DB code: M00216
| RLCP classification | 1.13.30000.41 : Hydrolysis | |
|---|---|---|
| CATH domain | 3.90.70.- : Cathepsin B; Chain A | |
| 4.10.90.10 : Foot-And-Mouth Disease Virus, subunit 4 | ||
| 2.60.120.10 : Jelly Rolls | ||
| 2.60.120.10 : Jelly Rolls | ||
| 2.60.120.10 : Jelly Rolls | ||
| -.-.-.- : | ||
| -.-.-.- : | ||
| -.-.-.- : | ||
| -.-.-.- : | ||
| -.-.-.- : | ||
| -.-.-.- : | ||
| -.-.-.- : | ||
| 2.40.10.10 : Thrombin, subunit H | Catalytic domain | |
| 2.40.10.10 : Thrombin, subunit H | Catalytic domain | |
| 3.90.-.- : | ||
| 3.30.-.- : | ||
| 1.20.-.- : | ||
| 1.10.-.- : | ||
| E.C. | 3.4.22.46 3.6.1.15 3.4.22.28 2.7.7.48 | |
| CSA | 2bhg | |
| M-CSA | 2bhg | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 2.40.10.10 : Thrombin, subunit H | M00139 D00214 M00167 D00426 M00133 D00428 D00429 D00430 D00431 D00432 D00433 D00434 D00435 M00227 M00209 D00194 D00197 D00211 D00212 D00216 M00212 D00224 D00497 M00217 D00528 D00848 D00850 D00851 D00852 D00855 M00152 M00155 M00157 M00181 M00315 M00316 M00317 M00348 M00349 T00074 T00410 T00411 |
| 2.60.120.10 : Jelly Rolls | S00145 S00155 D00842 D00843 T00255 T00101 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Contains | MEROPS | Pfam |
|---|---|---|---|---|---|
| P03306 |
Genome polyprotein
|
None |
(P3A)
Protein 3B-1 (P3B-1) Genome-linked protein VPg1 Protein 3B-2 (P3B-2) Genome-linked protein VPg2 Protein 3B-3 (P3B-3) Genome-linked protein VPg3 Picornain 3C EC 3.4.22.28 Protease 3C (P3C) Protease P20B RNA-directed RNA polymerase 3D-POL (P3D-POL) EC 2.7.7.48 P56A Leader protease (Lpro) EC 3.4.22.46 Protein VP0 VP4-VP2 Protein VP4 Virion protein 4 P1A Protein VP2 Virion protein 2 P1B Protein VP3 Virion protein 3 P1C Protein VP1 Virion protein 1 P1D Protein 2A (P2A) P52 Protein 2B (P2B) Protein 2C (P2C) EC 3.6.1.15 Protein 3A |
C03.008
(Cysteine)
|
PF05408
(Peptidase_C28)
PF00548 (Peptidase_C3) PF00680 (RdRP_1) PF00073 (Rhv) PF00910 (RNA_helicase) PF08935 (VP4_2) [Graphical View] |
| KEGG enzyme name |
|---|
|
L-peptidase
(EC 3.4.22.46 ) nucleoside-triphosphatase (EC 3.6.1.15 ) nucleoside triphosphate phosphohydrolase (EC 3.6.1.15 ) nucleoside-5-triphosphate phosphohydrolase (EC 3.6.1.15 ) nucleoside 5-triphosphatase (EC 3.6.1.15 ) picornain 3C (EC 3.4.22.28 ) picornavirus endopeptidase 3C (EC 3.4.22.28 ) poliovirus protease 3C (EC 3.4.22.28 ) rhinovirus protease 3C (EC 3.4.22.28 ) foot-and-mouth protease 3C (EC 3.4.22.28 ) poliovirus proteinase 3C (EC 3.4.22.28 ) rhinovirus proteinase 3C (EC 3.4.22.28 ) coxsackievirus 3C proteinase (EC 3.4.22.28 ) foot-and-mouth-disease virus proteinase 3C (EC 3.4.22.28 ) 3C protease (EC 3.4.22.28 ) 3C proteinase (EC 3.4.22.28 ) cysteine proteinase 3C (EC 3.4.22.28 ) hepatitis A virus 3C proteinase (EC 3.4.22.28 ) protease 3C (EC 3.4.22.28 ) tomato ringspot nepovirus 3C-related protease (EC 3.4.22.28 ) RNA-directed RNA polymerase (EC 2.7.7.48 ) RNA nucleotidyltransferase (RNA-directed) (EC 2.7.7.48 ) RNA nucleotidyltransferase (RNA-directed) (EC 2.7.7.48 ) RNA-dependent ribonucleate nucleotidyltransferase (EC 2.7.7.48 ) 3D polymerase (EC 2.7.7.48 ) PB1 proteins (EC 2.7.7.48 ) PB2 proteins (EC 2.7.7.48 ) phage f2 replicase (EC 2.7.7.48 ) polymerase L (EC 2.7.7.48 ) Q-beta replicase (EC 2.7.7.48 ) phage f2 replicase (EC 2.7.7.48 ) ribonucleic acid replicase (EC 2.7.7.48 ) ribonucleic acid-dependent ribonucleate nucleotidyltransferase (EC 2.7.7.48 ) ribonucleic acid-dependent ribonucleic acid polymerase (EC 2.7.7.48 ) ribonucleic replicase (EC 2.7.7.48 ) ribonucleic synthetase (EC 2.7.7.48 ) RNA replicase (EC 2.7.7.48 ) RNA synthetase (EC 2.7.7.48 ) RNA transcriptase (EC 2.7.7.48 ) RNA-dependent ribonucleate nucleotidyltransferase (EC 2.7.7.48 ) RDRP (EC 2.7.7.48 ) RNA-dependent RNA polymerase (EC 2.7.7.48 ) RNA-dependent RNA replicase (EC 2.7.7.48 ) transcriptase (EC 2.7.7.48 ) |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P03306 | POLG_FMDV1 | Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF- 4G at bonds -Gly-|-Arg- and -Lys-|-Arg-. NTP + H(2)O = NDP + phosphate. Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). | Protein VP2: Virion. Cytoplasm (Potential). Protein VP3: Virion. Cytoplasm (Potential). Protein VP1: Virion. Cytoplasm (Potential). Protein 2B: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity). Protein 2C: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity). Protein 3A: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity). Protein 3B-1: Virion (Potential). Protein 3B-2: Virion (Potential). Protein 3B-3: Virion (Potential). Picornain 3C: Cytoplasm (Potential). RNA-directed RNA polymerase 3D-POL: Cytoplasmic vesicle membrane, Peripheral membrane protein, Cytoplasmic side (Potential). Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity). |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00230 | Purine metabolism | 3.6.1.15 2.7.7.48 |
| MAP00730 | Thiamine metabolism | 3.6.1.15 |
| Compound table | ||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | ||||||||||||||
| KEGG-id | C00017 | C00001 | C00201 | C00046 | C00017 | C00012 | C00454 | C00009 | C00046 | C00013 | ||||||
| E.C. |
3.4.22.46
3.4.22.28 |
3.4.22.46
3.4.22.28 3.6.1.15 |
3.6.1.15
2.7.7.48 |
2.7.7.48
|
3.4.22.46
3.4.22.28 |
3.4.22.46
3.4.22.28 |
3.6.1.15
|
3.6.1.15
|
2.7.7.48
|
2.7.7.48
|
||||||
| Compound | Protein | H2O | Nucleoside triphosphate | RNA(n) | Protein | Peptide | Nucleoside diphosphate | Phosphate | RNA(n+1) | Diphosphate | ||||||
| Type | peptide/protein | H2O | nucleotide | nucleic acids | peptide/protein | peptide/protein | nucleotide | phosphate group/phosphate ion | nucleic acids | phosphate group/phosphate ion | ||||||
| ChEBI |
15377 15377 |
26078 26078 |
29888 29888 |
|||||||||||||
| PubChem |
22247451 962 22247451 962 |
1004 22486802 1004 22486802 |
1023 21961011 1023 21961011 |
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| 1zba4 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1zbe4 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1zba2 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1zbe2 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1zba3 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1zbe3 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1zba1 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1zbe1 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2bhgA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2bhgB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2bhgA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2bhgB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P03306 & literature [9] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1zba4 |
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| 1zbe4 |
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| 1zba2 |
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| 1zbe2 |
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| 1zba3 |
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| 1zbe3 |
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| 1zba1 |
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| 1zbe1 |
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| 2bhgA01 |
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HIS 46;ASP 84 | ||||
| 2bhgB01 |
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HIS 46;ASP 84 | ||||
| 2bhgA02 |
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GLY 161 | mutant C163A | |||
| 2bhgB02 |
|
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|
|
GLY 161 | mutant C163A | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[2]
|
p.110 | |
|
[9]
|
p.11524 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3186696 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1988 |
| Volume | 85 |
| Pages | 7872-6 |
| Authors | Bazan JF, Fletterick RJ |
| Title | Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2645167 |
| Journal | FEBS Lett |
| Year | 1989 |
| Volume | 243 |
| Pages | 103-14 |
| Authors | Gorbalenya AE, Donchenko AP, Blinov VM, Koonin EV |
| Title |
Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8320292 |
| Journal | J Chem Inf Comput Sci |
| Year | 1993 |
| Volume | 33 |
| Pages | 345-9 |
| Authors | Arad D, Kreisberg R, Shokhen M |
| Title | Structural and mechanistic aspects of 3C proteases from the Picornavirus family. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8164744 |
| Journal | Nature |
| Year | 1994 |
| Volume | 369 |
| Pages | 72-6 |
| Authors | Allaire M, Chernaia MM, Malcolm BA, James MN |
| Title | Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7491782 |
| Journal | Virology |
| Year | 1995 |
| Volume | 213 |
| Pages | 581-9 |
| Authors | Grubman MJ, Zellner M, Bablanian G, Mason PW, Piccone ME |
| Title | Identification of the active-site residues of the 3C proteinase of foot-and-mouth disease virus. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9060667 |
| Journal | J Virol |
| Year | 1997 |
| Volume | 71 |
| Pages | 3062-8 |
| Authors | Gosert R, Dollenmaier G, Weitz M |
| Title | Identification of active-site residues in protease 3C of hepatitis A virus by site-directed mutagenesis. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12036580 |
| Journal | Gene |
| Year | 2002 |
| Volume | 289 |
| Pages | 19-29 |
| Authors | van Rensburg H, Haydon D, Joubert F, Bastos A, Heath L, Nel L |
| Title | Genetic heterogeneity in the foot-and-mouth disease virus Leader and 3C proteinases. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12377789 |
| Journal | J Biol Chem |
| Year | 2002 |
| Volume | 277 |
| Pages | 50564-72 |
| Authors | Phan J, Zdanov A, Evdokimov AG, Tropea JE, Peters HK 3rd, Kapust RB, Li M, Wlodawer A, Waugh DS |
| Title | Structural basis for the substrate specificity of tobacco etch virus protease. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 15654079 |
| Journal | J Biol Chem |
| Year | 2005 |
| Volume | 280 |
| Pages | 11520-7 |
| Authors | Birtley JR, Knox SR, Jaulent AM, Brick P, Leatherbarrow RJ, Curry S |
| Title |
Crystal structure of foot-and-mouth disease virus 3C protease. |
| Related PDB | 2bhg |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 16288920 |
| Journal | J Mol Biol |
| Year | 2005 |
| Volume | 354 |
| Pages | 854-71 |
| Authors | Yin J, Bergmann EM, Cherney MM, Lall MS, Jain RP, Vederas JC, James MN |
| Title | Dual modes of modification of hepatitis A virus 3C protease by a serine-derived beta-lactone: selective crystallization and formation of a functional catalytic triad in the active site. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
The enzymes in this entry are parts of genome polyprotein from foot-and-mouth disease virus, The tertiary structures for the 4 coat proteins (PDB; 1zba, The enzyme (picornain 3C; EC 3.4.22.28) cleaves GLN/GLU-|-GLY/SER/THR bonds in its polyprotein. The catalytic mechanism of this enzyme seems to be similar to that of trypsin (D00197 in EzCatDB), |
| Created | Updated |
|---|---|
| 2006-07-11 | 2009-02-26 |