STRINGSTRING
glcB glcB AGB43259.1 AGB43259.1 AGB43275.1 AGB43275.1 AGB43277.1 AGB43277.1 AGB43454.1 AGB43454.1 mdh mdh sucC sucC sucD sucD AGB43542.1 AGB43542.1 AGB43565.1 AGB43565.1 AGB43566.1 AGB43566.1 AGB43567.1 AGB43567.1 AGB43569.1 AGB43569.1 AGB43788.1 AGB43788.1 AGB43839.1 AGB43839.1 AGB44283.1 AGB44283.1 ubiE ubiE AGB44583.1 AGB44583.1 AGB44624.1 AGB44624.1 AGB44924.1 AGB44924.1 AGB44927.1 AGB44927.1 AGB44982.1 AGB44982.1 AGB44983.1 AGB44983.1 AGB42628.1 AGB42628.1 AGB42640.1 AGB42640.1 AGB42912.1 AGB42912.1 AGB45025.1 AGB45025.1 AGB45026.1 AGB45026.1 AGB45065.1 AGB45065.1 AGB45157.1 AGB45157.1 AGB45158.1 AGB45158.1 AGB45328.1 AGB45328.1 AGB45579.1 AGB45579.1 AGB45638.1 AGB45638.1 AGB45716.1 AGB45716.1 AGB45723.1 AGB45723.1 AGB45815.1 AGB45815.1 AGB45921.1 AGB45921.1 AGB45924.1 AGB45924.1 nuoH nuoH nuoI nuoI nuoK nuoK AGB45929.1 AGB45929.1 AGB45930.1 AGB45930.1 nuoN nuoN sucD-2 sucD-2 sucC-2 sucC-2 AGB46012.1 AGB46012.1 AGB46026.1 AGB46026.1 AGB46192.1 AGB46192.1 AGB46382.1 AGB46382.1 AGB46422.1 AGB46422.1 AGB46423.1 AGB46423.1 AGB46425.1 AGB46425.1 AGB46515.1 AGB46515.1 AGB46664.1 AGB46664.1 AGB46709.1 AGB46709.1 AGB46770.1 AGB46770.1 AGB46956.1 AGB46956.1 fumC fumC AGB47079.1 AGB47079.1 AGB47235.1 AGB47235.1 AGB47385.1 AGB47385.1 AGB47418.1 AGB47418.1 AGB47422.1 AGB47422.1 AGB47426.1 AGB47426.1 AGB47750.1 AGB47750.1 AGB47789.1 AGB47789.1 AGB47860.1 AGB47860.1 AGB47863.1 AGB47863.1 AGB48273.1 AGB48273.1 AGB48274.1 AGB48274.1 AGB48275.1 AGB48275.1
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
Your Input:
glcBMalate synthase G; Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CoA) and glyoxylate to form malate and CoA; Belongs to the malate synthase family. GlcB subfamily. (722 aa)
AGB43259.1Putative periplasmic protein; PFAM: Bacterial protein of unknown function (DUF920). (204 aa)
AGB43275.1PFAM: Cytochrome oxidase subunit II; TIGRFAM: cytochrome d oxidase, subunit II (cydB). (334 aa)
AGB43277.1Cytochrome bd-type quinol oxidase, subunit 1; PFAM: Bacterial Cytochrome Ubiquinol Oxidase. (453 aa)
AGB43454.1Aconitate hydratase 1; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate. (896 aa)
mdhMalate dehydrogenase, NAD-dependent; Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 3 family. (322 aa)
sucCsuccinyl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (397 aa)
sucDsuccinyl-CoA synthetase, alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. (300 aa)
AGB43542.1PFAM: Dehydrogenase E1 component; Transketolase, pyrimidine binding domain; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 component. (994 aa)
AGB43565.1Succinate dehydrogenase, cytochrome b556 subunit; PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit; TIGRFAM: succinate dehydrogenase, cytochrome b556 subunit. (138 aa)
AGB43566.1PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit; TIGRFAM: succinate dehydrogenase, hydrophobic membrane anchor protein. (131 aa)
AGB43567.1PFAM: domain; FAD binding domain; TIGRFAM: succinate dehydrogenase, flavoprotein subunit, E. coli/mitochondrial subgroup; succinate dehydrogenase or fumarate reductase, flavoprotein subunitGram-negative/mitochondrial subgroup; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (611 aa)
AGB43569.1TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (259 aa)
AGB43788.1Hypothetical protein. (130 aa)
AGB43839.1PFAM: Citrate synthase. (380 aa)
AGB44283.1PFAM: Citrate synthase. (283 aa)
ubiEUbiquinone/menaquinone biosynthesis methyltransferase; Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3- methyl-6-methoxy-1,4-benzoquinol (DMQH2). (258 aa)
AGB44583.1PFAM: Cytochrome b(N-terminal)/b6/petB. (210 aa)
AGB44624.1Cytochrome b subunit of the bc complex; 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. (433 aa)
AGB44924.1Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (287 aa)
AGB44927.1PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit I; Belongs to the heme-copper respiratory oxidase family. (565 aa)
AGB44982.1Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III; TIGRFAM: cytochrome o ubiquinol oxidase, subunit III. (228 aa)
AGB44983.1PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome o ubiquinol oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family. (667 aa)
AGB42628.1Trimethylamine:corrinoid methyltransferase; Belongs to the trimethylamine methyltransferase family. (527 aa)
AGB42640.1Formate dehydrogenase, alpha subunit, archaeal-type; PFAM: Molybdopterin oxidoreductase; Molydopterin dinucleotide binding domain; Molybdopterin oxidoreductase Fe4S4 domain; TIGRFAM: formate dehydrogenase, alpha subunit, archaeal-type; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (970 aa)
AGB42912.1PFAM: Cytochrome b(N-terminal)/b6/petB. (190 aa)
AGB45025.1PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome o ubiquinol oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family. (665 aa)
AGB45026.1PFAM: Cytochrome c oxidase subunit III; TIGRFAM: cytochrome o ubiquinol oxidase, subunit III. (208 aa)
AGB45065.1Fe-S oxidoreductase; PFAM: Cysteine-rich domain. (441 aa)
AGB45157.1Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (552 aa)
AGB45158.1PFAM: Succinate dehydrogenase/Fumarate reductase transmembrane subunit; TIGRFAM: succinate dehydrogenase, hydrophobic membrane anchor protein. (129 aa)
AGB45328.1Methylase involved in ubiquinone/menaquinone biosynthesis; PFAM: Methyltransferase domain. (293 aa)
AGB45579.1PFAM: Prokaryotic cytochrome b561. (187 aa)
AGB45638.1Succinate dehydrogenase/fumarate reductase flavoprotein subunit; PFAM: domain; FAD binding domain. (541 aa)
AGB45716.1PFAM: Trimethylamine methyltransferase (MTTB); Belongs to the trimethylamine methyltransferase family. (512 aa)
AGB45723.1Methylase involved in ubiquinone/menaquinone biosynthesis; PFAM: Methyltransferase domain. (280 aa)
AGB45815.1PFAM: Trimethylamine methyltransferase (MTTB); Belongs to the trimethylamine methyltransferase family. (517 aa)
AGB45921.1PFAM: Respiratory-chain NADH dehydrogenase 24 Kd subunit; TIGRFAM: NADH-quinone oxidoreductase, E subunit. (337 aa)
AGB45924.1NADH-quinone oxidoreductase, chain 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. (693 aa)
nuoHNADH:ubiquinone oxidoreductase subunit 1 (chain H); 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. This subunit may bind ubiquinone. (347 aa)
nuoINADH-quinone oxidoreductase, 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. (163 aa)
nuoKNADH:ubiquinone oxidoreductase subunit 11 or 4L (chain K); 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; Belongs to the complex I subunit 4L family. (102 aa)
AGB45929.1Proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH dehydrogenase subunit 5 C-terminus; NADH-Ubiquinone/plastoquinone (complex I), various chains; NADH-Ubiquinone oxidoreductase (complex I), chain 5 N-terminus; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L. (657 aa)
AGB45930.1Proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH-Ubiquinone/plastoquinone (complex I), various chains; NADH-ubiquinone oxidoreductase chain 4, amino terminus; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M. (501 aa)
nuoNProton-translocating NADH-quinone oxidoreductase, chain N; 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; Belongs to the complex I subunit 2 family. (478 aa)
sucD-2succinyl-CoA synthetase, alpha subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. (299 aa)
sucC-2succinyl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (394 aa)
AGB46012.1PFAM: Trimethylamine methyltransferase (MTTB); Belongs to the trimethylamine methyltransferase family. (525 aa)
AGB46026.1PFAM: Trimethylamine methyltransferase (MTTB); Belongs to the trimethylamine methyltransferase family. (525 aa)
AGB46192.1Thiosulfate reductase cytochrome B subunit (membrane anchoring protein); PFAM: Prokaryotic cytochrome b561. (293 aa)
AGB46382.1PFAM: Citrate synthase; TIGRFAM: citrate synthase I (hexameric type); Belongs to the citrate synthase family. (440 aa)
AGB46422.1Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III. (201 aa)
AGB46423.1Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (658 aa)
AGB46425.1Cytochrome c, mono- and diheme variants family; PFAM: Cytochrome c; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit III. (177 aa)
AGB46515.1Oligoketide cyclase/lipid transport protein; PFAM: Polyketide cyclase / dehydrase and lipid transport. (152 aa)
AGB46664.1Putative periplasmic protein; PFAM: Bacterial protein of unknown function (DUF920). (202 aa)
AGB46709.1Putative periplasmic protein; PFAM: Bacterial protein of unknown function (DUF920). (208 aa)
AGB46770.1Isocitrate dehydrogenase, NADP-dependent; PFAM: Isocitrate/isopropylmalate dehydrogenase; TIGRFAM: isocitrate dehydrogenase, NADP-dependent, eukaryotic type; Belongs to the isocitrate and isopropylmalate dehydrogenases family. (403 aa)
AGB46956.1PFAM: Trimethylamine methyltransferase (MTTB); Belongs to the trimethylamine methyltransferase family. (516 aa)
fumCFumarate hydratase, class II; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (465 aa)
AGB47079.1Anaerobic dehydrogenase, typically selenocysteine-containing; PFAM: Molybdopterin oxidoreductase; Molydopterin dinucleotide binding domain; Molybdopterin oxidoreductase Fe4S4 domain; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (702 aa)
AGB47235.1Flavin-dependent dehydrogenase; Accepts electrons from ETF and reduces ubiquinone. (559 aa)
AGB47385.1Putative periplasmic protein; PFAM: Bacterial protein of unknown function (DUF920). (317 aa)
AGB47418.1Heme/copper-type cytochrome/quinol oxidase, subunit 3; PFAM: Cytochrome c oxidase subunit III. (293 aa)
AGB47422.1Cytochrome c oxidase, subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (550 aa)
AGB47426.1Putative periplasmic protein; PFAM: Bacterial protein of unknown function (DUF920); manually curated. (227 aa)
AGB47750.1Putative phosphoesterase, ICC. (249 aa)
AGB47789.1Methylase involved in ubiquinone/menaquinone biosynthesis; PFAM: Methyltransferase domain. (348 aa)
AGB47860.1Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (287 aa)
AGB47863.1PFAM: Cytochrome C and Quinol oxidase polypeptide I; TIGRFAM: cytochrome c oxidase, cbb3-type, subunit I; Belongs to the heme-copper respiratory oxidase family. (542 aa)
AGB48273.1Anaerobic dehydrogenase, typically selenocysteine-containing; PFAM: Molybdopterin oxidoreductase; Molydopterin dinucleotide binding domain; Molybdopterin oxidoreductase Fe4S4 domain; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (975 aa)
AGB48274.1Fe-S-cluster-containing hydrogenase subunit; PFAM: 4Fe-4S binding domain. (244 aa)
AGB48275.1PFAM: DMSO reductase anchor subunit (DmsC). (311 aa)
Your Current Organism:
Mesorhizobium australicum
NCBI taxonomy Id: 754035
Other names: M. australicum WSM2073, Mesorhizobium australicum LMG 24608, Mesorhizobium australicum WSM2073, Mesorhizobium australicum str. WSM2073, Mesorhizobium australicum strain WSM2073, Mesorhizobium sp. WSM 2073, Mesorhizobium sp. WSM2073
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