M00206
type: Enzyme
active site residues resources: P16088
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/-.-.-.-
cath: Cathepsin D, subunit A; domain 1
cath: HIV Type 1 Reverse Transcriptase; Chain A, domain 1
cath: Alpha-Beta Plaits
cath: Nucleotidyltransferase; domain 5
cath: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A
cath: Arc Repressor Mutant, subunit A
cath: SH3 type barrels.
ec: https://purl.uniprot.org/enzyme/3.4.23.-
ec: https://purl.uniprot.org/enzyme/2.7.7.49
ec: https://purl.uniprot.org/enzyme/3.1.26.4
ec: https://purl.uniprot.org/enzyme/3.6.1.23
kegg cofactor: Magnesium
kegg enzyme: RNA-directed DNA polymerase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.49
kegg enzyme: DNA nucleotidyltransferase (RNA-directed)
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.49
kegg enzyme: reverse transcriptase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.49
kegg enzyme: revertase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.49
kegg enzyme: RNA-dependent deoxyribonucleate nucleotidyltransferase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.49
kegg enzyme: RNA revertase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.49
kegg intermediate: Amino-diol-tetrahedral intermediate
kegg pathway: Pyrimidine metabolism
kegg product: Protein
kegg product: Peptide
kegg product: DNA(n)
kegg product: RNA 5'-phosphate
kegg product: dUMP
kegg product: Pyrophosphate
kegg substrate: Protein
kegg substrate: Peptide
kegg substrate: Deoxynucleoside triphosphate
kegg substrate: DNA(n)
kegg substrate: RNA
kegg substrate: dUTP
kegg substrate: H2O
pdb: 1b11A
pdb: 1fivA
pdb: 2fivA
pdb: 3fivA
pdb: 4fivA
pdb: 5fivA
pdb: 6fivA
pdb: 2fivB
pdb: 3fivB
pdb: 1dutA
pdb: 1dutB
pdb: 1f7dA
pdb: 1f7dB
pdb: 1f7kA
pdb: 1f7kB
pdb: 1f7nA
pdb: 1f7nB
pdb: 1f7oA
pdb: 1f7oB
pdb: 1f7oC
pdb: 1f7pA
pdb: 1f7pB
pdb: 1f7pC
pdb: 1f7qA
pdb: 1f7qB
pdb: 1f7qC
pdb: 1f7rA
rlcp: p966
uniprot: P16088
references: Structure of an inhibitor complex of the proteinase from feline immunodeficiency virus.
references: C2-symmetrical tetrahydroxyazepanes as inhibitors of glycosidases and HIV/FIV proteases.
references: Crystal structure of dUTP pyrophosphatase from feline immunodeficiency virus.
references: Crystal structures of the inactive D30N mutant of feline immunodeficiency virus protease complexed with a substrate and an inhibitor.
references: Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV.
references: Comparison of inhibitor binding to feline and human immunodeficiency virus proteases: structure-based drug design and the resistance problem.
references: Methodology for protein-ligand binding studies: application to a model for drug resistance, the HIV/FIV protease system.
references: Structure/function analysis of a dUTPase: catalytic mechanism of a potential chemotherapeutic target.
references: Structural studies of FIV and HIV-1 proteases complexed with an efficient inhibitor of FIV protease.
references: Structures of feline immunodeficiency virus dUTP pyrophosphatase and its nucleotide complexes in three crystal forms.
references: Design, synthesis, and biological evaluation of HIV/FIV protease inhibitors incorporating a conformationally constrained macrocycle with a small P3' residue.
references: Structural basis for distinctions between substrate and inhibitor specificities for feline immunodeficiency virus and human immunodeficiency virus proteases.
references: Inhibitor design by wrapping packing defects in HIV-1 proteins.
references: The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases.
comment: This enzyme is composed of retropepsin (EC 3.4.23.-), RNA-directed DNA polymerase (EC 2.7.7.49), RNase H (EC 3.1.26.4), dUTP pyrophosphatase (EC 3.6.1.23), and integrase. The tertiary structures have been solved only for retropepsin (EC 3.4.23.-) and dUTP pyrophosphatase (EC 3.6.1.23). The dUTP pyrophosphatase domain (EC 3.6.1.23) forms a trimer, which binds one Mg2+ ion (see PDB;1dut). The domains which corresponds to protease domain (EC 3.4.23.-) belong to the peptidase family-A2. Although this domain has a catalytic aspartic residue, it forms a homodimer with a single active site with a typical catalytic dyad, composed of two aspartic acid residues. According to the literature [4], the catalytic mechanism is very similar to that of pepsin (see D00436 in EzCatDB).

Arc Repressor Mutant, subunit A
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.10.200

SH3 type barrels.
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.30.30.10

Cathepsin D, subunit A; domain 1
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/2.40.70.10

Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A
type: Cath
catalytic domain: index.html
references: http://www.cathdb.info/version/latest/superfamily/2.70.40.10

HIV Type 1 Reverse Transcriptase; Chain A, domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.10.10.10

Nucleotidyltransferase; domain 5
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.420.10

Alpha-Beta Plaits
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.70.270

H2O
type: KeggSubstrate
compound type: H2O
ec: https://purl.uniprot.org/enzyme/3.4.23.-
ec: https://purl.uniprot.org/enzyme/3.1.26.4
ec: https://purl.uniprot.org/enzyme/3.6.1.23
references: KEGG:C00001
references: CHEBI:15377
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Pyrimidine metabolism
type: KeggPathway
ec: https://purl.uniprot.org/enzyme/3.6.1.23
references: KEGG:MAP00240

Structure of an inhibitor complex of the proteinase from feline immunodeficiency virus.
type: BibliographicResource
authors:
  item: Wlodawer A
  item: Bhatt D
  item: et al
  item: Gustchina A
  item: Reshetnikova L
  item: Lubkowski J
  item: Zdanov A
  item: Hui KY
  item: Angleton EL
  item: Farmerie WG
  item: Goodenow MM
journal: Nat Struct Biol
medline id: 95393228
pages: 480-8
published year: 1995
volume: 2
references: http://www.ncbi.nlm.nih.gov/pubmed/7664111
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P16088
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-154. Retropepsin (3.4.23.-)

Structures of feline immunodeficiency virus dUTP pyrophosphatase and its nucleotide complexes in three crystal forms.
type: BibliographicResource
authors:
  item: Prasad GS
  item: Stura EA
  item: Elder JH
  item: Stout CD
journal: Acta Crystallogr D Biol Crystallogr
pages: 1100-9
published year: 2000
volume: 56
references: http://www.ncbi.nlm.nih.gov/pubmed/10957629
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: dUTP pyrophosphatase (3.6.1.23)

Design, synthesis, and biological evaluation of HIV/FIV protease inhibitors incorporating a conformationally constrained macrocycle with a small P3' residue.
type: BibliographicResource
authors:
  item: Mak CC
  item: Le VD
  item: Lin YC
  item: Elder JH
  item: Wong CH
journal: Bioorg Med Chem Lett
pages: 219-22
published year: 2001
volume: 11
references: http://www.ncbi.nlm.nih.gov/pubmed/11206463
comment: Retropepsin (3.4.23.-)

Structural basis for distinctions between substrate and inhibitor specificities for feline immunodeficiency virus and human immunodeficiency virus proteases.
type: BibliographicResource
authors:
  item: Lin YC
  item: Beck Z
  item: Morris GM
  item: Olson AJ
  item: Elder JH
journal: J Virol
pages: 6589-600
published year: 2003
volume: 77
references: http://www.ncbi.nlm.nih.gov/pubmed/12767979
comment: Retropepsin (3.4.23.-)

Inhibitor design by wrapping packing defects in HIV-1 proteins.
type: BibliographicResource
authors:
  item: Fernandez A
  item: Rogale K
  item: Scott R
  item: Scheraga HA
journal: Proc Natl Acad Sci U S A
pages: 11640-5
published year: 2004
volume: 101
references: http://www.ncbi.nlm.nih.gov/pubmed/15289598
comment: Retropepsin (3.4.23.-)

The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases.
type: BibliographicResource
authors:
  item: Tarbouriech N
  item: Buisson M
  item: Seigneurin JM
  item: Cusack S
  item: Burmeister WP
journal: Structure
pages: 1299-310
published year: 2005
volume: 13
references: http://www.ncbi.nlm.nih.gov/pubmed/16154087
comment: dUTP pyrophosphatase (3.6.1.23)

C2-symmetrical tetrahydroxyazepanes as inhibitors of glycosidases and HIV/FIV proteases.
type: BibliographicResource
authors:
  item: Qian X
  item: Moris-Varas F
  item: Fitzgerald MC
  item: Wong CH
journal: Bioorg Med Chem
pages: 2055-69
published year: 1996
volume: 4
references: http://www.ncbi.nlm.nih.gov/pubmed/9022971
comment: Retropepsin (3.4.23.-)

Crystal structure of dUTP pyrophosphatase from feline immunodeficiency virus.
type: BibliographicResource
authors:
  item: Prasad GS
  item: Stura EA
  item: McRee DE
  item: Laco GS
  item: Hasselkus-Light C
  item: Elder JH
  item: Stout CD
journal: Protein Sci
pages: 2429-37
published year: 1996
volume: 5
references: http://www.ncbi.nlm.nih.gov/pubmed/8976551
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: dUTP pyrophosphatase (3.6.1.23)

Crystal structures of the inactive D30N mutant of feline immunodeficiency virus protease complexed with a substrate and an inhibitor.
type: BibliographicResource
authors:
  item: Laco GS
  item: Schalk-Hihi C
  item: Lubkowski J
  item: Morris G
  item: Zdanov A
  item: Olson A
  item: Elder JH
  item: Wlodawer A
  item: Gustchina A
journal: Biochemistry
medline id: 97419133
pages: 10696-708
published year: 1997
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/9271500
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P16088
comment: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-154. Retropepsin (3.4.23.-)

Toward a universal inhibitor of retroviral proteases: comparative analysis of the interactions of LP-130 complexed with proteases from HIV-1, FIV, and EIAV.
type: BibliographicResource
authors:
  item: Kervinen J
  item: Gustchina A
  item: Lubkowski J
  item: Zdanov A
  item: Bhatt D
  item: Dunn BM
  item: Hui KY
  item: Powell DJ
  item: Kay J
  item: Wlodawer A
journal: Protein Sci
pages: 2314-23
published year: 1998
volume: 7
references: http://www.ncbi.nlm.nih.gov/pubmed/9827997
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography. Retropepsin (3.4.23.-)

Comparison of inhibitor binding to feline and human immunodeficiency virus proteases: structure-based drug design and the resistance problem.
type: BibliographicResource
authors:
  item: Dunn BM
  item: Pennington MW
  item: Frase DC
  item: Nash K
journal: Biopolymers
pages: 69-77
published year: 1999
volume: 51
references: http://www.ncbi.nlm.nih.gov/pubmed/10380354
comment: Retropepsin (3.4.23.-)

Methodology for protein-ligand binding studies: application to a model for drug resistance, the HIV/FIV protease system.
type: BibliographicResource
authors:
  item: Dominy BN
  item: Brooks CL 3rd
journal: Proteins
pages: 318-31
published year: 1999
volume: 36
references: http://www.ncbi.nlm.nih.gov/pubmed/10409825
comment: Retropepsin (3.4.23.-)

Structure/function analysis of a dUTPase: catalytic mechanism of a potential chemotherapeutic target.
type: BibliographicResource
authors:
  item: Harris JM
  item: McIntosh EM
  item: Muscat GE
journal: J Mol Biol
pages: 275-87
published year: 1999
volume: 288
references: http://www.ncbi.nlm.nih.gov/pubmed/10329142
comment: dUTP pyrophosphatase (3.6.1.23)

Structural studies of FIV and HIV-1 proteases complexed with an efficient inhibitor of FIV protease.
type: BibliographicResource
authors:
  item: Li M
  item: Morris GM
  item: Lee T
  item: Laco GS
  item: Wong CH
  item: Olson AJ
  item: Elder JH
  item: Wlodawer A
  item: Gustchina A
journal: Proteins
pages: 29-40
published year: 2000
volume: 38
references: http://www.ncbi.nlm.nih.gov/pubmed/10651036
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
comment: X-ray crystallography. Retropepsin (3.4.23.-)

1f7kA
type: Pdb
catalytic residue: LYS 55;ASP 71;LYS 97;GLN 100
cofactor binding residue: ASP 64(magnesium binding)
main chain in catalysis: SER 56;SER 57
references: 1f7k
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7k
comment: (EC 3.6.1.23)

1f7kB
type: Pdb
catalytic residue: LYS 255;ASP 271;LYS 297;GLN 300
cofactor binding residue: ASP 264(magnesium binding)
main chain in catalysis: SER 256;SER 257
references: 1f7k
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7k
comment: (EC 3.6.1.23)

1f7nA
type: Pdb
catalytic residue: LYS 55;ASP 71;LYS 97;GLN 100
cofactor binding residue: ASP 64(magnesium binding)
main chain in catalysis: SER 56;SER 57
references: 1f7n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7n
comment: (EC 3.6.1.23)

1f7nB
type: Pdb
catalytic residue: LYS 255;ASP 271;LYS 297;GLN 300
cofactor binding residue: ASP 264(magnesium binding)
main chain in catalysis: SER 256;SER 257
references: 1f7n
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7n
comment: (EC 3.6.1.23)

1dutA
type: Pdb
catalytic residue: LYS 55;ASP 71;LYS 97;GLN 100
cofactor binding residue: ASP 64(magnesium binding)
main chain in catalysis: SER 56;SER 57
references: 1dut
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dut
comment: (EC 3.6.1.23)

1dutB
type: Pdb
catalytic residue: LYS 55;ASP 71;LYS 97;GLN 100
cofactor binding residue: ASP 64(magnesium binding)
main chain in catalysis: SER 56;SER 57
references: 1dut
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dut
comment: (EC 3.6.1.23)

1f7dA
type: Pdb
catalytic residue: LYS 55;ASP 71;LYS 97;GLN 100
cofactor binding residue: ASP 64(magnesium binding)
main chain in catalysis: SER 56;SER 57
references: 1f7d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7d
comment: (EC 3.6.1.23)

1f7dB
type: Pdb
catalytic residue: LYS 255;ASP 271;LYS 297;GLN 300
cofactor binding residue: ASP 264(magnesium binding)
main chain in catalysis: SER 256;SER 257
references: 1f7d
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7d
comment: (EC 3.6.1.23)

1f7qA
type: Pdb
catalytic residue: LYS 55;ASP 71;LYS 97;GLN 100
cofactor binding residue: ASP 64(magnesium binding)
main chain in catalysis: SER 56;SER 57
references: 1f7q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7q
comment: (EC 3.6.1.23)

1f7qC
type: Pdb
catalytic residue: LYS 455;ASP 471;LYS 497;GLN 500
cofactor binding residue: ASP 464(magnesium binding)
main chain in catalysis: SER 456;SER 457
references: 1f7q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7q
comment: (EC 3.6.1.23)

1f7rA
type: Pdb
catalytic residue: LYS 55;ASP 71;LYS 97;GLN 100
cofactor binding residue: ASP 64(magnesium binding)
main chain in catalysis: SER 56;SER 57
references: 1f7r
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7r
comment: (EC 3.6.1.23)

1b11A
type: Pdb
catalytic residue: ASP 30
references: 1b11
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1b11
comment: (EC 3.4.23.-)

1f7oA
type: Pdb
catalytic residue: LYS 55;ASP 71;LYS 97;GLN 100
cofactor binding residue: ASP 64(magnesium binding)
main chain in catalysis: SER 56;SER 57
references: 1f7o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7o
comment: (EC 3.6.1.23)

1f7oB
type: Pdb
catalytic residue: LYS 255;ASP 271;LYS 297;GLN 300
cofactor binding residue: ASP 264(magnesium binding)
main chain in catalysis: SER 256;SER 257
references: 1f7o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7o
comment: (EC 3.6.1.23)

1f7oC
type: Pdb
catalytic residue: LYS 455;ASP 471;LYS 497;GLN 500
cofactor binding residue: ASP 464(magnesium binding)
main chain in catalysis: SER 456;SER 457
references: 1f7o
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7o
comment: (EC 3.6.1.23)

1f7pA
type: Pdb
catalytic residue: LYS 55;ASP 71;LYS 97;GLN 100
cofactor binding residue: ASP 64(magnesium binding)
main chain in catalysis: SER 56;SER 57
references: 1f7p
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7p
comment: (EC 3.6.1.23)

1f7pB
type: Pdb
catalytic residue: LYS 255;ASP 271;LYS 297;GLN 300
cofactor binding residue: ASP 264(magnesium binding)
main chain in catalysis: SER 256;SER 257
references: 1f7p
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7p
comment: (EC 3.6.1.23)

1f7pC
type: Pdb
catalytic residue: LYS 455;ASP 471;LYS 497;GLN 500
cofactor binding residue: ASP 464(magnesium binding)
main chain in catalysis: SER 456;SER 457
references: 1f7p
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7p
comment: (EC 3.6.1.23)

1f7qB
type: Pdb
catalytic residue: LYS 255;ASP 271;LYS 297;GLN 300
cofactor binding residue: ASP 264(magnesium binding)
main chain in catalysis: SER 256;SER 257
references: 1f7q
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1f7q
comment: (EC 3.6.1.23)

1fivA
type: Pdb
catalytic residue: ASP 30
references: 1fiv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fiv
comment: (EC 3.4.23.-)

2fivA
type: Pdb
references: 2fiv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2fiv
comment: (EC 3.4.23.-) mutant D30N

2fivB
type: Pdb
references: 2fiv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2fiv
comment: (EC 3.4.23.-) mutant D30N

3fivA
type: Pdb
references: 3fiv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3fiv
comment: (EC 3.4.23.-) mutant D30N

3fivB
type: Pdb
references: 3fiv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3fiv
comment: (EC 3.4.23.-) mutant D30N

4fivA
type: Pdb
catalytic residue: ASP 30
references: 4fiv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:4fiv
comment: (EC 3.4.23.-)

5fivA
type: Pdb
catalytic residue: ASP 30
references: 5fiv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:5fiv
comment: (EC 3.4.23.-)

6fivA
type: Pdb
catalytic residue: ASP 30
references: 6fiv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:6fiv
comment: (EC 3.4.23.-)

Magnesium
type: KeggCofactor
compound type: divalent metal (Ca2+, Mg2+)
references: KEGG:C00305
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

dUMP
type: KeggProduct
compound type: amide group
compound type: nucleotide
ec: https://purl.uniprot.org/enzyme/3.6.1.23
references: KEGG:C00365
references: CHEBI:17622
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

dUTP
type: KeggSubstrate
compound type: amide group
compound type: nucleotide
ec: https://purl.uniprot.org/enzyme/3.6.1.23
references: KEGG:C00460
references: CHEBI:17625
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Pyrophosphate
type: KeggProduct
compound type: phosphate group/phosphate ion
ec: https://purl.uniprot.org/enzyme/2.7.7.49
ec: https://purl.uniprot.org/enzyme/3.6.1.23
references: KEGG:C00013
references: CHEBI:29888
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

RNA
type: KeggSubstrate
compound type: nucleic acids
ec: https://purl.uniprot.org/enzyme/3.1.26.4
references: KEGG:C00046

Deoxynucleoside triphosphate
type: KeggSubstrate
compound type: nucleotide
ec: https://purl.uniprot.org/enzyme/2.7.7.49
references: KEGG:C00677

RNA 5'-phosphate
type: KeggProduct
compound type: nucleic acids
compound type: phosphate group/phosphate ion
ec: https://purl.uniprot.org/enzyme/3.1.26.4
references: KEGG:C00960

Amino-diol-tetrahedral intermediate
type: KeggIntermediate
ec: https://purl.uniprot.org/enzyme/3.4.23.-
references: KEGG:I00136

Peptide
type: KeggSubstrate
type: KeggProduct
compound type: peptide/protein
ec: https://purl.uniprot.org/enzyme/3.4.23.-
references: KEGG:C00012

Protein
type: KeggSubstrate
type: KeggProduct
compound type: peptide/protein
ec: https://purl.uniprot.org/enzyme/3.4.23.-
references: KEGG:C00017

DNA(n)
type: KeggSubstrate
type: KeggProduct
label: DNA(n+1)
compound type: nucleic acids
ec: https://purl.uniprot.org/enzyme/2.7.7.49
references: KEGG:C00039

RNA-dependent DNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.49

RNA-instructed DNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.49

RT
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.49

calf thymus ribonuclease H
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.26.4

endoribonuclease H (calf thymus)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.26.4

RNase H
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.26.4

RNA*DNA hybrid ribonucleotidohydrolase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.26.4

hybrid ribonuclease
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.26.4

hybridase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.26.4

hybridase (ribonuclease H)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.26.4

ribonuclease H
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.26.4

hybrid nuclease
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.1.26.4

dUTP diphosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.23

deoxyuridine-triphosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.23

dUTPase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.23

dUTP pyrophosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.23

desoxyuridine 5'-triphosphate nucleotidohydrolase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.23

desoxyuridine 5'-triphosphatase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/3.6.1.23

Analogue
compound: Peptide
ligand het code: ACE-ALN-VAL-LEU-ALA-GLU-ALN-NH2 (chain I, J)
pdb: 3fivA

Analogue
compound: dUTP
ligand het code: UDP
pdb: 1f7pA

Analogue
compound: dUTP
ligand het code: UDP
pdb: 1f7pC

Analogue
compound: dUTP
ligand het code: UDP
pdb: 1f7rA

Analogue
compound: Peptide
ligand het code: INT
pdb: 1b11A

Analogue
compound: Peptide
ligand het code: INT
pdb: 5fivA

Analogue
compound: Peptide
ligand het code: INT
pdb: 6fivA

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: ACE-ALN-VAL-STA-GLU-ALN
pdb: 1fivA

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: ACE-ALN-VAL-STA-GLU-ALN-NH2
pdb: 2fivA

TransitionStateAnalogue
compound: Amino-diol-tetrahedral intermediate
ligand het code: LP1
pdb: 4fivA

ReferenceForCatalyticMechanism
reference index: 2
reference section: Fig.1

ReferenceForCatalyticMechanism
reference index: 4
reference section: Fig.8, p.10705-10707