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lpg2536 | Ferredoxin reductase. (318 aa) | ||||
lpg0899 | A/G specific adenine glycosylase; Adenine glycosylase active on G-A mispairs. (355 aa) | ||||
lpg1044 | Oxidoreductase, FAD-binding. (657 aa) | ||||
lpg1170 | Pyruvate formate lyase-activating enzyme PflA. (364 aa) | ||||
lpg1276 | Electron transferring flavoprotein dehydrogenase; Accepts electrons from ETF and reduces ubiquinone. (543 aa) | ||||
lpg0288 | L-lysine 2,3-aminomutase, radical SAM domain protein. (326 aa) | ||||
nadA | Quinolinate synthetase A (NadA); Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. (447 aa) | ||||
edd | 6-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. (612 aa) | ||||
miaB | tRNA thiotransferase; 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. (447 aa) | ||||
nth | Endonuclease 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) | ||||
lpg2881 | Iron-sulfur cluster binding protein; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily. (204 aa) | ||||
grlA | Glutaredoxin-related protein; Belongs to the glutaredoxin family. Monothiol subfamily. (89 aa) | ||||
erpA | Hypothetical protein; Required for insertion of 4Fe-4S clusters for at least IspG. (130 aa) | ||||
rlmD | 23S rRNA (uracil-5-)methyltransferase RumA; 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. (444 aa) | ||||
bioB | Biotin synthase BioB; 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. (315 aa) | ||||
prpD | 2-methylcitrate dehydratase PrpD. (490 aa) | ||||
rlmN | Radical SAM enzyme, Cfr family; 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. (386 aa) | ||||
lpg1634 | Oxidase. (1000 aa) | ||||
acnA | Aconitate hydratase; Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis- aconitate. The apo form of AcnA functions as a RNA-binding regulatory protein. Could catalyze the hydration of 2-methyl-cis- aconitate to yield (2R,3S)-2-methylisocitrate (By similarity). (891 aa) | ||||
ydiC | HesB family protein; Belongs to the HesB/IscA family. (122 aa) | ||||
lpg1745 | NifU family iron binding protein, [Fe-S] cluster formation/repair protein IscU, HesB. (127 aa) | ||||
mrp | ATPase (Mrp); Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. (357 aa) | ||||
lpg1923 | Ferredoxin II (4Fe-4S); Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (111 aa) | ||||
queE | Radical activating enzyme; 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. (217 aa) | ||||
lpg2218 | Choline monooxygenase. (363 aa) | ||||
lpg2354 | (oxygen-independent) coproporphyrinogen III 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. (375 aa) | ||||
lpg2468 | Sulfhydrogenase delta subunit. (261 aa) | ||||
hydG-2 | Hydrogenase/sulfur reductase gamma subunit. (281 aa) | ||||
lpg2470 | Cytochrome c3 hydrogenase alpha (or beta) chain. (403 aa) | ||||
lpg2534 | Hypothetical protein; Transcription factors / DNA binding proteins. (143 aa) | ||||
sdhB-2 | Succinate dehydrogenase iron-sulfur protein subunit B. (240 aa) | ||||
lpg0600 | Rrf2 family protein. (153 aa) | ||||
ycf24 | ABC transporter, permease. (482 aa) | ||||
lpg0605 | Nitrogen fixation protein (Fe-S cluster formation) NifU. (149 aa) | ||||
lpg0606 | Metal-sulfur cluster biosynthetic enzyme. (123 aa) | ||||
rimO | Fe-S oxidoreductase; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (435 aa) | ||||
ttcA | Hypothetical protein; 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. (283 aa) | ||||
lipA | Lipoic acid synthetase; 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. (329 aa) | ||||
sda-2 | L-serine dehydratase (iron, sulfur-dependent); Belongs to the iron-sulfur dependent L-serine dehydratase family. (458 aa) | ||||
yrbA | Hypothetical BolA like protein; Belongs to the BolA/IbaG family. (81 aa) | ||||
petA | Ubiquinol-cytochrome c reductase, iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (208 aa) | ||||
lpg2708 | Ferredoxin 2Fe-2S protein. (71 aa) | ||||
queH | Hypothetical 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). (220 aa) | ||||
nuoI | NADH dehydrogenase I, I subunit; 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. (166 aa) | ||||
nuoG | NADH dehydrogenase I, G subunit; 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. Belongs to the complex I 75 kDa subunit family. (783 aa) | ||||
nuoF | NADH dehydrogenase I, F subunit; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (428 aa) | ||||
lpg2785 | NADH dehydrogenase I, E subunit. (167 aa) | ||||
nuoB2 | NADH dehydrogenase I, B subunit; 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 (By similarity). (158 aa) |