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cofH | FO synthase subunit 2; Catalyzes the radical-mediated synthesis of 5-amino-5-(4- hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D- ribitylamino)uracil and L-tyrosine. (398 aa) | ||||
ilvD | KEGG: ava:Ava_0023 dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; Belongs to the IlvD/Edd family. (561 aa) | ||||
queE | Conserved hypothetical protein; 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. (207 aa) | ||||
cofG | FO synthase subunit 1; Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8- hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D- ribitylimino)-5,6-dihydrouracil. (319 aa) | ||||
moaA | GTP cyclohydrolase subunit MoaA; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (328 aa) | ||||
miaB | tRNA-i(6)A37 thiotransferase enzyme MiaB; 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. (451 aa) | ||||
psaC | 4Fe-4S ferredoxin, iron-sulfur binding; Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized a [...] (81 aa) | ||||
Tery_0579 | 4Fe-4S ferredoxin, iron-sulfur binding; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (75 aa) | ||||
Tery_0664 | Aconitase; PFAM: aconitate hydratase-like aconitate hydratase 2; KEGG: syn:slr0665 aconitate hydratase; Belongs to the aconitase/IPM isomerase family. (869 aa) | ||||
Tery_0677 | TIGRFAM: glutaredoxin-like protein; PFAM: glutaredoxin; KEGG: syn:slr1846 monothiol glutaredoxin; Belongs to the glutaredoxin family. Monothiol subfamily. (111 aa) | ||||
Tery_1068 | Assimilatory nitrite reductase (ferredoxin) precursor; PFAM: nitrite/sulfite reductase, hemoprotein beta-component, ferrodoxin-like nitrite and sulphite reductase 4Fe-4S region; KEGG: ana:alr0607 nitrite reductase. (510 aa) | ||||
Tery_1070 | Assimilatory nitrate reductase (ferredoxin) precursor; PFAM: molybdopterin oxidoreductase molydopterin dinucleotide-binding region molybdopterin oxidoreductase Fe4S4 region; KEGG: ava:Ava_4544 molybdopterin oxidoreductase; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. (734 aa) | ||||
Tery_1165 | Protein of unknown function DUF59; Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP; Belongs to the Mrp/NBP35 ATP-binding proteins family. (356 aa) | ||||
Tery_1194 | Coproporphyrinogen III oxidase, anaerobic; 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. (421 aa) | ||||
chlN | Light-independent protochlorophyllide reductase, N subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. (465 aa) | ||||
chlL | Light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. (288 aa) | ||||
Tery_1567 | Ferredoxin thioredoxin reductase, beta chain; Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin. (121 aa) | ||||
ndhI | NADH-plastoquinone oxidoreductase, I subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient; Belongs to the complex I 23 kDa subunit family. (209 aa) | ||||
petC | Rieske (2Fe-2S) region; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. Belongs to the Rieske iron-sulfur protein family. (179 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. (292 aa) | ||||
nadA | Quinolinate synthetase A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. (323 aa) | ||||
thiC | Thiamine biosynthesis protein ThiC; 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. Belongs to the ThiC family. (486 aa) | ||||
Tery_2728 | TIGRFAM: homoaconitate hydratase family protein 3-isopropylmalate dehydratase; PFAM: aconitate hydratase-like; KEGG: cme:CMS078C 3-isopropylmalate dehydratase Pfam: Aconitase; Belongs to the aconitase/IPM isomerase family. (439 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; Belongs to the radical SAM superfamily. RlmN family. (345 aa) | ||||
nth | DNA-(apurinic or apyrimidinic site) lyase / 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. (217 aa) | ||||
lipA-2 | 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. (307 aa) | ||||
ndhK | NADH-quinone oxidoreductase, B subunit; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family. (240 aa) | ||||
bioB | Biotin synthase; 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. (370 aa) | ||||
Tery_3544 | TIGRFAM: sulfite reductase, ferredoxin dependent; PFAM: nitrite/sulfite reductase, hemoprotein beta-component, ferrodoxin-like nitrite and sulphite reductase 4Fe-4S region; KEGG: ava:Ava_5043 sulfite reductase, ferredoxin dependent. (902 aa) | ||||
purF | Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. (493 aa) | ||||
Tery_3726 | KEGG: ava:Ava_0523 succinate dehydrogenase; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: ferredoxin; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (346 aa) | ||||
rimO | MiaB-like tRNA modifying enzyme YliG; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (441 aa) | ||||
chlB | Light-independent protochlorophyllide reductase, B subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. (508 aa) | ||||
iscS | 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 atoms from cysteine 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; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily. (389 aa) | ||||
Tery_4133 | TIGRFAM: nitrogenase cofactor biosynthesis protein NifB; PFAM: Dinitrogenase iron-molybdenum cofactor biosynthesis Radical SAM; KEGG: ava:Ava_3912 nitrogenase cofactor biosynthesis protein NifB. (489 aa) | ||||
Tery_4134 | Aminotransferase, class V; Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. (400 aa) | ||||
nifH | Nitrogenase iron protein subunit NifH; The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein. (296 aa) | ||||
nifK | Nitrogenase molybdenum-iron protein beta chain; This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation; Belongs to the NifD/NifK/NifE/NifN family. (512 aa) | ||||
ispH | Hydroxymethylbutenyl pyrophosphate reductase; 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. Belongs to the IspH family. (401 aa) | ||||
ispG | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase; 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. (406 aa) | ||||
psaB | Photosystem I core protein PsaB; PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6. (738 aa) | ||||
psaA | Photosystem I core protein PsaA; PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6. (753 aa) | ||||
queG | Putative iron-sulfur cluster binding 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. (308 aa) |