node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SCM57714.1 | SCM58379.1 | ING2E5A_1474 | ING2E5A_1783 | Putative protein {ECO:0000313|EMBL:AFL85551,1}; tr|I3Z8I3|I3Z8I3_BELBD;evalue=3e-070; PctID=56.90; score=271. | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | 0.740 |
SCM58377.1 | SCM58379.1 | ING2E5A_1782 | ING2E5A_1783 | Putative protein {ECO:0000313|EMBL:EIY86314,1}; tr|I9JHS5|I9JHS5_9BACE;evalue=2e-034; PctID=82.56; score=150. | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | 0.641 |
SCM58377.1 | SCM58381.1 | ING2E5A_1782 | ING2E5A_1784 | Putative protein {ECO:0000313|EMBL:EIY86314,1}; tr|I9JHS5|I9JHS5_9BACE;evalue=2e-034; PctID=82.56; score=150. | Putative protein {ECO:0000313|EMBL:CDB72153,1}; tr|R6KAJ0|R6KAJ0_9BACE;evalue=3e-036; PctID=50.68; score=157. | 0.821 |
SCM58377.1 | SCM58383.1 | ING2E5A_1782 | ING2E5A_1785 | Putative protein {ECO:0000313|EMBL:EIY86314,1}; tr|I9JHS5|I9JHS5_9BACE;evalue=2e-034; PctID=82.56; score=150. | Putative protein {ECO:0000313|EMBL:EIZ00658,1}; tr|I9BLA5|I9BLA5_BACFG;evalue=5e-073; PctID=64.19; score=280. | 0.753 |
SCM58377.1 | SCM58384.1 | ING2E5A_1782 | ING2E5A_1786 | Putative protein {ECO:0000313|EMBL:EIY86314,1}; tr|I9JHS5|I9JHS5_9BACE;evalue=2e-034; PctID=82.56; score=150. | UPF0718 protein; sp|Q58004|Y584_METJA;evalue=1e-039; PctID=50.88; score=164. | 0.689 |
SCM58379.1 | SCM57714.1 | ING2E5A_1783 | ING2E5A_1474 | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | Putative protein {ECO:0000313|EMBL:AFL85551,1}; tr|I3Z8I3|I3Z8I3_BELBD;evalue=3e-070; PctID=56.90; score=271. | 0.740 |
SCM58379.1 | SCM58377.1 | ING2E5A_1783 | ING2E5A_1782 | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | Putative protein {ECO:0000313|EMBL:EIY86314,1}; tr|I9JHS5|I9JHS5_9BACE;evalue=2e-034; PctID=82.56; score=150. | 0.641 |
SCM58379.1 | SCM58381.1 | ING2E5A_1783 | ING2E5A_1784 | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | Putative protein {ECO:0000313|EMBL:CDB72153,1}; tr|R6KAJ0|R6KAJ0_9BACE;evalue=3e-036; PctID=50.68; score=157. | 0.891 |
SCM58379.1 | SCM58383.1 | ING2E5A_1783 | ING2E5A_1785 | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | Putative protein {ECO:0000313|EMBL:EIZ00658,1}; tr|I9BLA5|I9BLA5_BACFG;evalue=5e-073; PctID=64.19; score=280. | 0.913 |
SCM58379.1 | SCM58384.1 | ING2E5A_1783 | ING2E5A_1786 | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | UPF0718 protein; sp|Q58004|Y584_METJA;evalue=1e-039; PctID=50.88; score=164. | 0.943 |
SCM58379.1 | SCM59820.1 | ING2E5A_1783 | ING2E5A_3028 | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | 2-Cys peroxiredoxin BAS1-like, chloroplastic; May be an antioxidant enzyme particularly in the developing shoot and photosynthesizing leaf. Involved in the detoxification of alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system (By similarity). H(2)O(2), and the oxidized Cys-126 (probably Cys-SOH) rapidly reacts with Cys-248-SH of the other subunit to form an intermolecular disulfide. This disulfide might subsequently be reduced by thioredoxin (By similarity). ProRule:PRU00691}. Sequence=AAG40040.2; Type=Erroneous initiation; Note=Translation N-terminal [...] | 0.822 |
SCM58379.1 | acoL | ING2E5A_1783 | ING2E5A_1492 | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | Dihydrolipoyl dehydrogenase; sp|O34324|DLDH3_BACSU;evalue=2e-078; PctID=35.60; score=293. | 0.670 |
SCM58379.1 | dsbD | ING2E5A_1783 | ING2E5A_1790 | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | Thiol:disulfide interchange protein DsbD {ECO:0000255|HAMAP-Rule:MF_00399}; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. disulfide + NAD(P)H. Rule:MF_00399}; Multi-pass membrane protein Rule:MF_00399}; sp|Q7VMZ4|DSBD_HAEDU;evalue=7e-011; PctID=25.94; score=69.7. | 0.783 |
SCM58379.1 | msrA | ING2E5A_1783 | ING2E5A_1837 | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | Peptide methionine sulfoxide reductase MsrA {ECO:0000255|HAMAP-Rule:MF_01401}; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.913 |
SCM58379.1 | pdhD1 | ING2E5A_1783 | ING2E5A_1159 | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. protein N(6)-(lipoyl)lysine + NADH. Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit; oxidoreductase family; sp|P11959|DLDH1_GEOSE;evalue=1e-075; PctID=38.50; score=284. | 0.639 |
SCM58381.1 | SCM58377.1 | ING2E5A_1784 | ING2E5A_1782 | Putative protein {ECO:0000313|EMBL:CDB72153,1}; tr|R6KAJ0|R6KAJ0_9BACE;evalue=3e-036; PctID=50.68; score=157. | Putative protein {ECO:0000313|EMBL:EIY86314,1}; tr|I9JHS5|I9JHS5_9BACE;evalue=2e-034; PctID=82.56; score=150. | 0.821 |
SCM58381.1 | SCM58379.1 | ING2E5A_1784 | ING2E5A_1783 | Putative protein {ECO:0000313|EMBL:CDB72153,1}; tr|R6KAJ0|R6KAJ0_9BACE;evalue=3e-036; PctID=50.68; score=157. | Thioredoxin {ECO:0000250|UniProtKB:O26981}; Does not function as a glutathione-disulfide oxidoreductase in the presence of glutathione and glutathione reductase (By similarity). Has low thioredoxin activity in vitro (By similarity); sp|Q58001|THIRX_METJA;evalue=6e-011; PctID=44.59; score=66.2. | 0.891 |
SCM58381.1 | SCM58383.1 | ING2E5A_1784 | ING2E5A_1785 | Putative protein {ECO:0000313|EMBL:CDB72153,1}; tr|R6KAJ0|R6KAJ0_9BACE;evalue=3e-036; PctID=50.68; score=157. | Putative protein {ECO:0000313|EMBL:EIZ00658,1}; tr|I9BLA5|I9BLA5_BACFG;evalue=5e-073; PctID=64.19; score=280. | 0.951 |
SCM58381.1 | SCM58384.1 | ING2E5A_1784 | ING2E5A_1786 | Putative protein {ECO:0000313|EMBL:CDB72153,1}; tr|R6KAJ0|R6KAJ0_9BACE;evalue=3e-036; PctID=50.68; score=157. | UPF0718 protein; sp|Q58004|Y584_METJA;evalue=1e-039; PctID=50.88; score=164. | 0.882 |
SCM58383.1 | SCM58377.1 | ING2E5A_1785 | ING2E5A_1782 | Putative protein {ECO:0000313|EMBL:EIZ00658,1}; tr|I9BLA5|I9BLA5_BACFG;evalue=5e-073; PctID=64.19; score=280. | Putative protein {ECO:0000313|EMBL:EIY86314,1}; tr|I9JHS5|I9JHS5_9BACE;evalue=2e-034; PctID=82.56; score=150. | 0.753 |