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GLE_3907 GLE_3907 GLE_3818 GLE_3818 hemA hemA pqqE pqqE pqqD pqqD GLE_3696 GLE_3696 ravA ravA tig tig GLE_3395 GLE_3395 map map GLE_2871 GLE_2871 GLE_2870 GLE_2870 GLE_2733 GLE_2733 GLE_2666 GLE_2666 GLE_2663 GLE_2663 GLE_2544 GLE_2544 GLE_2530 GLE_2530 GLE_2425 GLE_2425 GLE_2407 GLE_2407 GLE_2350 GLE_2350 GLE_2291 GLE_2291 GLE_2289 GLE_2289 gluQ gluQ GLE_1683 GLE_1683 GLE_1618 GLE_1618 GLE_1563 GLE_1563 GLE_1480 GLE_1480 GLE_1437 GLE_1437 gltX gltX cobA cobA hemE hemE GLE_0937 GLE_0937 hemN hemN hemL hemL GLE_0837 GLE_0837 bfr bfr rsmC rsmC GLE_0325 GLE_0325 cyoE cyoE GLE_0294 GLE_0294 hemH hemH cysG cysG hemD hemD GLE_5021 GLE_5021 GLE_4999 GLE_4999 hemB hemB hemF hemF GLE_4921 GLE_4921 hemC hemC GLE_4439 GLE_4439 GLE_4298 GLE_4298 GLE_4271 GLE_4271 map-2 map-2 cobO cobO cobB cobB cobD cobD GLE_4086 GLE_4086 cobQ cobQ cobU cobU cobT cobT GLE_4082 GLE_4082 cobS cobS dps dps
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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
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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
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textmining
co-expression
protein homology
Your Input:
GLE_3907ATP:cob(I)alamin adenosyltransferase; Belongs to the Cob(I)alamin adenosyltransferase family. (184 aa)
GLE_3818Hypothetical protein. (195 aa)
hemAglutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (450 aa)
pqqECoenzyme PQQ biosynthesis protein E; Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ). (369 aa)
pqqDCoenzyme PQQ synthesis protein D. (98 aa)
GLE_3696General stress protein. (161 aa)
ravAATPase RavA. (380 aa)
tigTrigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. (433 aa)
GLE_3395Hypothetical protein. (102 aa)
mapMethionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. (258 aa)
GLE_2871CalU5. (283 aa)
GLE_2870Coproporphyrinogen III oxidase family protein. (466 aa)
GLE_2733Ferritin-like domain. (215 aa)
GLE_2666Methanol dehydrogenase regulator. (333 aa)
GLE_2663Hypothetical protein. (724 aa)
GLE_2544Heme oxygenase. (197 aa)
GLE_2530Radical SAM domain protein. (390 aa)
GLE_2425Heme oxygenase. (199 aa)
GLE_2407Hypothetical protein. (224 aa)
GLE_2350Oxidoreductase, short chain dehydrogenase/reductase family; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (251 aa)
GLE_2291VWA domain containing CoxE-like protein. (404 aa)
GLE_2289ATPase. (359 aa)
gluQglutamyl-Q tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. (322 aa)
GLE_1683Methanol dehydrogenase regulator. (350 aa)
GLE_1618GlcG protein. (160 aa)
GLE_1563Transcriptional regulatory protein. (1107 aa)
GLE_1480Hypothetical protein. (239 aa)
GLE_1437Membrane protein. (150 aa)
gltXglutamyl-tRNA synthetase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (465 aa)
cobAuroporphyrin-III C-methyltransferase; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. Belongs to the precorrin methyltransferase family. In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. (498 aa)
hemEUroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (358 aa)
GLE_0937Methanol dehydrogenase regulatory protein. (342 aa)
hemNOxygen-independent coproporphyrinogen III oxidase; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (400 aa)
hemLGlutamate-1-semialdehyde-2,1-aminomutase. (427 aa)
GLE_0837Transcriptional regulator. (762 aa)
bfrBacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family. (158 aa)
rsmCRibosomal RNA small subunit methyltransferase C; Belongs to the methyltransferase superfamily. (350 aa)
GLE_0325NAD-dependent epimerase/dehydratase family protein. (298 aa)
cyoEProtoheme IX farnesyltransferase; 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. (310 aa)
GLE_0294Cytochrome oxidase assembly protein. (387 aa)
hemHFerrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. (332 aa)
cysGPutative uroporphyrin-III C-methyltransferase. (333 aa)
hemDuroporphyrinogen-III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. (233 aa)
GLE_5021GHMP kinases putative ATP-binding protein. (314 aa)
GLE_4999Protein containing ATPase domain associated with various cellular activities (AAA). (329 aa)
hemBDelta-aminolevulinic acid dehydratase; Belongs to the ALAD family. (330 aa)
hemFCoproporphyrinogen III oxidase, aerobic; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX. (303 aa)
GLE_4921NAD dependent epimerase/dehydratase family. (256 aa)
hemCPorphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. (313 aa)
GLE_4439Oxygen-independent coproporphyrinogen III oxidase 1. (449 aa)
GLE_4298NAD-dependent epimerase/dehydratase. (288 aa)
GLE_4271Antibiotic biosynthesis monooxygenase. (113 aa)
map-2Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. (245 aa)
cobOcob(I)yrinic acid a,c-diamide adenosyltransferase; Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids. (210 aa)
cobBCobyrinic Acid a,c-diamide synthase. (404 aa)
cobDCobalamin biosynthesis protein; Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. (312 aa)
GLE_4086L-threonine-O-3-phosphate decarboxylase. (330 aa)
cobQCobyric acid synthase CobQ; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. (506 aa)
cobUCobinamide kinase/cobinamide phosphate guanylyltransferase; Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate. (172 aa)
cobTNicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase; Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). (362 aa)
GLE_4082Phosphoglycerate mutase family protein. (202 aa)
cobSCobalamin 5'-phosphate synthase; Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'- phosphate; Belongs to the CobS family. (246 aa)
dpsDNA protection during starvation protein; Belongs to the Dps family. (193 aa)
Your Current Organism:
Lysobacter enzymogenes
NCBI taxonomy Id: 69
Other names: ATCC 29487, DSM 2043, L. enzymogenes, LMG 8762, LMG:8762, Lysobacter enzymogenes subsp. enzymogenes, UASM 495
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