DB code: M00182

CATH domain -.-.-.- :
1.10.10.41 : Arc Repressor Mutant, subunit A
2.170.11.10 : DNA Topoisomerase I; domain 2
3.90.15.10 : Topoisomerase I; Chain A, domain 3
1.10.132.10 : Topoisomerase I; Chain A, domain 4 Catalytic domain
1.-.-.- :
E.C. 5.99.1.2
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.170.11.10 : DNA Topoisomerase I; domain 2 M00047
3.90.15.10 : Topoisomerase I; Chain A, domain 3 T00228 M00047
1.10.10.41 : Arc Repressor Mutant, subunit A M00047
1.10.132.10 : Topoisomerase I; Chain A, domain 4 M00047

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P04786 DNA topoisomerase 1
EC 5.99.1.2
DNA topoisomerase I
Maintenance of killer protein 1
NP_014637.1 (Protein)
NM_001183260.1 (DNA/RNA sequence)
PF14370 (Topo_C_assoc)
PF01028 (Topoisom_I)
PF02919 (Topoisom_I_N)
[Graphical View]

KEGG enzyme name
DNA topoisomerase
type I DNA topoisomerase
untwisting enzyme
relaxing enzyme
nicking-closing enzyme
swivelase
omega-protein
deoxyribonucleate topoisomerase
topoisomerase
type I DNA topoisomerase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P04786 TOP1_YEAST ATP-independent breakage of single-stranded DNA, followed by passage and rejoining. Monomer. Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumolyated forms found in both nucleoplasm and nucleoli (By similarity).

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00271 C00271
E.C.
Compound Single-stranded DNA Single-stranded DNA
Type nucleic acids nucleic acids
ChEBI
PubChem
1oisA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound
1oisA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P11387, P04786

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1oisA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1oisA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
p.2-4
[6]
Fig.1

References
[1]
Resource
Comments
Medline ID
PubMed ID 2852543
Journal Cell Biol Int Rep
Year 1988
Volume 12
Pages 927-30
Authors Holmstrom M
Title Homology at a possible catalytic site in DNA topoisomerase I.
Related PDB
Related UniProtKB
[2]
Resource
Comments ACTIVE SITE TYROSINE.
Medline ID 89340401
PubMed ID 2547758
Journal J Biol Chem
Year 1989
Volume 264
Pages 13373-6
Authors Eng WK, Pandit SD, Sternglanz R
Title Mapping of the active site tyrosine of eukaryotic DNA topoisomerase I.
Related PDB
Related UniProtKB P04786
[3]
Resource
Comments ACTIVE SITE TYROSINE.
Medline ID 89264463
PubMed ID 2542938
Journal Proc Natl Acad Sci U S A
Year 1989
Volume 86
Pages 3559-63
Authors Lynn RM, Bjornsti MA, Caron PR, Wang JC
Title Peptide sequencing and site-directed mutagenesis identify tyrosine-727 as the active site tyrosine of Saccharomyces cerevisiae DNA topoisomerase I.
Related PDB
Related UniProtKB P04786
[4]
Resource
Comments
Medline ID
PubMed ID 7772596
Journal Biochim Biophys Acta
Year 1995
Volume 1262
Pages 1-14
Authors Gupta M, Fujimori A, Pommier Y
Title Eukaryotic DNA topoisomerases I.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 141-363.
Medline ID 96363669
PubMed ID 8747458
Journal Structure
Year 1995
Volume 3
Pages 1315-22
Authors Lue N, Sharma A, Mondragon A, Wang JC
Title A 26 kDa yeast DNA topoisomerase I fragment: crystallographic structure and mechanistic implications.
Related PDB 1ois
Related UniProtKB P04786
[6]
Resource
Comments
Medline ID
PubMed ID 9428510
Journal Cell
Year 1997
Volume 91
Pages 873-4
Authors Burgin AB Jr
Title Can DNA topoisomerases be ribonucleases?
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10380229
Journal Pac Symp Biocomput
Year 1999
Volume
Pages 578-89
Authors Shaiu WL, Hu T, Hsieh TS
Title The hydrophilic, protease-sensitive terminal domains of eucaryotic DNA topoisomerases have essential intracellular functions.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11532027
Journal Genes Cells
Year 2001
Volume 6
Pages 677-87
Authors Pouliot JJ, Robertson CA, Nash HA
Title Pathways for repair of topoisomerase I covalent complexes in Saccharomyces cerevisiae.
Related PDB
Related UniProtKB

Comments
This enzyme must be composed of at least six domains. It must have a catalytic domain at the C-terminus.
Although the tertiary structure of catalytic domain for this enzyme has not been solved yet, comparison of its amino acid sequence with the topoisomerase I from human suggests that it must have a similar catalytic domain to that of the human counterpart enzyme (M00047 in EzCatDB). However, global domain compositions are slightly different from the counterpart enzyme.

Created Updated
2004-04-27 2009-02-26