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dusC dusC fabL fabL hemY hemY yhfP yhfP fabI fabI fadH fadH pyrD pyrD sirC sirC yngJ yngJ yoaI yoaI acdA acdA fadE fadE dhbA dhbA sdhC sdhC sdhA sdhA sdhB sdhB hemN hemN dapB dapB tyrA tyrA dusB dusB ydbM ydbM yfmJ yfmJ mmgC mmgC bacH bacH
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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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experimentally determined
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gene neighborhood
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dusCtRNA-dihydrouridine synthase 2; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the Dus family. (325 aa)
fabLEnoyl-acyl carrier protein reductase III; Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It confers resistance to triclosan. Belongs to the short-chain dehydrogenases/reductases (SDR) family. (250 aa)
hemYProtoporphyrinogen IX and coproporphyrinogen III oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. Also oxidizes the pathway intermediate coproporphyrinogen-III. (470 aa)
yhfPPutative oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily. (330 aa)
fabIEnoyl-acyl carrier protein reductase; Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism. (258 aa)
fadHPutative 2,4-dienoyl-CoA reductase; Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA (By similarity); Belongs to the short-chain dehydrogenases/reductases (SDR) family. 2,4-dienoyl-CoA reductase subfamily. (254 aa)
pyrDDihydroorotate dehydrogenase (catalytic subunit); Catalyzes the conversion of dihydroorotate to orotate with NAD(+) as electron acceptor. (311 aa)
sirCPrecorrin-2 dehydrogenase; Catalyzes the dehydrogenation of precorrin-2 to form sirohydrochlorin which is used as a precursor in both siroheme biosynthesis and in the anaerobic branch of adenosylcobalamin biosynthesis; Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. (162 aa)
yngJacyl-CoA dehydrogenase, short-chain specific; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the acyl-CoA dehydrogenase family. (380 aa)
yoaIPutative 4-hydroxyphenylacetate-3-hydroxylase; Catalyzes the hydroxylation of 4-hydroxyphenylacetic acid (4HPA), leading to the production of 3,4-dihydroxyphenylacetic acid (DHPA). (483 aa)
acdAacyl-CoA dehydrogenase; Involved in the degradation of long-chain fatty acids. (379 aa)
fadEacyl-CoA dehydrogenase (FAD dependent); Involved in the degradation of long-chain fatty acids. (594 aa)
dhbA2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (261 aa)
sdhCSuccinate dehydrogenase (cytochrome b558 subunit); Di-heme cytochrome of the succinate dehydrogenase complex. (202 aa)
sdhASuccinate dehydrogenase (flavoprotein subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. (586 aa)
sdhBSuccinate dehydrogenase (iron-sulfur protein); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (253 aa)
hemNCoproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L- methionine (By similarity). (379 aa)
dapB(4S)-4-hydroxy-2,3,4, 5-tetrahydro-(2S)-dipicolinic acid (HTPA) dehydratase reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. (267 aa)
tyrAPrephenate dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the prephenate/arogenate dehydrogenase family. (371 aa)
dusBtRNA-dihydrouridine synthase B; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the Dus family. (333 aa)
ydbMPutative acyl-CoA dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the acyl-CoA dehydrogenase family. (381 aa)
yfmJPutative oxidoreductase; Putative quinone oxidoreductase that may contribute to the degradation of aromatic compounds; Belongs to the NADP-dependent oxidoreductase L4BD family. (339 aa)
mmgCShort chain acyl-CoA dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the acyl-CoA dehydrogenase family. (379 aa)
bacHCyclohexenol-containing tetrahydro-4-hydroxyphenylpyruvate H(4)HPP in bacilysin synthesis; Along with the bacABCDEF operon, BacG is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. Bacilysin is an irreversible inactivator of the glutaminase domain of glucosamine synthetase. BacG catalyzes the stereoselective reduction of exocyclic-delta(3),delta(5)-dihydro-hydroxyphenylpyruvate (ex-H2HPP), adding a pro-S hydride equivalent to C4 position to yield tetrahydro-hydroxyphenylpyruvate (H4HPP). Although the [...] (259 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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