspG family. (372 aa)
yfgBPutative Fe-S-cluster redox enzyme; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family. (388 aa)
STM2530Similar to E. coli putative oxidoreductase, major subunit (AAC74660.1); Blastp hit to AAC74660.1 (808 aa), 42% identity in aa 15 - 807; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (801 aa)
nifSPutative aminotransferase class-V; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate; Belongs to the class-V pyridoxal-phosphate-dependent [...] (404 aa)
yfhPHypothetical protein; Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins. (164 aa)
asrAAnaerobic sulfide reductase; Electron transfer protein for anaerobic sulfite reductase subunit A. (347 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)
cysINADPH dependent sulfite reductase, alpha subunit; Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate; Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (570 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)
nrdGAnaerobic ribonucleotide reductase activating protein; Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine; Belongs to the organic radical-activating enzymes family. (154 aa)
yjeBPutative negative regulator; Nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress. May require iron for activity. Represses hmp expression under conditions of elevated intracellular iron concentrations, in the absence of nitric oxide. (141 aa)
yjeSPutative Fe-S protein; Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr); Belongs to the QueG family. (384 aa)
frdBFumarate reductase; Anaerobic; Fe-S protein subunit; similar to E. coli fumarate reductase, anaerobic, iron-sulfur protein subunit (AAC77113.1); Blastp hit to AAC77113.1 (244 aa), 95% identity in aa 1 - 244; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (244 aa)
yjeKPutative aminomutase; 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) (By similarity). (342 aa)
STM4305Similar to E. coli anaerobic dimethyl sulfoxide reductase subunit A (AAC73980.1); Blastp hit to AAC73980.1 (785 aa), 51% identity in aa 3 - 784; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (783 aa)
fumBFumarase B; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (548 aa)
fdhFFormate dehydrogenase; Similar to E. coli selenopolypeptide subunit of formate dehydrogenase H (AAD13462.1); Blastp hit to AAD13462.1 (715 aa), 97% identity in aa 1 - 714; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (715 aa)
soxRRedox-sensing transcriptional activator SoxR; Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron- sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress (By similarity). (152 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)
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)
fdoGSimilar to E. coli formate dehydrogenase-O, major subunit (AAD13456.1); Blastp hit to AAD13456.1 (1016 aa), 93% identity in aa 1 - 1016. (1016 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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