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Deba_0013 Deba_0013 Deba_0086 Deba_0086 trpB trpB ilvD ilvD leuC leuC leuD leuD Deba_0367 Deba_0367 Deba_0423 Deba_0423 Deba_0479 Deba_0479 Deba_0557 Deba_0557 trpA trpA trpB-2 trpB-2 Deba_0670 Deba_0670 Deba_0815 Deba_0815 Deba_0918 Deba_0918 mutM mutM nnrD nnrD Deba_0964 Deba_0964 mqnA mqnA Deba_1092 Deba_1092 ectC ectC Deba_1359 Deba_1359 hisB hisB Deba_1863 Deba_1863 dapA dapA nth nth eno eno fabZ fabZ Deba_2192 Deba_2192 Deba_2217 Deba_2217 Deba_2288 Deba_2288 Deba_2489 Deba_2489 Deba_2842 Deba_2842 Deba_2889 Deba_2889 Deba_2958 Deba_2958 Deba_3009 Deba_3009 Deba_3026 Deba_3026 Deba_3096 Deba_3096 Deba_3108 Deba_3108 aroC aroC aroQ aroQ
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Deba_0013Protein of unknown function UPF0031; InterPro IPR000631; KEGG: dat:HRM2_44810 hypothetical protein; PFAM: protein of unknown function UPF0031; SPTR: C0QF36 Putative uncharacterized protein; PFAM: Carbohydrate kinase. (289 aa)
Deba_0086COGs: COG1250 3-hydroxyacyl-CoA dehydrogenase; InterProIPR001753:IPR006176:IPR006108:IPR016040:IPR 008927:IPR018376:IPR013328; KEGG: 3-hydroxyacyl-CoA dehyrogenase, putative; PFAM: 3-hydroxyacyl-CoA dehydrogenase NAD-binding; Enoyl-CoA hydratase/isomerase; 3-hydroxyacyl-CoA dehydrogenase domain protein; SPTR: B9RKN5 3-hydroxyacyl-CoA dehyrogenase, putative; PFAM: Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; Belongs to the enoyl-CoA hydratase/isomerase family. (709 aa)
trpBPyridoxal-phosphate dependent TrpB-like enzyme; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (451 aa)
ilvDCOGs: COG0129 Dihydroxyacid dehydratase/phosphogluconate dehydratase; InterPro IPR000581:IPR004404:IPR020558; KEGG: mja:MJ1276 dihydroxy-acid dehydratase; PFAM: dihydroxy-acid and 6-phosphogluconate dehydratase; PRIAM: Dihydroxy-acid dehydratase; SPTR: C5U5V1 Dihydroxy-acid dehydratase; TIGRFAM: dihydroxy-acid dehydratase; PFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. (561 aa)
leuC3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (464 aa)
leuD3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. (207 aa)
Deba_0367KEGG: lxx:Lxx09000 hypothetical protein; SPTR: A6FRA1 Putative uncharacterized protein; PFAM: VanZ like family. (173 aa)
Deba_0423COGs: COG0720 6-pyruvoyl-tetrahydropterin synthase; InterPro IPR007115; KEGG: dol:Dole_1493 putative 6-pyruvoyl tetrahydropterin synthase; PFAM: 6-pyruvoyl tetrahydropterin synthase and hypothetical protein; SPTR: A8ZZE4 Putative uncharacterized protein; PFAM: 6-pyruvoyl tetrahydropterin synthase; TIGRFAM: queuosine biosynthesis protein QueD; 6-pyruvoyl tetrahydropterin synthase/QueD family protein. (122 aa)
Deba_0479COGs: COG0077 Prephenate dehydratase; InterProIPR020822:IPR001086:IPR002912:IPR008242:IPR 002701:IPR018528; KEGG: pca:Pcar_1887 chorismate mutase-P and prephenate dehydratase; PFAM: prephenate dehydratase; Chorismate mutase, type II; amino acid-binding ACT domain protein; SPTR: Q1K0T9 Chorismate mutase; PFAM: Prephenate dehydratase; ACT domain; Chorismate mutase type II. (410 aa)
Deba_0557COGs: COG0288 Carbonic anhydrase; InterPro IPR001765; KEGG: pca:Pcar_2939 carbonic anhydrase; PFAM: carbonic anhydrase; SPTR: Q3A0D3 Carbonic anhydrase; PFAM: Carbonic anhydrase. (260 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. (270 aa)
trpB-2Tryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (408 aa)
Deba_0670COGs: COG1024 Enoyl-CoA hydratase/carnithine racemase; InterPro IPR001753:IPR018376; KEGG: acr:Acry_1715 enoyl-CoA hydratase/isomerase; PFAM: Enoyl-CoA hydratase/isomerase; SPTR: A5FZ87 Enoyl-CoA hydratase; PFAM: Enoyl-CoA hydratase/isomerase family; Belongs to the enoyl-CoA hydratase/isomerase family. (268 aa)
Deba_0815uroporphyrin-III C-methyltransferase; COGs: COG0007 Uroporphyrinogen-III methylase; InterProIPR006366:IPR014777:IPR014776:IPR000878:IPR 003754:IPR003043; KEGG: sfu:Sfum_3201 uroporphyrin-III C-methyltransferase; PFAM: Uroporphyrin-III C/tetrapyrrole (Corrin/Porphyrin) methyltransferase; Uroporphyrinogen III synthase HEM4; SPTR: A0LN72 Uroporphyrinogen-III synthase / uroporphyrinogen-III C-methyltransferase; TIGRFAM: uroporphyrin-III C-methyltransferase; PFAM: Tetrapyrrole (Corrin/Porphyrin) Methylases; Uroporphyrinogen-III synthase HemD; TIGRFAM: uroporphyrin-III C-methyltransferase. (509 aa)
Deba_0918Molybdopterin oxidoreductase; COGs: COG0243 Anaerobic dehydrogenase typically selenocysteine-containing; InterPro IPR009010:IPR006963:IPR006656:IPR006657; KEGG: dal:Dalk_0693 molydopterin dinucleotide-binding region; PFAM: molybdopterin oxidoreductase; molybdopterin oxidoreductase Fe4S4 region; molydopterin dinucleotide-binding region; SPTR: B8FJX0 Molydopterin dinucleotide-binding region; PFAM: Molybdopterin oxidoreductase; Molydopterin dinucleotide binding domain; Molybdopterin oxidoreductase Fe4S4 domain; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (746 aa)
mutMformamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. (272 aa)
nnrDCarbohydrate kinase, YjeF related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow t [...] (525 aa)
Deba_0964Protein of unknown function UPF0047; COGs: COG0432 conserved hypothetical protein; InterPro IPR001602; KEGG: pth:PTH_0986 hypothetical protein; PFAM: protein of unknown function UPF0047; SPTR: A5D3M9 Uncharacterized conserved protein; PFAM: Uncharacterised protein family UPF0047; TIGRFAM: conserved hypothetical protein TIGR00149. (133 aa)
mqnAProtein of unknown function DUF178; Catalyzes the dehydration of chorismate into 3-[(1- carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2). (276 aa)
Deba_1092Hydro-lyase, Fe-S type, tartrate/fumarate subfamily, beta subunit; COGs: COG1838 Tartrate dehydratase beta subunit/Fumarate hydratase class I C-terminal domain; InterPro IPR004647; KEGG: nis:NIS_0837 fumarate/tartrate hydratase, beta subunit; PFAM: Fe-S type hydro-lyase tartrate/fumarate beta region; SPTR: A6Q390 Fumarate/tartrate hydratase, beta subunit; TIGRFAM: hydro-lyase, Fe-S type, tartrate/fumarate subfamily, beta subunit; PFAM: Fumarase C-terminus; TIGRFAM: hydro-lyases, Fe-S type, tartrate/fumarate subfamily, beta region. (185 aa)
ectCEctoine synthase; Catalyzes the circularization of gamma-N-acetyl-alpha,gamma- diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4- pyrimidine carboxylic acid), which is an excellent osmoprotectant. (130 aa)
Deba_1359COGs: COG0498 Threonine synthase; InterPro IPR001926:IPR000634:IPR004450; KEGG: dal:Dalk_4397 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; PRIAM: Threonine synthase; SPTR: B8FNA7 Threonine synthase; TIGRFAM: threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. (500 aa)
hisBCOGs: COG0131 Imidazoleglycerol-phosphate dehydratase; InterPro IPR000807:IPR020565:IPR020568; KEGG: gyc:GYMC61_3155 imidazoleglycerol-phosphate dehydratase; PFAM: imidazoleglycerol-phosphate dehydratase; PRIAM: Imidazoleglycerol-phosphate dehydratase; SPTR: C9RV81 Imidazoleglycerol-phosphate dehydratase; PFAM: Imidazoleglycerol-phosphate dehydratase. (195 aa)
Deba_1863COGs: COG1250 3-hydroxyacyl-CoA dehydrogenase; InterProIPR017441:IPR006176:IPR006108:IPR001753:IPR 016040:IPR008927:IPR013328; KEGG: chy:CHY_1609 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase/isomerase family protein; PFAM: 3-hydroxyacyl-CoA dehydrogenase NAD-binding; 3-hydroxyacyl-CoA dehydrogenase domain protein; Enoyl-CoA hydratase/isomerase; SPTR: Q3ABP7 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase/isomerase family protein; PFAM: Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase, C-terminal domain; 3-hydroxyacyl-CoA dehydrogenase, NAD binding domain. (811 aa)
dapADihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). (291 aa)
nthEndonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. (232 aa)
enoEnolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family. (422 aa)
fabZBeta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabZ; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. (158 aa)
Deba_2192Aconitate hydratase; COGs: COG1048 Aconitase A; InterProIPR001030:IPR015928:IPR015931:IPR015932:IPR 000573:IPR006250; KEGG: glo:Glov_1612 aconitate hydratase; PFAM: aconitate hydratase domain protein; SPTR: Q1NKB5 Putative aconitate hydratase; TIGRFAM: aconitate hydratase; PFAM: Aconitase C-terminal domain; Aconitase family (aconitate hydratase); TIGRFAM: aconitate hydratase, putative, Aquifex type. (639 aa)
Deba_2217Molybdopterin oxidoreductase; COGs: COG0243 Anaerobic dehydrogenase typically selenocysteine-containing; InterPro IPR009010:IPR000169:IPR006656:IPR006657; KEGG: dal:Dalk_1268 molybdopterin oxidoreductase; PFAM: molybdopterin oxidoreductase; molydopterin dinucleotide-binding region; SPTR: B8F9M5 Molybdopterin oxidoreductase; PFAM: Molybdopterin oxidoreductase; Molydopterin dinucleotide binding domain; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (713 aa)
Deba_2288dTDP-glucose 4,6-dehydratase; COGs: COG1088 dTDP-D-glucose 4 6-dehydratase; InterPro IPR016040:IPR002198:IPR001509:IPR005888; KEGG: rpd:RPD_1571 dTDP-glucose 4,6-dehydratase; PFAM: NAD-dependent epimerase/dehydratase; SPTR: Q13AT1 dTDP-glucose 4,6-dehydratase; TIGRFAM: dTDP-glucose 4,6-dehydratase; PFAM: NAD dependent epimerase/dehydratase family; TIGRFAM: dTDP-glucose 4,6-dehydratase; Belongs to the NAD(P)-dependent epimerase/dehydratase family. dTDP-glucose dehydratase subfamily. (350 aa)
Deba_2489InterPro IPR002539; KEGG: dal:Dalk_5057 MaoC domain protein dehydratase; PFAM: MaoC domain protein dehydratase; SPTR: B8FDU7 MaoC domain protein dehydratase; PFAM: MaoC like domain. (293 aa)
Deba_2842Molybdopterin oxidoreductase; COGs: COG0243 Anaerobic dehydrogenase typically selenocysteine-containing; InterProIPR006963:IPR006656:IPR006657:IPR009010:IPR 006655; KEGG: dvl:Dvul_2794 molybdopterin oxidoreductase; PFAM: molybdopterin oxidoreductase; molybdopterin oxidoreductase Fe4S4 region; molydopterin dinucleotide-binding region; SPTR: Q1NQN8 Formate dehydrogenase; PFAM: Molybdopterin oxidoreductase; Molydopterin dinucleotide binding domain; Molybdopterin oxidoreductase Fe4S4 domain; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (713 aa)
Deba_2889COGs: COG1024 Enoyl-CoA hydratase/carnithine racemase; InterPro IPR001753:IPR018376; KEGG: bpt:Bpet4719 enoyl-CoA hydratase; PFAM: Enoyl-CoA hydratase/isomerase; SPTR: A9IFN7 Enoyl-CoA hydratase; PFAM: Enoyl-CoA hydratase/isomerase family; Belongs to the enoyl-CoA hydratase/isomerase family. (266 aa)
Deba_2958Porphobilinogen synthase; COGs: COG0113 Delta-aminolevulinic acid dehydratase; InterPro IPR001731:IPR013785; KEGG: dol:Dole_1224 delta-aminolevulinic acid dehydratase; PFAM: delta-aminolevulinic acid dehydratase; PRIAM: Porphobilinogen synthase; SPTR: A8ZY23 Delta-aminolevulinic acid dehydratase; PFAM: Delta-aminolevulinic acid dehydratase; Belongs to the ALAD family. (327 aa)
Deba_3009Lytic transglycosylase catalytic; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. (486 aa)
Deba_3026COGs: COG1024 Enoyl-CoA hydratase/carnithine racemase; InterPro IPR001753; KEGG: dal:Dalk_1295 enoyl-CoA hydratase/isomerase; PFAM: Enoyl-CoA hydratase/isomerase; SPTR: B8F9Q2 Enoyl-CoA hydratase/isomerase; PFAM: Enoyl-CoA hydratase/isomerase family. (257 aa)
Deba_3096Hypothetical protein; KEGG: phe:Phep_2408 heparinase II/III family protein; SPTR: B0NLH9 Putative uncharacterized protein. (877 aa)
Deba_3108Extracellular solute-binding protein family 3; Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. In the N-terminal section; belongs to the bacterial solute- binding protein 3 family. (480 aa)
aroCChorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. (356 aa)
aroQ3-dehydroquinate dehydratase, type II; Catalyzes a trans-dehydration via an enolate intermediate. Belongs to the type-II 3-dehydroquinase family. (144 aa)
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
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