STRINGSTRING
Sps_02420 Sps_02420 Sps_00201 Sps_00201 cyoE cyoE Sps_00311 Sps_00311 Sps_00532 Sps_00532 Sps_00645 Sps_00645 nadA nadA aroA aroA Sps_00829 Sps_00829 Sps_01084 Sps_01084 Sps_01095 Sps_01095 Sps_01137 Sps_01137 cmoB cmoB thiE thiE Sps_01188 Sps_01188 Sps_01414 Sps_01414 menA menA uppS uppS metK metK hemC hemC ubiA ubiA Sps_03543 Sps_03543 Sps_03739 Sps_03739 ribH ribH Sps_04124 Sps_04124 Sps_04255 Sps_04255 kdsA kdsA Sps_04580 Sps_04580 Sps_04783 Sps_04783 Sps_04805 Sps_04805 ubiX ubiX speE speE miaA miaA murA murA selU selU cyoE-2 cyoE-2
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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
Predicted Interactions
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Sps_024203-deoxy-D-arabinoheptulosonate-7-phosphate synthase; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). (363 aa)
Sps_00201PFAM: Protein of unknown function (DUF3137). (336 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. (304 aa)
Sps_00311Hypothetical protein; PFAM: DTW domain. (174 aa)
Sps_005323-deoxy-D-arabinoheptulosonate-7-phosphate synthase; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). (353 aa)
Sps_00645Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. (296 aa)
nadAQuinolinate synthetase; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate; Belongs to the quinolinate synthase A family. Type 1 subfamily. (355 aa)
aroA3-phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. (426 aa)
Sps_00829Hypothetical protein; PFAM: DTW domain. (252 aa)
Sps_01084PFAM: Lumazine binding domain; 'TIGRFAM: riboflavin synthase, alpha subunit'. (204 aa)
Sps_01095Hypothetical protein; PFAM: Domain of unknown function (DUF336). (144 aa)
Sps_01137Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme. (353 aa)
cmoBtRNA (mo5U34)-methyltransferase; Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L- methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5- carboxymethoxyuridine (cmo5U) at position 34 in tRNAs. (330 aa)
thiEThiamine-phosphate diphosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Belongs to the thiamine-phosphate synthase family. (525 aa)
Sps_01188PFAM: DTW domain. (175 aa)
Sps_01414'PFAM: Glutathione S-transferase, N-terminal domain; Glutathione S-transferase, C-terminal domain'. (336 aa)
menA1,4-dihydroxy-2-naphthoate prenyltransferase; Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK); Belongs to the MenA family. Type 1 subfamily. (290 aa)
uppSUndecaprenyl pyrophosphate synthetase; Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di- trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide. (264 aa)
metKMethionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. (383 aa)
hemCHydroxymethylbilane synthase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. (309 aa)
ubiA4-hydroxybenzoate polyprenyltransferase; Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate. (288 aa)
Sps_03543Cysteine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: cysteine synthase A; cysteine synthase; Belongs to the cysteine synthase/cystathionine beta- synthase family. (322 aa)
Sps_03739PFAM: NeuB family; TIGRFAM: N-acetylneuraminate synthase. (355 aa)
ribH6,7-dimethyl-8-ribityllumazine synthase; Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2- butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin; Belongs to the DMRL synthase family. (160 aa)
Sps_04124PFAM: Lumazine binding domain; 'TIGRFAM: riboflavin synthase, alpha subunit'. (220 aa)
Sps_04255Dihydropteroate synthase; Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. (280 aa)
kdsAPFAM: DAHP synthetase I family; TIGRFAM: 3-deoxy-8-phosphooctulonate synthase; Belongs to the KdsA family. (282 aa)
Sps_045803-deoxy-D-arabinoheptulosonate-7-phosphate synthase; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). (351 aa)
Sps_04783cob(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. (217 aa)
Sps_04805PFAM: Pyridoxal-phosphate dependent enzyme; 'TIGRFAM: 2,3-diaminopropionate biosynthesis protein SbnA'. (312 aa)
ubiXPolyprenyl p-hydroxybenzoate/phenylacrylic acid decarboxylase; Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN; Belongs to the UbiX/PAD1 family. (220 aa)
speEPutative spermidine synthase with an N-terminal membrane domain; Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. (575 aa)
miaAtRNA isopentenyltransferase MiaA; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family. (308 aa)
murAUDP-N-acetylglucosamine 1-carboxyvinyltransferase; Cell wall formation. Adds enolpyruvyl to UDP-N- acetylglucosamine; Belongs to the EPSP synthase family. MurA subfamily. (419 aa)
selUtRNA 2-selenouridine synthase; Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2- selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiouridine (geS2U) and subsequent selenation of the latter derivative to 2-selenouridine (Se2U) in the tRNA chain. (369 aa)
cyoE-2Protoheme 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)
Your Current Organism:
Shewanella psychrophila
NCBI taxonomy Id: 225848
Other names: CGMCC 1.6159, JCM 13876, S. psychrophila, Shewanella psychrophila Xiao et al. 2007 emend. Thorell et al. 2019, Shewanella sp. WP2, strain WP2
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