M00146
type: Enzyme
cath: HIV Type 1 Reverse Transcriptase; Chain A, domain 1
cath: Alpha-Beta Plaits
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/1.-.-.-
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/3.-.-.-
cath: Nucleotidyltransferase; domain 5
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/-.-.-.-
cath: SH3 type barrels.
ec: https://purl.uniprot.org/enzyme/2.7.7.49
ec: https://purl.uniprot.org/enzyme/2.7.7.7
ec: https://purl.uniprot.org/enzyme/3.1.26.4
uniprot: P03354
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 enzyme: RNA-dependent DNA polymerase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.49
kegg enzyme: RNA-instructed DNA polymerase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.49
kegg pathway: Purine metabolism
kegg pathway: Pyrimidine metabolism
kegg cofactor: Manganese
kegg substrate: Deoxynucleoside triphosphate
kegg substrate: DNA(n)
kegg substrate: RNA
kegg substrate: H2O
kegg product: Pyrophosphate
kegg product: DNA(n)
kegg product: RNA 5'-phosphate
pdb: 1c0mA01
pdb: 1c0mB01
pdb: 1c0mC01
pdb: 1c0mD01
pdb: 1c1aA01
pdb: 1c1aB01
pdb: 1a5vA
pdb: 1a5wA
pdb: 1a5xA
pdb: 1asuA
pdb: 1asvA
pdb: 1aswA
pdb: 1cxqA
pdb: 1cxuA
pdb: 1cz9A
pdb: 1czbA
pdb: 1vsdA
pdb: 1vseA
pdb: 1vsfA
pdb: 1vshA
pdb: 1vsiA
pdb: 1vskA
pdb: 1vslA
pdb: 1vsmA
pdb: 1c0mA02
pdb: 1c0mB02
pdb: 1c0mC02
pdb: 1c0mD02
pdb: 1c1aA02
pdb: 1c1aB02
active site residues resources: Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity.
active site residues resources: Similarities in the HIV-1 and ASV integrase active sites upon metal cofactor binding.
references: Crystal structure of an active two-domain derivative of Rous sarcoma virus integrase.
references: High-resolution structure of the catalytic domain of avian sarcoma virus integrase.
references: The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations.
references: Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity.
references: Avian retrovirus U3 and U5 DNA inverted repeats. Role Of nonsymmetrical nucleotides in promoting full-site integration by purified virion and bacterial recombinant integrases.
references: Structure of the catalytic domain of avian sarcoma virus integrase with a bound HIV-1 integrase-targeted inhibitor.
references: Structural basis for inactivating mutations and pH-dependent activity of avian sarcoma virus integrase.
references: Atomic resolution structures of the core domain of avian sarcoma virus integrase and its D64N mutant.
references: Crystal structures of catalytic core domains of retroviral integrases and role of divalent cations in enzymatic activity.
references: Similarities in the HIV-1 and ASV integrase active sites upon metal cofactor binding.
references: Tautomers of styrylquinoline derivatives containing a methoxy substituent: computation of their population in aqueous solution and their interaction with RSV integrase catalytic core.
references: Role of DNA end distortion in catalysis by avian sarcoma virus integrase.
references: Nucleophile selection for the endonuclease activities of human, ovine, and avian retroviral integrases.
references: Presteady-state analysis of avian sarcoma virus integrase. I. A splicing activity and structure-function implications for cognate site recognition.
references: Presteady-state analysis of avian sarcoma virus integrase. II. Reverse-polarity substrates identify preferential processing of the U3-U5 pair.
references: An amino acid in the central catalytic domain of three retroviral integrases that affects target site selection in nonviral DNA.
references: Functional oligomeric state of avian sarcoma virus integrase.
comment: The tertiary structure of the N-terminal domains of this enzyme has not been determined yet. Only the catalytic domain of integrase has been solved so far. However, this enzyme seems to be homologous to the structures of its homologue, Pol polyprotein from Moloney murine leukemia virus (M00135 in EzCatDB), except for its N-terminal protease domain. This enzyme catalyzes two successive reactions, hydrolysis (called processing) and transfer (called joining) (see [3]). Although manganese is annotated as the cofactor, other divalent metal such as magnesium, cadmium and zinc can act as the cofactor (see [2] & [3]). However, in the presence of zinc ions, the polynucleotidyl transfer reaction can be inhibited, whilst the endonucleolytic reaction (hydrolysis) can be catalyzed (see [3]).

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

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

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

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

Purine metabolism
type: KeggPathway
references: KEGG:MAP00230
ec: https://purl.uniprot.org/enzyme/2.7.7.7

Pyrimidine metabolism
type: KeggPathway
references: KEGG:MAP00240
ec: https://purl.uniprot.org/enzyme/2.7.7.7

Manganese
type: KeggCofactor
references: KEGG:C00034
compound type: heavy metal
references: CHEBI:18291
references: CHEBI:35154
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Deoxynucleoside triphosphate
type: KeggSubstrate
references: KEGG:C00677
ec: https://purl.uniprot.org/enzyme/2.7.7.49
ec: https://purl.uniprot.org/enzyme/2.7.7.7
compound type: nucleotide

DNA(n)
type: KeggSubstrate
references: KEGG:C00039
ec: https://purl.uniprot.org/enzyme/2.7.7.49
ec: https://purl.uniprot.org/enzyme/2.7.7.7
compound type: nucleic acids
type: KeggProduct
label: DNA(n+1)

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

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

Pyrophosphate
type: KeggProduct
references: KEGG:C00013
ec: https://purl.uniprot.org/enzyme/2.7.7.49
ec: https://purl.uniprot.org/enzyme/2.7.7.7
compound type: phosphate group/phosphate ion
references: CHEBI:29888
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

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

1c0mA01
type: Pdb
references: 1c0m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c0m
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1c0mB01
type: Pdb
references: 1c0m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c0m
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1c0mC01
type: Pdb
references: 1c0m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c0m
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1c0mD01
type: Pdb
references: 1c0m
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c0m
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1c1aA01
type: Pdb
references: 1c1a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c1a
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1c1aB01
type: Pdb
references: 1c1a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c1a
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1a5vA
type: Pdb
references: 1a5v
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5v
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1a5wA
type: Pdb
references: 1a5w
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5w
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1a5xA
type: Pdb
references: 1a5x
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1a5x
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1asuA
type: Pdb
references: 1asu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1asu
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1asvA
type: Pdb
references: 1asv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1asv
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1aswA
type: Pdb
references: 1asw
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1asw
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1cxqA
type: Pdb
references: 1cxq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxq
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1cxuA
type: Pdb
references: 1cxu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cxu
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1cz9A
type: Pdb
references: 1cz9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1cz9
cofactor binding residue: ;ASP 121;GLU 157(Magnesium or Manganese binding)
comment: mutant D64N

1czbA
type: Pdb
references: 1czb
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1czb
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1vsdA
type: Pdb
references: 1vsd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vsd
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1vseA
type: Pdb
references: 1vse
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vse
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1vsfA
type: Pdb
references: 1vsf
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vsf
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1vshA
type: Pdb
references: 1vsh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vsh
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1vsiA
type: Pdb
references: 1vsi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vsi
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

1vskA
type: Pdb
references: 1vsk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vsk
cofactor binding residue: ;ASP 121;GLU 157(Magnesium or Manganese binding)
comment: mutant D64N

1vslA
type: Pdb
references: 1vsl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vsl
cofactor binding residue: ;ASP 121;GLU 157(Magnesium or Manganese binding)
comment: mutant D64N

1vsmA
type: Pdb
references: 1vsm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vsm
cofactor binding residue: ASP 64;ASP 121;GLU 157(Magnesium or Manganese binding)

Crystal structure of an active two-domain derivative of Rous sarcoma virus integrase.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10669607
journal: J Mol Biol
volume: 296
pages: 535-48
published year: 2000
authors:
  item: Yang ZN
  item: Mueser TC
  item: Bushman FD
  item: Hyde CC
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

High-resolution structure of the catalytic domain of avian sarcoma virus integrase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7563093
journal: J Mol Biol
volume: 253
pages: 333-46
published year: 1995
authors:
  item: Bujacz G
  item: Jaskolski M
  item: Alexandratos J
  item: Wlodawer A
  item: Merkel G
  item: Katz RA
  item: Skalka AM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8805516
journal: Structure
volume: 4
pages: 89-96
published year: 1996
authors:
  item: Bujacz G
  item: Jaskolski M
  item: Alexandratos J
  item: Wlodawer A
  item: Merkel G
  item: Katz RA
  item: Skalka AM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9218451
journal: J Biol Chem
volume: 272
pages: 18161-8
published year: 1997
authors:
  item: Bujacz G
  item: Alexandratos J
  item: Wlodawer A
  item: Merkel G
  item: Andrake M
  item: Katz RA
  item: Skalka AM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Avian retrovirus U3 and U5 DNA inverted repeats. Role Of nonsymmetrical nucleotides in promoting full-site integration by purified virion and bacterial recombinant integrases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9295344
journal: J Biol Chem
volume: 272
pages: 23938-45
published year: 1997
authors:
  item: Vora AC
  item: Chiu R
  item: McCord M
  item: Goodarzi G
  item: Stahl SJ
  item: Mueser TC
  item: Hyde CC
  item: Grandgenett DP

Structure of the catalytic domain of avian sarcoma virus integrase with a bound HIV-1 integrase-targeted inhibitor.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9560188
journal: Proc Natl Acad Sci U S A
volume: 95
pages: 4831-6
published year: 1998
authors:
  item: Lubkowski J
  item: Yang F
  item: Alexandratos J
  item: Wlodawer A
  item: Zhao H
  item: Burke TR Jr
  item: Neamati N
  item: Pommier Y
  item: Merkel G
  item: Skalka AM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structural basis for inactivating mutations and pH-dependent activity of avian sarcoma virus integrase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9830010
journal: J Biol Chem
volume: 273
pages: 32685-9
published year: 1998
authors:
  item: Lubkowski J
  item: Yang F
  item: Alexandratos J
  item: Merkel G
  item: Katz RA
  item: Gravuer K
  item: Skalka AM
  item: Wlodawer A
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Atomic resolution structures of the core domain of avian sarcoma virus integrase and its D64N mutant.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10521258
journal: Biochemistry
volume: 38
pages: 13512-22
published year: 1999
authors:
  item: Lubkowski J
  item: Dauter Z
  item: Yang F
  item: Alexandratos J
  item: Merkel G
  item: Skalka AM
  item: Wlodawer A
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structures of catalytic core domains of retroviral integrases and role of divalent cations in enzymatic activity.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10384241
journal: Adv Virus Res
volume: 52
pages: 335-50
published year: 1999
authors:
  item: Wlodawer A

Similarities in the HIV-1 and ASV integrase active sites upon metal cofactor binding.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10685051
journal: Biopolymers
volume: 53
pages: 308-15
published year: 2000
authors:
  item: Lins RD
  item: Straatsma TP
  item: Briggs JM

Tautomers of styrylquinoline derivatives containing a methoxy substituent: computation of their population in aqueous solution and their interaction with RSV integrase catalytic core.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10961674
journal: Acta Biochim Pol
volume: 47
pages: 11-22
published year: 2000
authors:
  item: Ouali M
  item: Laboulais C
  item: Leh H
  item: Gill D
  item: Xhuvani E
  item: Zouhiri F
  item: Desmaele D
  item: d'Angelo J
  item: Auclair C
  item: Mouscadet JF
  item: Le Bret M

Role of DNA end distortion in catalysis by avian sarcoma virus integrase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11441016
journal: J Biol Chem
volume: 276
pages: 34213-20
published year: 2001
authors:
  item: Katz RA
  item: DiCandeloro P
  item: Kukolj G
  item: Skalka AM

Nucleophile selection for the endonuclease activities of human, ovine, and avian retroviral integrases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11024025
journal: J Biol Chem
volume: 276
pages: 114-24
published year: 2001
authors:
  item: Skinner LM
  item: Sudol M
  item: Harper AL
  item: Katzman M

Presteady-state analysis of avian sarcoma virus integrase. I. A splicing activity and structure-function implications for cognate site recognition.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11821409
journal: J Biol Chem
volume: 277
pages: 12089-98
published year: 2002
authors:
  item: Bao KK
  item: Skalka AM
  item: Wong I

Presteady-state analysis of avian sarcoma virus integrase. II. Reverse-polarity substrates identify preferential processing of the U3-U5 pair.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11821408
journal: J Biol Chem
volume: 277
pages: 12099-108
published year: 2002
authors:
  item: Bao KK
  item: Skalka AM
  item: Wong I

An amino acid in the central catalytic domain of three retroviral integrases that affects target site selection in nonviral DNA.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12610159
journal: J Virol
volume: 77
pages: 3838-45
published year: 2003
authors:
  item: Harper AL
  item: Sudol M
  item: Katzman M

Functional oligomeric state of avian sarcoma virus integrase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12446721
journal: J Biol Chem
volume: 278
pages: 1323-7
published year: 2003
authors:
  item: Bao KK
  item: Wang H
  item: Miller JK
  item: Erie DA
  item: Skalka AM
  item: Wong I

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

DNA-directed DNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase I
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase II
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase III
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase alpha
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase beta
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase gamma
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA nucleotidyltransferase (DNA-directed)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA nucleotidyltransferase (DNA-directed)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxyribonucleate nucleotidyltransferase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxynucleate polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxyribonucleic acid duplicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxyribonucleic acid polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxyribonucleic duplicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxyribonucleic polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

deoxyribonucleic polymerase I
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA duplicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA nucleotidyltransferase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA replicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

DNA-dependent DNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

duplicase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

Klenow fragment
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

sequenase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

Taq DNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

Taq Pol I
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

Tca DNA polymerase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.7.7.7

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

Analogue
compound: Manganese
pdb: 1vsdA
ligand het code: _MG

Analogue
compound: Manganese
pdb: 1vshA
ligand het code: 2x_ZN

Analogue
compound: Manganese
pdb: 1vsiA
ligand het code: _CA

Analogue
compound: Manganese
pdb: 1vslA
ligand het code: _ZN

Analogue
compound: Pyrophosphate
pdb: 1cz9A
ligand het code: SO4

ReferenceForCatalyticMechanism
reference index: 1
reference section: p.339

ReferenceForCatalyticMechanism
reference index: 2
reference section: Fig.3

ReferenceForCatalyticMechanism
reference index: 3

ReferenceForCatalyticMechanism
reference index: 14
reference section: Fig.9, p.12097-12098
reference step: 3