EzCatDB: M00182
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeM00182
CATH domainDomain 1-.-.-.-
Domain 21.10.10.41 : Arc Repressor Mutant, subunit A
Domain 32.170.11.10 : DNA Topoisomerase I; domain 2
Domain 43.90.15.10 : Topoisomerase I; Chain A, domain 3
Domain 51.10.132.10 : Topoisomerase I; Chain A, domain 4Catalytic domain
Domain 61.-.-.-
E.C.5.99.1.2

CATH domainRelated DB codes (homologues)
1.10.10.41 : Arc Repressor Mutant, subunit AM00047
1.10.132.10 : Topoisomerase I; Chain A, domain 4M00047
2.170.11.10 : DNA Topoisomerase I; domain 2M00047
3.90.15.10 : Topoisomerase I; Chain A, domain 3T00228,M00047

Enzyme Name
UniProtKBKEGG

P04786
Protein nameDNA topoisomerase 1DNA topoisomerase
type I DNA topoisomerase
untwisting enzyme
relaxing enzyme
nicking-closing enzyme
swivelase
omega-protein
deoxyribonucleate topoisomerase
topoisomerase
type I DNA topoisomerase
SynonymsEC 5.99.1.2
DNA topoisomerase I
Maintenance of killer protein 1
RefSeqNP_014637.1 (Protein)
NM_001183260.1 (DNA/RNA sequence)
PfamPF14370 (Topo_C_assoc)
PF01028 (Topoisom_I)
PF02919 (Topoisom_I_N)
[Graphical view]


UniProtKB:Accession NumberP04786
Entry nameTOP1_YEAST
ActivityATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
SubunitMonomer.
Subcellular locationNucleus, 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).
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00271C00271
CompoundSingle-stranded DNASingle-stranded DNA
Typenucleic acidsnucleic acids
ChEBI

PubChem

          
1oisA01UnboundUnbound
1oisA02UnboundUnbound

Active-site residues
resource
Swiss-prot;P11387, P04786
pdb
        
1oisA01
1oisA02

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]p.2-4
[6]Fig.1

references
[1]
PubMed ID2852543
JournalCell Biol Int Rep
Year1988
Volume12
Pages927-30
AuthorsHolmstrom M
TitleHomology at a possible catalytic site in DNA topoisomerase I.
[2]
CommentsACTIVE SITE TYROSINE.
Medline ID89340401
PubMed ID2547758
JournalJ Biol Chem
Year1989
Volume264
Pages13373-6
AuthorsEng WK, Pandit SD, Sternglanz R
TitleMapping of the active site tyrosine of eukaryotic DNA topoisomerase I.
Related UniProtKBP04786
[3]
CommentsACTIVE SITE TYROSINE.
Medline ID89264463
PubMed ID2542938
JournalProc Natl Acad Sci U S A
Year1989
Volume86
Pages3559-63
AuthorsLynn RM, Bjornsti MA, Caron PR, Wang JC
TitlePeptide sequencing and site-directed mutagenesis identify tyrosine-727 as the active site tyrosine of Saccharomyces cerevisiae DNA topoisomerase I.
Related UniProtKBP04786
[4]
PubMed ID7772596
JournalBiochim Biophys Acta
Year1995
Volume1262
Pages1-14
AuthorsGupta M, Fujimori A, Pommier Y
TitleEukaryotic DNA topoisomerases I.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 141-363.
Medline ID96363669
PubMed ID8747458
JournalStructure
Year1995
Volume3
Pages1315-22
AuthorsLue N, Sharma A, Mondragon A, Wang JC
TitleA 26 kDa yeast DNA topoisomerase I fragment: crystallographic structure and mechanistic implications.
Related PDB1ois
Related UniProtKBP04786
[6]
PubMed ID9428510
JournalCell
Year1997
Volume91
Pages873-4
AuthorsBurgin AB Jr
TitleCan DNA topoisomerases be ribonucleases?
[7]
PubMed ID10380229
JournalPac Symp Biocomput
Year1999
Volume
Pages578-89
AuthorsShaiu WL, Hu T, Hsieh TS
TitleThe hydrophilic, protease-sensitive terminal domains of eucaryotic DNA topoisomerases have essential intracellular functions.
[8]
PubMed ID11532027
JournalGenes Cells
Year2001
Volume6
Pages677-87
AuthorsPouliot JJ, Robertson CA, Nash HA
TitlePathways for repair of topoisomerase I covalent complexes in Saccharomyces cerevisiae.

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.

createdupdated
2004-04-272009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.