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gsaB gsaB rocD rocD spsC spsC bacG bacG glyA glyA epsN epsN sufS sufS pucG pucG patB patB yugH yugH bioK bioK bioF bioF iscSB iscSB hemL hemL nifS nifS iscSA iscSA mccB mccB gcvPA gcvPA gcvPB gcvPB hisC hisC aspB aspB yodT yodT kbl kbl speA speA dapX dapX mtnE mtnE metC metC metI metI argD argD yisV yisV ntdA ntdA serC serC yhxA yhxA ydfD ydfD ydeF ydeF gabT gabT ycbU ycbU
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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
gene co-occurrence
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textmining
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gsaBGlutamate-1-semialdehyde aminotransferase, class III aminotransferase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme. (429 aa)
rocDOrnithine aminotransferase; Catalyzes the interconversion of ornithine to glutamate semialdehyde. Controls arginine catabolism. (401 aa)
spsCPutative glutamine-dependent sugar transaminase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the DegT/DnrJ/EryC1 family. (389 aa)
bacGPhenylalanine aminotransferase forming tetrahydrotyrosine in bacilysin synthesis; Part of the bacABCDEF operon responsible for 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. Catalyzes the reductive amination of the C2 ketone of tetrahydro-hydroxyphenylpyruvate (H4HPP), with L-Phe as an amino donor, to yield tetrahydrotyrosine (H4Tyr) diastereomer. D-Phe is not an effective amino donor. BacF associated to BacG converts [...] (399 aa)
glyASerine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism (By similarity); Belongs to the SHMT family. (415 aa)
epsNPutative aminotransferase; May be involved in the production of the exopolysaccharide (EPS) component of the extracellular matrix during biofilm formation. EPS is responsible for the adhesion of chains of cells into bundles. (388 aa)
sufSCysteine desulfurase; Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40- to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity. (406 aa)
pucGVitamin B6-dependent (S)-ureidoglycine glyoxylate aminotransferase; Catalyzes the transamination between an unstable intermediate ((S)-ureidoglycine) and the end product of purine catabolism (glyoxylate) to yield oxalurate and glycine. Glyoxylate is the preferred substrate, but other amino-group acceptors can be used. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. (416 aa)
patBPromiscuous cystathionine beta-lyase / cysteine desulfhydrase; Catalyzes the transformation of cystathionine to homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily. (387 aa)
yugHPutative aspartate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (386 aa)
bioKLysine-8-amino-7-oxononanoate aminotransferase; Catalyzes the transfer of the alpha-amino group from L-lysine to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). B.subtilis is the only bacterium known to utilize L-lysine as an amino donor in the biosynthesis of DAPA. Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily. (448 aa)
bioF8-amino-7-oxononanoate synthase; Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. (389 aa)
iscSBCysteine desulfurase; Catalyzes the removal of elemental sulfur from cysteine to produce alanine. (381 aa)
hemLGlutamate-1-semialdehyde 2,1-aminotransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (430 aa)
nifSPutative desulfurase involved in iron-sulfur clusters for NAD biosynthesis; Catalyzes the removal of elemental sulfur from cysteine to produce alanine (By similarity). Seems to be required for NAD biosynthesis. (395 aa)
iscSACysteine desulfurase involved in tRNA thiolation; Catalyzes the removal of elemental sulfur from cysteine to produce alanine. (379 aa)
mccBCystathionine gamma-lyase and homocysteine gamma-lyase for reverse transsulfuration pathway; Catalyzes the conversion of cystathionine to cysteine, and homocysteine to sulfide. (379 aa)
gcvPAGlycine decarboxylase (subunit 1) (glycine cleavage system protein P); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity). (448 aa)
gcvPBGlycine decarboxylase (subunit 2) (glycine cleavage system protein P); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity); Belongs to the GcvP family. C-terminal subunit subfamily. (488 aa)
hisCHistidinol-phosphate aminotransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (360 aa)
aspBPutative aspartate aminotransferase; 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 class-I pyridoxal-phosphate-dependent aminotransferase family. (393 aa)
yodTPutative aminovalerate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (444 aa)
kbl2-amino-3-ketobutyrate CoA ligase (glycine acetyl transferase); Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. (392 aa)
speAArginine decarboxylase; Catalyzes the formation of agmatine from arginine. (490 aa)
dapXN-acetyl-L,L-diaminopimelate aminotransferase; Essential for murein biosynthesis. Probably catalyzes the conversion of L-2-acetamido-6-oxopimelate to N-acetyl-LL- 2,6-diaminopimelate (Probable); Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (393 aa)
mtnEMethionine-glutamine aminotransferase; Catalyzes the formation of methionine from 2-keto-4- methylthiobutyrate (KMTB). (398 aa)
metCCystathionine beta-lyase; Catalyzes the transformation of cystathionine into homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine; Belongs to the trans-sulfuration enzymes family. (390 aa)
metICystathionine gamma-synthase and O-acetylhomoserine thiolyase; Catalyzes the formation of L-cystathionine from O-acetyl-L- homoserine and L-cysteine. Cannot use O-succinyl-L-homoserine as substrate. Also exhibits O-acetylhomoserine thiolyase activity, catalyzing the synthesis of L-homocysteine from O-acetyl-L-homoserine and sulfide. (373 aa)
argDN-acetylornithine aminotransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (385 aa)
yisVPutative PLP-dependent transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (484 aa)
ntdA3-oxo-glucose-6-phosphate:glutamate aminotransferase; Involved in the biosynthesis of kanosamine (3-amino-3-deoxy- D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the reversible pyridoxal phosphate-dependent transamination of 3-dehydro- alpha-D-glucose 6-phosphate to form alpha-D-kanosamine-6-phosphate. It can only use alpha-anomer and glutamate is the only amino donor. (441 aa)
serCPhosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. (359 aa)
yhxAHypothetical protein; Essential for glycerol catabolism; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (450 aa)
ydfDPutative PLP-dependent transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (482 aa)
ydeFPutative PLP-dependent transcriptional regulator; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator. (462 aa)
gabT4-aminobutyrate aminotransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (436 aa)
ycbUPutative cysteine desulfurase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (370 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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