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bioB bioB acnA acnA cysI cysI AEI05844.1 AEI05844.1 lipA lipA rimO rimO moaA moaA narG narG ispH2 ispH2 fdhA2 fdhA2 kamA kamA hemN hemN AEI07612.1 AEI07612.1 AEI07613.1 AEI07613.1 fbiC fbiC citB citB AEI05843.1 AEI05843.1 AEI05834.1 AEI05834.1 mutY mutY queE queE thiC thiC fdoG fdoG AEI07488.1 AEI07488.1 AEI07381.1 AEI07381.1 nuoF3 nuoF3 fdhA3 fdhA3 fumA fumA AEI07079.1 AEI07079.1 AEI06885.1 AEI06885.1 nuoB nuoB nuoF2 nuoF2 nuoG nuoG nuoI nuoI sufB sufB AEI05693.1 AEI05693.1 nadA nadA AEI05902.1 AEI05902.1 fdhA1 fdhA1 queH queH nuoF1 nuoF1 glcF glcF ispH1 ispH1 cysH cysH AEI05172.1 AEI05172.1 ispG ispG AEI04985.1 AEI04985.1 leuC leuC sdhB sdhB rlmN rlmN AEI04852.1 AEI04852.1 nth nth miaB miaB
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
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textmining
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bioBBiotin 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. (347 aa)
acnAAconitate hydratase AcnA; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. (906 aa)
cysISulfite reductase [NADPH] hemoprotein beta-componentCysI; 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. (582 aa)
AEI05844.1Electron transfer flavoprotein-ubiquinone oxidoreductase; Accepts electrons from ETF and reduces ubiquinone. (557 aa)
lipALipoyl synthase LipA; 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. (322 aa)
rimORibosomal protein S12 methylthiotransferase RimO; Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein S12; Belongs to the methylthiotransferase family. RimO subfamily. (440 aa)
moaAMolybdenum cofactor biosynthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (343 aa)
narGRespiratory nitrate reductase alpha chain NarG; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1248 aa)
ispH24-hydroxy-3-methylbut-2-enyl diphosphate reductase IspH; 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. (322 aa)
fdhA2Formate dehydrogenase subunit alpha; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (923 aa)
kamAL-lysine 2,3-aminomutase KamA. (357 aa)
hemNOxygen-independent coproporphyrinogen-III oxidase HemN; Belongs to the anaerobic coproporphyrinogen-III oxidase family. (458 aa)
AEI07612.1Peptidase U32. (322 aa)
AEI07613.1Peptidase U32. (325 aa)
fbiCFO synthase FbiC. (804 aa)
citBCitrate utilization protein B. (383 aa)
AEI05843.1Putative uracil-DNA glycosylase. (271 aa)
AEI05834.1Radical SAM domain protein. (391 aa)
mutYA/G-specific adenine DNA glycosylase MutY; Adenine glycosylase active on G-A mispairs. (371 aa)
queEHypothetical 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. (210 aa)
thiCPhosphomethylpyrimidine synthase 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. (632 aa)
fdoGFormate dehydrogenase-O major subunit FdoG; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (1024 aa)
AEI07488.1uracil-DNA glycosylase family protein. (209 aa)
AEI07381.1NADH-quinone oxidoreductase family protein. (319 aa)
nuoF3NADH-quinone oxidoreductase subunit F. (620 aa)
fdhA3Formate dehydrogenase alpha subunit FdhA; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (687 aa)
fumAFumarate hydratase class I, aerobic; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family. (548 aa)
AEI07079.1Dihydrodipicolinate synthase. (334 aa)
AEI06885.1uracil-DNA glycosylase family protein. (238 aa)
nuoBNADH-quinone oxidoreductase subunit 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. (198 aa)
nuoF2NADH-quinone oxidoreductase subunit F 1; 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. (441 aa)
nuoGNADH-quinone oxidoreductase, subunit G; 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. (690 aa)
nuoINADH-quinone oxidoreductase subunit 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. (162 aa)
sufBFeS assembly protein SufB. (499 aa)
AEI05693.1Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (113 aa)
nadAQuinolinate synthase A; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. (368 aa)
AEI05902.1Putative RNA methyltransferase; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. (413 aa)
fdhA1Formate dehydrogenase alpha subunit FdhA. (1026 aa)
queHHypothetical 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). (222 aa)
nuoF1NADH-quinone oxidoreductase subunit F. (570 aa)
glcFGlycolate oxidase, iron-sulfur subunit GlcF. (449 aa)
ispH14-hydroxy-3-methylbut-2-enyl diphosphate reductase IspH; 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. (333 aa)
cysHPhosphoadenosine phosphosulfate reductase CysH; Reduction of activated sulfate into sulfite. (249 aa)
AEI05172.1Ferredoxin; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (112 aa)
ispG4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG; 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. (435 aa)
AEI04985.1Putative 2-methylthioadenine synthase. (420 aa)
leuC3-isopropylmalate dehydratase large subunit LeuC; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (470 aa)
sdhBSuccinate dehydrogenase iron-sulfur subunit SdhB; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (260 aa)
rlmNRibosomal RNA large subunit methyltransferase N; 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. (404 aa)
AEI04852.1Oxygen-independent coproporphyrinogen; 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. (385 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. (249 aa)
miaB(dimethylallyl)adenosine tRNA methylthiotransferase 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. (473 aa)
Your Current Organism:
Oligotropha carboxidovorans
NCBI taxonomy Id: 504832
Other names: O. carboxidovorans OM5, Oligotropha carboxidovorans OM5, Oligotropha carboxidovorans str. OM5, Oligotropha carboxidovorans strain OM5
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