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cbiA/cobB cbiA/cobB Mbur_1038 Mbur_1038 Mbur_1037 Mbur_1037 Mbur_1036 Mbur_1036 cbiXS cbiXS mttB mttB mer mer mcrA mcrA mcrG mcrG mcrC mcrC mcrD mcrD mcrB mcrB Mbur_2436 Mbur_2436 Mbur_2437 Mbur_2437 Mbur_2438 Mbur_2438 Mbur_2439 Mbur_2439 cdhE cdhE cdhD cdhD cdhC cdhC cdhB cdhB cdhA cdhA mtmC-2 mtmC-2 hdrA hdrA Mbur_0808 Mbur_0808 mch mch mtd mtd fmdB fmdB fmdD fmdD fmdC fmdC Mbur_0335 Mbur_0335 Mbur_0337 Mbur_0337 Mbur_0336 Mbur_0336 mtrB mtrB mtrC mtrC mtrD mtrD mtrA mtrA mtrF mtrF mtrG mtrG mtrH mtrH hdrB hdrB mtrE mtrE ftr ftr mtbA-2 mtbA-2 mtbC-3 mtbC-3 mttB-2 mttB-2 hdrC hdrC mtbC-2 mtbC-2 fpoH fpoH mtmC mtmC Mbur_0813 Mbur_0813 Mbur_0811 Mbur_0811
Nodes:
Network nodes represent proteins
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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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cbiA/cobBCobyrinic acid a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. (489 aa)
Mbur_1038Nitrogenase iron protein; Evidence code ER2. (264 aa)
Mbur_1037Protein containing oxidoreductase/nitrogenase, component 1-like domain; Evidence code ER4. (370 aa)
Mbur_1036Protein containing Mur ligase middle domain-like central region; Evidence code ER4. (454 aa)
cbiXSSirohydrochlorin cobaltochelatase; Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni- sirohydrochlorin. (131 aa)
mttBTrimethylamine methyltransferase; Evidence code ER3; Belongs to the trimethylamine methyltransferase family. (484 aa)
merCoenzyme F420-dependent N(5),N(10)-methylenetetrahydromethanopterin reductase; Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT; Belongs to the mer family. (328 aa)
mcrAMethyl-coenzyme M reductase, subunit alpha; Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis. (572 aa)
mcrGMethyl-coenzyme M reductase, subunit gamma; Evidence code ER2. (248 aa)
mcrCHighly conserved methyl-coenzyme M reductase operon protein C with unknown function; Evidence code ER4. (200 aa)
mcrDConserved methyl-coenzyme M reductase operon protein D with unknown function; Evidence code ER4. (162 aa)
mcrBMethyl-coenzyme M reductase, subunit beta; Evidence code ER2. (434 aa)
Mbur_2436CoB-CoM heterodisulfide reductase, subunit E; Evidence code ER2. (268 aa)
Mbur_2437CoB-CoM heterodisulfide reductase, subunit D; Evidence code ER2. (415 aa)
Mbur_2438Protein of unknown function DUF116; Evidence code ER4. (211 aa)
Mbur_2439Protein of unknown function DUF116; Evidence code ER4. (208 aa)
cdhEAcetyl-CoA decarbonylase/synthase complex gamma subunit; Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. (468 aa)
cdhDAcetyl-CoA decarbonylase/synthase complex delta subunit; Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. Probably maintains the overall quaternary structure of the ACDS complex. (439 aa)
cdhCAcetyl-CoA decarbonylase/synthase complex beta subunit; Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon complex generates CO from CO(2), while the beta subunit (this protein) combines the CO with CoA and a methyl group to form acetyl-CoA. The methyl group, which is incorporated into acetyl-CoA, is transferred to the beta subunit by a corrinoid iron- sulfur protein (the gamma-delta complex). (470 aa)
cdhBAcetyl-CoA decarbonylase/synthase complex epsilon subunit; Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. The precise role of the epsilon subunit is unclear; it may have a stabilizing role within the alpha(2)epsilon(2) component and/or be involved in electron transfer to FAD during a potential FAD- mediated CO oxidation. (171 aa)
cdhAAcetyl-CoA decarbonylase/synthase complex alpha subunit 2; Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase. (802 aa)
mtmC-2Monomethylamine corrinoid protein; Evidence code ER2. (217 aa)
hdrACoB--CoM heterodisulfide reductase iron-sulfur subunit A; Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B). (786 aa)
Mbur_0808Methanol-specific methylcobalamin:CoM methyltransferase; Evidence code ER2. (338 aa)
mchMethenyltetrahydromethanopterin cyclohydrolase; Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl- H(4)MPT. (320 aa)
mtdMethylenetetrahydromethanopterin dehydrogenase; Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT. (273 aa)
fmdBMolybdenum formylmethanofuran dehydrogenase subunit B; Evidence code ER2. (435 aa)
fmdDMolybdenum formylmethanofuran dehydrogenase subunit D; Evidence code ER2. (129 aa)
fmdCMolybdenum formylmethanofuran dehydrogenase subunit C; Evidence code ER2. (269 aa)
Mbur_0335Formylmethanofuran dehydrogenase subunit G; Evidence code ER3. (152 aa)
Mbur_0337Formylmethanofuran dehydrogenase subunit D; Evidence code ER3. (132 aa)
Mbur_0336Formylmethanofuran dehydrogenase subunit B; Evidence code ER3. (414 aa)
mtrBTetrahydromethanopterin S-methyltransferase subunit B; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. (107 aa)
mtrCTetrahydromethanopterin S-methyltransferase subunit C; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. (269 aa)
mtrDTetrahydromethanopterin S-methyltransferase subunit D; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. (239 aa)
mtrATetrahydromethanopterin S-methyltransferase subunit A; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step; Belongs to the MtrA family. (241 aa)
mtrFTetrahydromethanopterin S-methyltransferase subunit F; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. (79 aa)
mtrGTetrahydromethanopterin S-methyltransferase subunit G; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. (75 aa)
mtrHTetrahydromethanopterin S-methyltransferase subunit H; Evidence code ER2. (318 aa)
hdrBCoB--CoM heterodisulfide reductase subunit B; Evidence code ER2. (306 aa)
mtrETetrahydromethanopterin S-methyltransferase subunit E; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step; Belongs to the MtrE family. (301 aa)
ftrFormylmethanofuran--tetrahydromethanopterin formyltransferase; Catalyzes the transfer of a formyl group from 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) so as to produce formylmethanofuran (formyl-MFR) and tetrahydromethanopterin (H(4)MPT). (297 aa)
mtbA-2Methylamine-specific methylcobamide:CoM methyltransferase; Evidence code ER2. (344 aa)
mtbC-3Dimethylamine corrinoid protein; Evidence code ER2. (168 aa)
mttB-2Trimethylamine methyltransferase; Catalyzes the transfer of a methyl group from trimethylamine to the corrinoid cofactor of MttC. (497 aa)
hdrCCoB--CoM heterodisulfide reductase iron-sulfur subunit C; Evidence code ER2. (164 aa)
mtbC-2Dimethylamine corrinoid protein; Evidence code ER2. (251 aa)
fpoHF420H2 dehydrogenase subunit H; FPO shuttles electrons from F(420)H(2), via FAD and iron- sulfur (Fe-S) centers, to quinones in the F(420)H(2):heterodisulfide oxidoreduction chain. The immediate electron acceptor for the enzyme in this species is believed to be methanophenazine. Couples the redox reaction to proton translocation (for every two electrons transferred, 0.9 hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (344 aa)
mtmCMonomethylamine corrinoid protein; Evidence code ER2. (217 aa)
Mbur_0813Methanol corrinoid protein; Evidence code ER2. (256 aa)
Mbur_0811Methanol corrinoid protein; Evidence code ER2. (254 aa)
Your Current Organism:
Methanococcoides burtonii
NCBI taxonomy Id: 259564
Other names: M. burtonii DSM 6242, Methanococcoides burtonii DSM 6242, Methanococcoides burtonii str. DSM 6242
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