STRINGSTRING
nasF nasF hmoA hmoA gsaB gsaB hemZ hemZ hemE hemE hemH hemH hemY hemY ctaO ctaO yjjA yjjA ctaA ctaA ctaB ctaB sumT sumT sirB sirB sirC sirC hemN hemN hemL hemL hemB hemB hemD hemD hemC hemC hemA hemA pduO pduO hemQ hemQ
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.
Node Color
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
Edges:
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:
nasFuroporphyrin-III C-methyltransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the precorrin methyltransferase family. (483 aa)
hmoAHeme-degrading monooxygenase; Allows bacterial pathogens to use the host heme as an iron source. Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron; Belongs to the antibiotic biosynthesis monooxygenase family. (108 aa)
gsaBGlutamate-1-semialdehyde aminotransferase, class III aminotransferase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme. (429 aa)
hemZCoproporphyrinogen III oxidase; Involved in the biosynthesis of porphyrin-containing compound; Belongs to the anaerobic coproporphyrinogen-III oxidase family. HemZ subfamily. (501 aa)
hemEUroporphyrinogen III decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (353 aa)
hemHFerrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX; Belongs to the ferrochelatase family. (310 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)
ctaOMinor protoheme IX farnesyltransferase 1 (heme O synthase); Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (329 aa)
yjjAPutative enzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (270 aa)
ctaAheme-A synthase; Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group. Also involved in the sporulation. (306 aa)
ctaBProtoheme IX farnesyltransferase 2; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group; Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily. (305 aa)
sumTUroporphyrinogen III and precorrin-1 C-methyltransferase; Catalyzes both methylations at C-2 and C-7 of uroporphyrinogen III leading to precorrin-1 and precorrin-2; their oxidative esterification gives respectively factor I octamethyl ester and sirohydrochlorin. (257 aa)
sirBSirohydrochlorin ferrochelatase; Chelates iron to the siroheme precursor; Belongs to the CbiX family. SirB subfamily. (261 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)
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)
hemLGlutamate-1-semialdehyde 2,1-aminotransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (430 aa)
hemBDelta-aminolevulinic acid dehydratase (porphobilinogen synthase); Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). (324 aa)
hemDUroporphyrinogen III cosynthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. Belongs to the uroporphyrinogen-III synthase family. (262 aa)
hemCPorphobilinogen deaminase (hydroxymethylbilane synthase); Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. (314 aa)
hemAglutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (455 aa)
pduOPutative ATP:cob(I)alamin adenosyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type e: enzyme. (193 aa)
hemQEssential component of heme biosynthesis; May function as heme-dependent peroxidase. (254 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
Server load: low (32%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.