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	Unbound	Unbound
1oisA02	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
1oisA02

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.

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