STRINGSTRING
gltB gltB kbaY kbaY kbaZ kbaZ fadH fadH yggW yggW fbaA fbaA queE queE ygcP ygcP aroF aroF pdxJ pdxJ rlmN rlmN guaB guaB dapA dapA ybiY ybiY moaA moaA bioB bioB aroG aroG lipA lipA hemB hemB mhpE mhpE yagE yagE nadC nadC leuA leuA talB talB guaC guaC dgoA dgoA deoC deoC yjjW yjjW sgcE sgcE yjhH yjhH nrdG nrdG ulaD ulaD epmB epmB alsE alsE dusA dusA thiE thiE thiG thiG thiH thiH pflC pflC fsaB fsaB tpiA tpiA yihT yihT fsaA fsaA pflA pflA pyrD pyrD kdsA kdsA trpA trpA trpC trpC pyrF pyrF ydeM ydeM hemN hemN lsrF lsrF nemA nemA aroD aroD aroH aroH ydjI ydjI eda eda hisA hisA hisF hisF gatZ gatZ gatY gatY fbaB fbaB dusC dusC preA preA eutB eutB talA talA aslB aslB yidF yidF lldD lldD sgbH sgbH rpe rpe dusB dusB nanA nanA nanE nanE
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:
gltBGlutamate synthase, large subunit; Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate. (1486 aa)
kbaYTagatose 6-phosphate aldolase 1, kbaY subunit; Catalytic subunit of the tagatose-1,6-bisphosphate aldolase KbaYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires KbaZ subunit for full activity and stability. (286 aa)
kbaZTagatose 6-phosphate aldolase 1, kbaZ subunit; Component of the tagatose-1,6-bisphosphate aldolase KbaYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of KbaY. When expressed alone, KbaZ does not show any aldolase activity; Belongs to the GatZ/KbaZ family. KbaZ subfamily. (426 aa)
fadH2,4-dienoyl-CoA reductase, NADH and FMN-linked; Functions as an auxiliary enzyme in the beta-oxidation of unsaturated fatty acids with double bonds at even carbon positions. Catalyzes the NADPH-dependent reduction of the C4-C5 double bond of the acyl chain of 2,4-dienoyl-CoA to yield 2-trans-enoyl-CoA. Acts on both isomers, 2-trans,4- cis- and 2-trans,4-trans-decadienoyl-CoA, with almost equal efficiency. Is not active with NADH instead of NADPH. Does not show cis->trans isomerase activity. (672 aa)
yggWHemN family putative oxidoreductase; Probably acts as a heme chaperone, transferring heme to the NarI subunit of the respiratory enzyme nitrate reductase; transfer may be stimulated by NADH. Binds one molecule of heme per monomer, possibly covalently. Heme binding is not affected by either [4Fe-4S] or S- adenosyl-L-methionine (SAM)-binding. Does not have coproporphyrinogen III dehydrogenase activity in vitro. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (Probable). (378 aa)
fbaAFructose-bisphosphate aldolase, class II; Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. (359 aa)
queE7-carboxy-7-deazaguanine synthase; Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. (223 aa)
ygcPPutative anti-terminator regulatory protein. (191 aa)
aroF3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, tyrosine-repressible; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP); Belongs to the class-I DAHP synthase family. (356 aa)
pdxJPyridoxine 5'-phosphate synthase; Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino- 2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate. (243 aa)
rlmNDual specificity 23S rRNA m(2)A2503, tRNA m(2)A37 methyltransferase, SAM-dependent; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation. Belongs to the radical SAM superfamily. RlmN family. (384 aa)
guaBIMP dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family. (488 aa)
dapADihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). Belongs to the DapA family. (292 aa)
ybiYPutative pyruvate formate lyase activating enzyme; Activation of pyruvate formate-lyase 2 under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine; Belongs to the organic radical-activating enzymes family. (299 aa)
moaAMolybdopterin biosynthesis protein A; Catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z). (329 aa)
bioBBiotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. (346 aa)
aroG3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, phenylalanine repressible; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP); Belongs to the class-I DAHP synthase family. (350 aa)
lipALipoate synthase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. Free octanoate is not a substrate for LipA; Belongs to the radical SAM superfamily. Lipoyl synthase family. (321 aa)
hemB5-aminolevulinate 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; Belongs to the ALAD family. (324 aa)
mhpE4-hyroxy-2-oxovalerate/4-hydroxy-2-oxopentanoic acid aldolase, class I; Catalyzes the retro-aldol cleavage of 4-hydroxy-2- oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta- cleavage pathway for the degradation of 3-phenylpropanoate. Belongs to the 4-hydroxy-2-oxovalerate aldolase family. (337 aa)
yagE2-keto-3-deoxy gluconate (KDG) aldolase; Catalyzes the formation of 2-keto-3-deoxy-gluconate (KDG) from pyruvate and glyceraldehyde. May also function as a 2-dehydro-3-deoxy-D-pentonate aldolase. Overexpression leads to increased growth (over 2 hours) in the presence of the antibiotics norfloxacin, ampicillin and streptomycin ; Belongs to the DapA family. (302 aa)
nadCQuinolinate phosphoribosyltransferase; Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family. (297 aa)
leuA2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. (523 aa)
talBTransaldolase B; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. (317 aa)
guaCGMP reductase; Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides; Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily. (347 aa)
dgoA2-oxo-3-deoxygalactonate 6-phosphate aldolase; Involved in the degradation of galactose via the DeLey- Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with re- facial selectivity. It can use a limited number of aldehyde substrates, including D-glyceraldehyde-3-phosphate (natural substrate), D- glyceraldehyde, glycolaldehyde, 2-pyridinecarboxaldehyde, D-ribose, D- erythr [...] (205 aa)
deoC2-deoxyribose-5-phosphate aldolase, NAD(P)-linked; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5- phosphate. Can also catalyze the double aldol condensation of three acetaldehyde molecules, leading to the formation of 2,4,6-trideoxyhexose. Belongs to the DeoC/FbaB aldolase family. DeoC type 2 subfamily. (259 aa)
yjjWPutative activating enzyme; Protein involved in anaerobic respiration and protein modification process; Belongs to the organic radical-activating enzymes family. (287 aa)
sgcEPutative epimerase; Probable pentose-5-phosphate 3-epimerase. (210 aa)
yjhHPutative lyase/synthase; Functions as a 2-dehydro-3-deoxy-D-pentonate aldolase. Belongs to the DapA family. (301 aa)
nrdGAnaerobic ribonucleoside-triphosphate reductase-activating protein; Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine; Belongs to the organic radical-activating enzymes family. (154 aa)
ulaD3-keto-L-gulonate 6-phosphate decarboxylase; Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization. Belongs to the HPS/KGPDC family. KGPDC subfamily. (216 aa)
epmBEF-P-Lys34 lysylation protein; With EpmA is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P) on 'Lys-34'. EpmB appears to act before EpmA. Displays lysine 2,3- aminomutase activity, producing (R)-beta-lysine from (S)-alpha-lysine (L-lysine). Cannot use (S)-ornithine or (R)-alpha-lysine as a substrate; Belongs to the radical SAM superfamily. KamA family. (342 aa)
alsEAllulose-6-phosphate 3-epimerase; Catalyzes the reversible epimerization of D-allulose 6- phosphate to D-fructose 6-phosphate. Can also catalyze with lower efficiency the reversible epimerization of D-ribulose 5-phosphate to D- xylulose 5-phosphate. (231 aa)
dusAtRNA-dihydrouridine synthase A; 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. Specifically modifies U20 and U20a in tRNAs; Belongs to the Dus family. DusA subfamily. (345 aa)
thiEThiamine phosphate synthase (thiamine phosphate pyrophosphorylase); 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. (211 aa)
thiGThiamine biosynthesis ThiGH complex subunit; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S; Belongs to the ThiG family. (256 aa)
thiHTyrosine lyase, involved in thiamine-thiazole moiety synthesis; Catalyzes the radical-mediated cleavage of tyrosine to 2- iminoacetate and 4-cresol. (377 aa)
pflCPutative [formate-C-acetyltransferase 2]-activating enzyme; Activation of pyruvate formate-lyase 2 under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine; Belongs to the organic radical-activating enzymes family. (292 aa)
fsaBFructose-6-phosphate aldolase 2; Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize hydroxyacetone as an alternative donor substrate. Is also able to catalyze the direct self-aldol addition of glycolaldehyde. Is less catalytically efficient than the isozyme FsaA. Does not display transaldolase activity. (220 aa)
tpiATriosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (255 aa)
yihT6-deoxy-6-sulphofructose-1-phosphate aldolase; Cleaves 6-deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA). Belongs to the aldolase LacD family. (292 aa)
fsaAFructose-6-phosphate aldolase 1; Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone (DHA) and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize several aldehydes as acceptor compounds in vitro, and hydroxyacetone (HA) or 1-hydroxy-butan-2-one as alternative donor substrate. Is also able to catalyze the direct stereoselective self-aldol addition of glycolaldehyde to furnish D-(-)- threose, and cross-aldol reactions of glycolaldehyde to other aldehyde acceptors. Is not able to cleave fructose, fructose 1-phosphate, glucose 6-phosphate, s [...] (220 aa)
pflAPyruvate formate-lyase 1-activating enzyme; Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S- adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine; Belongs to the organic radical-activating enzymes family. (246 aa)
pyrDDihydro-orotate oxidase, FMN-linked; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. (336 aa)
kdsA3-deoxy-D-manno-octulosonate 8-phosphate synthase; Synthesis of KDO 8-P which is required for lipid A maturation and cellular growth. (284 aa)
trpATryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate; Belongs to the TrpA family. (268 aa)
trpCIndole-3-glycerolphosphate synthetase and N-(5-phosphoribosyl)anthranilate isomerase; Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain. (453 aa)
pyrFOrotidine-5'-phosphate decarboxylase; Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). (245 aa)
ydeMPutative enzyme; Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family. (385 aa)
hemNCoproporphyrinogen III oxidase, SAM and NAD(P)H dependent, oxygen-independent; Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX. It can use NAD or NADP, but NAD is preferred. Belongs to the anaerobic coproporphyrinogen-III oxidase family. (457 aa)
lsrFPutative autoinducer-2 (AI-2) aldolase; Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the transfer of an acetyl moiety from 3-hydroxy-5- phosphonooxypentane-2,4-dione to CoA to form glycerone phosphate and acetyl-CoA; Belongs to the DeoC/FbaB aldolase family. (291 aa)
nemAChromate reductase, quinone reductase, FMN-linked; Involved in the degradation of toxic compounds. Can use a variety of substrates, including the nitrate ester explosives glycerol trinitrate (GTN) and pentaerythritol tetranitrate (PETN), chromate and various electrophiles such as quinones. Involved in resistance to hypochlorous acid (HOCl), which is the active component of household bleach and a powerful antimicrobial during the innate immune response. Catalyzes the reduction of N- ethylmaleimide (NEM) to N-ethylsuccinimide. Together with NfsA and NfsB, can use the nitroaromatic explos [...] (365 aa)
aroD3-dehydroquinate dehydratase; Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids (AroAA). Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsylon-amino group of a lys-170 at the active site. (252 aa)
aroH3-deoxy-D-arabino-heptulosonate-7-phosphate synthase, tryptophan repressible; Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino- heptulosonate-7-phosphate (DAHP). (348 aa)
ydjIPutative aldolase. (278 aa)
edaKHG/KDPG aldolase; Involved in the degradation of glucose via the Entner- Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-Keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and D- glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with si-facial selectivity. It accepts some nucleophiles other than pyruvate, including 2-oxobutanoate, phenylpyruvate, and fluorobutanoate. It has a preference for the S-configuration at C2 of the electrophile. (213 aa)
hisAN-(5'-phospho-L-ribosyl-formimino)-5-amino-1- (5'-phosphoribosyl)-4-imidazolecarboxamide isomerase; Protein involved in histidine biosynthetic process; Belongs to the HisA/HisF family. (245 aa)
hisFImidazole glycerol phosphate synthase, catalytic subunit with HisH; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit; Belongs to the HisA/HisF family. (258 aa)
gatZD-tagatose 1,6-bisphosphate aldolase 2, subunit; Component of the tagatose-1,6-bisphosphate aldolase GatYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of GatY. When expressed alone, GatZ does not show any aldolase activity. Is involved in the catabolism of galactitol. Belongs to the GatZ/KbaZ family. GatZ subfamily. (420 aa)
gatYD-tagatose 1,6-bisphosphate aldolase 2, catalytic subunit; Catalytic subunit of the tagatose-1,6-bisphosphate aldolase GatYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires GatZ subunit for full activity and stability. Is involved in the catabolism of galactitol. (284 aa)
fbaBFructose-bisphosphate aldolase class I; Protein involved in glycolysis; Belongs to the DeoC/FbaB aldolase family. FbaB subfamily. (350 aa)
dusCtRNA-dihydrouridine synthase C; 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. DusC specifically modifies U16 in tRNAs. (315 aa)
preADihydropyrimidine dehydrogenase, NADH-dependent, subunit C; Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT). (411 aa)
eutBEthanolamine ammonia-lyase, heavy chain; Protein involved in amine catabolic process. (453 aa)
talATransaldolase A; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. (316 aa)
aslBPutative AslA-specific sulfatase-maturating enzyme; Putative arylsulfatase regulator; Protein involved in sulfur metabolic process and protein folding; Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family. (411 aa)
yidFPutative Cys-type oxidative YidJ-maturating enzyme; Putative transcriptional regulator. (165 aa)
lldDL-lactate dehydrogenase, FMN-linked; Catalyzes the conversion of L-lactate to pyruvate. Seems to be a primary dehydrogenase in the respiratory chain. To a lesser extent, can also oxidize DL-alpha-hydroxybutyrate, but not D-lactate. (396 aa)
sgbH3-keto-L-gulonate 6-phosphate decarboxylase; Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. May be involved in the utilization of 2,3-diketo-L- gulonate. (220 aa)
rpeD-ribulose-5-phosphate 3-epimerase; Catalyzes the reversible epimerization of D-ribulose 5- phosphate to D-xylulose 5-phosphate. (225 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. DusB subfamily. (321 aa)
nanAN-acetylneuraminate lyase; Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate; Belongs to the DapA family. NanA subfamily. (297 aa)
nanEPutative N-acetylmannosamine-6-P epimerase; Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N- acetylglucosamine-6-phosphate (GlcNAc-6-P). (229 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.