Immune System

Campbell GR, To RK, Hanna J, Spector SA. SARS-CoV-2, SARS-CoV-1, and HIV-1 derived ssRNA sequences activate the NLRP3 inflammasome in human macrophages through a non-classical pathway. iScience. 2021 Apr 23;24(4):102295. PMID: 33718825; PMCID: PMC7939994.; Moreno-Eutimio MA, López-Macías C, Pastelin-Palacios R. Bioinformatic analysis and identification of single-stranded RNA sequences recognized by TLR7/8 in the SARS-CoV-2, SARS-CoV, and MERS-CoV genomes. Microbes and Infection. 2020 May;22(4-5):226–9. doi: 10.1016/j.micinf.2020.04.009.; Zhang Z, Ohto U, Shibata T, Taoka M, Yamauchi Y, Sato R, Shukla NM, David SA, Isobe T, Miyake K, Shimizu T. Structural Analyses of Toll-like Receptor 7 Reveal Detailed RNA Sequence Specificity and Recognition Mechanism of Agonistic Ligands. Cell Rep. 2018 Dec 18;25(12):3371–3381.e5. doi: 10.1016/j.celrep.2018.11.081. PMID: 30566863.; Schierhorn KL, Jolmes F, Bespalowa J, Saenger S, Peteranderl C, Dzieciolowski J, Mielke M, Budt M, Pleschka S, Herrmann A, Herold S, Wolff T. Influenza A Virus Virulence Depends on Two Amino Acids in the N-Terminal Domain of Its NS1 Protein To Facilitate Inhibition of the RNA-Dependent Protein Kinase PKR. J Virol. 2017 May 15;91(10). PMID: 28250123; PMCID: PMC5411612.; Zhang Z, Ohto U, Shibata T, Krayukhina E, Taoka M, Yamauchi Y, Tanji H, Isobe T, Uchiyama S, Miyake K, Shimizu T. Structural Analysis Reveals that Toll-like Receptor 7 Is a Dual Receptor for Guanosine and Single-Stranded RNA. Immunity. 2016 Oct 18;45(4):737–48. doi: 10.1016/j.immuni.2016.09.011. PMID: 27742543.; Tanji H, Ohto U, Motoi Y, Shibata T, Miyake K, Shimizu T. Autoinhibition and relief mechanism by the proteolytic processing of Toll-like receptor 8. Proc Natl Acad Sci U S A. 2016 Mar 15;113(11):3012–7. PMID: 26929371; PMCID: PMC4801236.; Scheuplein VA, Seifried J, Malczyk AH, Miller L, Höcker L, Vergara-Alert J, Dolnik O, Zielecki F, Becker B, Spreitzer I, König R, Becker S, Waibler Z, Mühlebach MD. High secretion of interferons by human plasmacytoid dendritic cells upon recognition of Middle East respiratory syndrome coronavirus. J Virol. 2015 Apr;89(7):3859–69. PMID: 25609809; PMCID: PMC4403407.; Costedoat-Chalumeau N, Dunogué B, Morel N, Le Guern V, Guettrot-Imbert G. Hydroxychloroquine: a multifaceted treatment in lupus. Presse Med. 2014 Jun;43(6 Pt 2):e167–80. doi: 10.1016/j.lpm.2014.03.007. PMID: 24855048.; Lester SN, Li K. Toll-Like Receptors in Antiviral Innate Immunity. Journal of Molecular Biology. 2014 Mar;426(6):1246–64. doi: 10.1016/j.jmb.2013.11.024.; Lamphier M, Zheng W, Latz E, Spyvee M, Hansen H, Rose J, Genest M, Yang H, Shaffer C, Zhao Y, Shen Y, Liu C, Liu D, Mempel TR, Rowbottom C, Chow J, Twine NC, Yu M, Gusovsky F, Ishizaka ST. Novel small molecule inhibitors of TLR7 and TLR9: mechanism of action and efficacy in vivo. Mol Pharmacol. 2014 Mar;85(3):429–40. doi: 10.1124/mol.113.089821. PMID: 24342772.; Tanji H, Ohto U, Shibata T, Miyake K, Shimizu T. Structural reorganization of the Toll-like receptor 8 dimer induced by agonistic ligands. Science. 2013 Mar 22;339(6126):1426–9. doi: 10.1126/science.1229159. PMID: 23520111.; Li Y, Chen M, Cao H, Zhu Y, Zheng J, Zhou H. Extraordinary GU-rich single-strand RNA identified from SARS coronavirus contributes an excessive innate immune response. Microbes and Infection. 2013 Feb;15(2):88–95. doi: 10.1016/j.micinf.2012.10.008.; Melén K, Kinnunen L, Fagerlund R, Ikonen N, Twu KY, Krug RM, Julkunen I. Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes. J Virol. 2007 Jun;81(11):5995–6006. PMID: 17376915; PMCID: PMC1900311.; Dauber B, Schneider J, Wolff T. Double-stranded RNA binding of influenza B virus nonstructural NS1 protein inhibits protein kinase R but is not essential to antagonize production of alpha/beta interferon. J Virol. 2006 Dec;80(23):11667–77. PMID: 16987984; PMCID: PMC1642593.; Cervantes-Barragan L, Züst R, Weber F, Spiegel M, Lang KS, Akira S, Thiel V, Ludewig B. Control of coronavirus infection through plasmacytoid dendritic-cell-derived type I interferon. Blood. 2007 Feb 01;109(3):1131–7. PMID: 16985170; PMCID: PMC8254533.; Li S, Min JY, Krug RM, Sen GC. Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA. Virology. 2006 May 25;349(1):13–21. doi: 10.1016/j.virol.2006.01.005. PMID: 16466763.; Gorden KB, Gorski KS, Gibson SJ, Kedl RM, Kieper WC, Qiu X, Tomai MA, Alkan SS, Vasilakos JP. Synthetic TLR agonists reveal functional differences between human TLR7 and TLR8. J Immunol. 2005 Feb 01;174(3):1259–68. doi: 10.4049/jimmunol.174.3.1259. PMID: 15661881.; Cros JF, García-Sastre A, Palese P. An unconventional NLS is critical for the nuclear import of the influenza A virus nucleoprotein and ribonucleoprotein. Traffic. 2005 Mar;6(3):205–13. doi: 10.1111/j.1600-0854.2005.00263.x. PMID: 15702989.; Diebold SS, Kaisho T, Hemmi H, Akira S, Reis e Sousa C. Innate antiviral responses by means of TLR7-mediated recognition of single-stranded RNA. Science. 2004 Mar 05;303(5663):1529–31. doi: 10.1126/science.1093616. PMID: 14976261.; Heil F, Hemmi H, Hochrein H, Ampenberger F, Kirschning C, Akira S, Lipford G, Wagner H, Bauer S. Species-specific recognition of single-stranded RNA via toll-like receptor 7 and 8. Science. 2004 Mar 05;303(5663):1526–9. doi: 10.1126/science.1093620. PMID: 14976262.; Jurk M, Heil F, Vollmer J, Schetter C, Krieg AM, Wagner H, Lipford G, Bauer S. Human TLR7 or TLR8 independently confer responsiveness to the antiviral compound R-848. Nat Immunol. 2002 Jun;3(6):499. doi: 10.1038/ni0602-499. PMID: 12032557.; Hemmi H, Kaisho T, Takeuchi O, Sato S, Sanjo H, Hoshino K, Horiuchi T, Tomizawa H, Takeda K, Akira S. Small anti-viral compounds activate immune cells via the TLR7 MyD88-dependent signaling pathway. Nat Immunol. 2002 Feb;3(2):196–200. doi: 10.1038/ni758. PMID: 11812998.; Bergmann M, Garcia-Sastre A, Carnero E, Pehamberger H, Wolff K, Palese P, Muster T. Influenza Virus NS1 Protein Counteracts PKR-Mediated Inhibition of Replication. J Virol. 2000 Jul;74(13):6203–6. doi: 10.1128/jvi.74.13.6203-6206.2000.; Hatada E, Saito S, Fukuda R. Mutant Influenza Viruses with a Defective NS1 Protein Cannot Block the Activation of PKR in Infected Cells. J Virol. 1999 Mar;73(3):2425–33. doi: 10.1128/jvi.73.3.2425-2433.1999.; TAN S, KATZE MG. Biochemical and Genetic Evidence for Complex Formation Between the Influenza A Virus NS1 Protein and the Interferon-induced PKR Protein Kinase. Journal of Interferon & Cytokine Research. 1998 Sep;18(9):757–66. doi: 10.1089/jir.1998.18.757.; O'Neill RE, Jaskunas R, Blobel G, Palese P, Moroianu J. Nuclear Import of Influenza Virus RNA Can Be Mediated by Viral Nucleoprotein and Transport Factors Required for Protein Import. Journal of Biological Chemistry. 1995 Sep;270(39):22701–4. doi: 10.1074/jbc.270.39.22701.

Metabolites

2,5-Dihydroxybenzoate

Formula: C7H6O4 (154.0266076)

CAS ID: 490-79-9

3',5'-Cyclic diGMP

Formula: C20H24N10O14P2 (690.0948664)

CAS ID: 61093-23-0

beta-D-Glucose

Formula: C6H12O6 (180.0633852)

CAS ID: 492-61-5

Calcium cation

Formula: Ca (39.962591)

CAS ID: 14127-61-8

Cholesterol

Formula: C27H46O (386.3548466)

CAS ID: 57-88-5

Choline

Formula: C5H14NO (104.10753340000001)

CAS ID: 62-49-7

Choline phosphate

Formula: C5H15NO4P (184.07386599999998)

CAS ID: 107-73-3

Cl-

Formula: Cl (34.968853)

CAS ID: 16887-00-6

CO2

Formula: CO2 (43.98983)

CAS ID: 124-38-9

Cu+

Formula: Cu (62.929599)

CAS ID: 17493-86-6

Fe2+

Formula: Fe (55.934939)

CAS ID: 15438-31-0

Fe3+

Formula: Fe (55.934939)

CAS ID: 7439-89-6

H+

Formula: H (1.0078246)

CAS ID: 12408-02-5

H2O

Formula: H2O (18.0105642)

CAS ID: 7732-18-5

HO-

Formula: OH (17.0027396)

CAS ID: 14280-30-9

Hydrogen peroxide

Formula: H2O2 (34.0054792)

CAS ID: 7722-84-1

Hydroperoxyl radical

Formula: HO2 (32.997654600000004)

CAS ID: 3170-83-0

Hydroxyl radical

Formula: OH (17.0027396)

CAS ID: 3352-57-6

Hypochlorous acid

Formula: HClO (51.9715926)

CAS ID: 7790-92-3

Magnesium cation

Formula: Mg (23.98505)

CAS ID: 22537-22-0

Manganese(2+)

Formula: Mn (54.938046)

CAS ID: 7439-96-5

N-Acetyl-beta-D-glucosamine

Formula: C8H15NO6 (221.089933)

CAS ID: 14131-68-1

N-Acetylmuramate

Formula: C11H19NO8 (293.1110614)

CAS ID: 61633-75-8

NADP+

Formula: C21H29N7O17P3 (744.0832754)

CAS ID: 53-59-8

NADPH

Formula: C21H30N7O17P3 (745.0911)

CAS ID: 2646-71-1

Nitric oxide

Formula: NO (29.997989)

CAS ID: 10102-43-9

Nitrite

Formula: HNO2 (47.0007286)

CAS ID: 14797-65-0

Oxygen

Formula: O2 (31.98983)

CAS ID: 7782-44-7

Potassium cation

Formula: K (38.963708)

CAS ID: 24203-36-9

Sodium cation

Formula: Na (22.98977)

CAS ID: 17341-25-2

Superoxide

Formula: O2 (31.98983)

CAS ID: 11062-77-4

Zinc cation

Formula: Zn (63.929145)

CAS ID: 23713-49-7

Thiocyanate

Formula: CNS (57.975145999999995)

CAS ID: 302-04-5

S-Nitrosoglutathione

Formula: C10H16N4O7S (336.0739666)

CAS ID: 57564-91-7

Hypothiocyanite

Formula: CHNOS (74.9778856)

CAS ID: 63296-34-4

L-argininium(1+)

Formula: C6H15N4O2 (175.119495)

CAS ID: 17806-42-7

Dinitrogen trioxide

Formula: N2O3 (75.990893)

CAS ID: 10544-73-7

carbonate

Formula: CO3 (59.984745000000004)

CAS ID: 3812-32-6

nitrite

Formula: NO2 (45.992904)

CAS ID: 14797-65-0

NADPH(4-)

Formula: C21H26N7O17P3 (741.0598016)

CAS ID: 53-57-6

ATP(4-)

Formula: C10H12N5O13P3 (502.9644492)

CAS ID:

GTP(4-)

Formula: C10H12N5O14P3 (518.9593642)

CAS ID: 86527-72-2

NAD(1-)

Formula: C21H26N7O14P2 (662.1012936000001)

CAS ID: 53-84-9

UDP(3-)

Formula: C9H11N2O12P2 (400.9787246)

CAS ID: 86527-70-0

ADP(3-)

Formula: C10H12N5O10P2 (424.0059412)

CAS ID:

3',5'-cyclic AMP(1-)

Formula: C10H11N5O6P (328.0446936)

CAS ID: 62906-31-4

NADP(3-)

Formula: C21H25N7O17P3 (740.051977)

CAS ID: 53-59-8

dTMP(2-)

Formula: C10H13N2O8P (320.0409508)

CAS ID: 14057-65-9

oxidonitrogen(1+)

Formula: NO (29.997989)

CAS ID: 14452-93-8



Enzyme

EC Number name full name note
1.6.3.-
1.11.1.7 peroxidase phenolic donor:hydrogen-peroxide oxidoreductase
1.11.2.2 myeloperoxidase chloride:hydrogen-peroxide oxidoreductase (hypochlorite-forming)
1.14.14.18 heme oxygenase (biliverdin-producing) protoheme,NADPH-hemoprotein reductase:oxygen oxidoreductase (alpha-methene-oxidizing, hydroxylating)
1.14.99.1 prostaglandin-endoperoxide synthase (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate,hydrogen-donor:oxygen oxidoreductase
1.15.1.1 superoxide dismutase superoxide:superoxide oxidoreductase
1.17.1.4 xanthine dehydrogenase xanthine:NAD+ oxidoreductase
1.17.3.2 xanthine oxidase xanthine:oxygen oxidoreductase
1.20.4.2 methylarsonate reductase glutathione:methylarsonate oxidoreductase
1.3.1.91 tRNA-dihydrouridine20 synthase [NAD(P)+] tRNA-5,6-dihydrouracil20:NAD(P)+ oxidoreductase
1.4.3.21 primary-amine oxidase primary-amine:oxygen oxidoreductase (deaminating)
1.4.3.4 monoamine oxidase amine:oxygen oxidoreductase (deaminating)
1.8.5.1 glutathione dehydrogenase (ascorbate) glutathione:dehydroascorbate oxidoreductase
2.1.1.356 [histone H3]-lysine27 N-trimethyltransferase S-adenosyl-L-methionine:[histone H3]-L-lysine27 N6-methyltransferase
2.1.1.364 [histone H3]-lysine4 N-methyltransferase S-adenosyl-L-methionine:[histone H3]-L-lysine4 N6-methyltransferase
2.1.1.56 mRNA (guanine-N7)-methyltransferase S-adenosyl-L-methionine:mRNA (guanine-N7)-methyltransferase
2.2.1.2 transaldolase sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase
2.3.1.48 histone acetyltransferase acetyl-CoA:[protein]-L-lysine acetyltransferase
2.3.2.23 E2 ubiquitin-conjugating enzyme S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine:[E2 ubiquitin-conjugating enzyme] ubiquitinyl transferase
2.3.2.26 HECT-type E3 ubiquitin transferase [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming)
2.3.2.27 RING-type E3 ubiquitin transferase [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming; RING-type)
2.3.2.31 RBR-type E3 ubiquitin transferase [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:acceptor protein ubiquitin transferase (isopeptide bond-forming; RBR-type)
2.3.2.32 cullin-RING-type E3 NEDD8 transferase [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine:[cullin] [NEDD8-protein] transferase (isopeptide bond-forming; RING-type)
2.3.2.34 E2 NEDD8-conjugating enzyme [E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine:[E2 NEDD8-conjugating enzyme] [NEDD8-protein]-yl transferase
2.4.1.146 beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase UDP-N-acetyl-alpha-D-glucosamine:3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl/threonyl-[protein] 3-beta-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
2.4.1.149 N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase UDP-N-acetyl-alpha-D-glucosamine:beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R 3-beta N-acetylglucosaminyltransferase (configuration-inverting)
2.4.2.28 S-methyl-5'-thioadenosine phosphorylase S-methyl-5'-thioadenosine:phosphate S-methyl-5-thio-alpha-D-ribosyl-transferase
2.4.2.31 NAD+-protein-arginine ADP-ribosyltransferase NAD+:protein-L-arginine ADP-D-ribosyltransferase
2.5.1.18 glutathione transferase RX:glutathione R-transferase
2.5.1.58 protein farnesyltransferase farnesyl-diphosphate:protein-cysteine farnesyltransferase
2.5.1.59 protein geranylgeranyltransferase type I geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
2.7.1.137 phosphatidylinositol 3-kinase ATP:1-phosphatidyl-1D-myo-inositol 3-phosphotransferase
2.7.1.153 phosphatidylinositol-4,5-bisphosphate 3-kinase ATP:1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate 3-phosphotransferase
2.7.1.154 phosphatidylinositol-4-phosphate 3-kinase ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 3-phosphotransferase
2.7.1.28 triokinase ATP:D-glyceraldehyde 3-phosphotransferase
2.7.1.29 glycerone kinase ATP:glycerone phosphotransferase
2.7.1.91 sphingosine kinase ATP:sphingoid base 1-phosphotransferase
2.7.10.1 receptor protein-tyrosine kinase ATP:[protein]-L-tyrosine O-phosphotransferase (receptor-type)
2.7.10.2 non-specific protein-tyrosine kinase ATP:[protein]-L-tyrosine O-phosphotransferase (non-specific)
2.7.11.1 non-specific serine/threonine protein kinase ATP:protein phosphotransferase (non-specific)
2.7.11.10 IkappaB kinase ATP:[IkappaB protein] phosphotransferase
2.7.11.11 cAMP-dependent protein kinase ATP:protein Ser/Thr-phosphotransferase (3',5'-cAMP-dependent)
2.7.11.13 protein kinase C ATP:protein phosphotransferase (diacylglycerol-dependent)
2.7.11.22 cyclin-dependent kinase ATP:cyclin phosphotransferase
2.7.11.23 [RNA-polymerase]-subunit kinase ATP:[DNA-directed RNA polymerase] phosphotransferase
2.7.11.24 mitogen-activated protein kinase ATP:protein phosphotransferase (MAPKK-activated)
2.7.11.25 mitogen-activated protein kinase kinase kinase ATP:protein phosphotransferase (MAPKKKK-activated)
2.7.11.26 tau-protein kinase ATP:[tau-protein] O-phosphotransferase
2.7.12.2 mitogen-activated protein kinase kinase ATP:protein phosphotransferase (MAPKKK-activated)
2.7.7.50 mRNA guanylyltransferase GTP:mRNA guanylyltransferase
2.7.7.6 DNA-directed RNA polymerase nucleoside-triphosphate:RNA nucleotidyltransferase (DNA-directed)
2.7.7.84 2'-5' oligoadenylate synthase ATP:ATP adenylyltransferase (2'-5' linkages-forming)
2.7.7.86 cyclic GMP-AMP synthase ATP:GTP adenylyltransferase (cyclizing)
3.1.1.4 phospholipase A2 phosphatidylcholine 2-acylhydrolase
3.1.1.5 lysophospholipase 2-lysophosphatidylcholine acylhydrolase
3.1.11.2 exodeoxyribonuclease III
3.1.13.1 exoribonuclease II
3.1.13.4 poly(A)-specific ribonuclease
3.1.2.2 palmitoyl-CoA hydrolase palmitoyl-CoA hydrolase
3.1.3.16 protein-serine/threonine phosphatase protein-serine/threonine-phosphate phosphohydrolase
3.1.3.36 phosphoinositide 5-phosphatase phosphatidyl-myo-inositol-4,5-bisphosphate 4-phosphohydrolase
3.1.3.48 protein-tyrosine-phosphatase protein-tyrosine-phosphate phosphohydrolase
3.1.3.56 inositol-polyphosphate 5-phosphatase 1D-myo-inositol-1,4,5-trisphosphate 5-phosphohydrolase
3.1.3.67 phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase 1-phosphatidyl-1D-myo-inositol-3,4,5-trisphosphate 3-phosphohydrolase
3.1.3.86 phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1-phosphatidyl-1D-myo-inositol-3,4,5-trisphosphate 5-phosphohydrolase
3.1.4.11 phosphoinositide phospholipase C 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase
3.2.1.17 lysozyme peptidoglycan N-acetylmuramoylhydrolase
3.2.2.6 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase NAD+ glycohydrolase (cyclic ADP-ribose-forming)
3.4.11.3 cystinyl aminopeptidase
3.4.19.12 ubiquitinyl hydrolase 1
3.4.21.20 cathepsin G
3.4.21.41 complement subcomponent C1r
3.4.21.42 complement subcomponent C1s
3.4.21.43 classical-complement-pathway C3/C5 convertase
3.4.21.45 complement factor I
3.4.21.47 alternative-complement-pathway C3/C5 convertase
3.4.21.75 Furin
3.4.21.76 Myeloblastin
3.4.22.34 Legumain
3.4.22.36 caspase-1
3.4.22.56 caspase-3
3.4.22.57 caspase-4
3.4.22.58 caspase-5
3.4.22.61 caspase-8
3.4.22.63 caspase-10
3.4.24.15 thimet oligopeptidase
3.4.24.86 ADAM 17 endopeptidase
3.4.25.1 proteasome endopeptidase complex
3.5.1.28 N-acetylmuramoyl-L-alanine amidase peptidoglycan amidohydrolase
3.5.4.37 double-stranded RNA adenine deaminase double-stranded RNA(adenine) aminohydrolase
3.6.4.10 non-chaperonin molecular chaperone ATPase ATP phosphohydrolase (polypeptide-polymerizing)
3.6.4.12 DNA helicase
3.6.4.13 RNA helicase
3.6.4.6 vesicle-fusing ATPase ATP phosphohydrolase (vesicle-fusing)
3.6.5.2 small monomeric GTPase GTP phosphohydrolase (cell-regulating)
3.6.5.3 protein-synthesizing GTPase GTP phosphohydrolase (mRNA-translation-assisting)
4.2.1.1 carbonic anhydrase carbonic acid hydro-lyase (carbon-dioxide-forming)
4.2.1.69 cyanamide hydratase urea hydro-lyase (cyanamide-forming)
4.2.99.18 DNA-(apurinic or apyrimidinic site) lyase DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase
4.6.1.15 FAD-AMP lyase (cyclizing) FAD AMP-lyase (riboflavin-cyclic-4',5'-phosphate-forming)
5.2.1.8 peptidylprolyl isomerase Peptidylproline cis-trans-isomerase
5.3.2.1 phenylpyruvate tautomerase phenylpyruvate keto---enol-isomerase
5.3.3.12 L-dopachrome isomerase L-dopachrome keto-enol isomerase
5.3.4.1 protein disulfide-isomerase Protein disulfide-isomerase
5.6.2.4 DNA 3'-5' helicase DNA 3'-5' helicase (ATP-hydrolysing)
6.2.1.64 E1 NEDD8-activating enzyme [NEDD8 protein]:[E1 NEDD8-activating enzyme] ligase (AMP-forming)
7.2.2.8 P-type Cu+ transporter ATP phosphohydrolase (P-type, Cu+-exporting)
7.4.2.14 ABC-type antigen peptide transporter ATP phosphohydrolase (ABC-type, antigen peptide-exporting)


Proteins

Protein ID name full name
A0A0H2US87 ospC3 Arginine ADP-riboxanase OspC3