TOP1_MYCGA
ID TOP1_MYCGA Reviewed; 719 AA.
AC Q9JN65;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952};
DE EC=5.6.2.1 {ECO:0000255|HAMAP-Rule:MF_00952};
DE AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952};
DE AltName: Full=Omega-protein;
DE AltName: Full=Relaxing enzyme;
DE AltName: Full=Swivelase;
DE AltName: Full=Untwisting enzyme;
GN Name=topA {ECO:0000255|HAMAP-Rule:MF_00952}; OrderedLocusNames=MYCGA6340;
GN ORFNames=MGA_0454;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5969Var.B;
RA Skamrov A.V., Feoktistova E.S., Gol'dman M.A., Bibilashvili R.S.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 706-719.
RC STRAIN=A5969Var.B;
RX PubMed=1718781; DOI=10.1016/0014-5793(91)81106-i;
RA Skamrov A.V., Bibilashvili R.S.;
RT "Mycoplasma gallisepticum strain S6 genome contains three regions
RT hybridizing with 16 S rRNA and two regions hybridizing with 23 S and 5 S
RT rRNA.";
RL FEBS Lett. 291:71-74(1991).
CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which
CC is introduced during the DNA replication and transcription, by
CC transiently cleaving and rejoining one strand of the DNA duplex.
CC Introduces a single-strand break via transesterification at a target
CC site in duplex DNA. The scissile phosphodiester is attacked by the
CC catalytic tyrosine of the enzyme, resulting in the formation of a DNA-
CC (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH
CC DNA strand. The free DNA strand then undergoes passage around the
CC unbroken strand, thus removing DNA supercoils. Finally, in the
CC religation step, the DNA 3'-OH attacks the covalent intermediate to
CC expel the active-site tyrosine and restore the DNA phosphodiester
CC backbone. {ECO:0000255|HAMAP-Rule:MF_00952}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00952};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00952};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00952};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00952}.
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00952}.
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DR EMBL; L35043; AAF36767.1; -; Genomic_DNA.
DR EMBL; AE015450; AAP56984.1; -; Genomic_DNA.
DR RefSeq; WP_011113893.1; NC_004829.2.
DR AlphaFoldDB; Q9JN65; -.
DR SMR; Q9JN65; -.
DR KEGG; mga:MGA_0454; -.
DR PATRIC; fig|233150.7.peg.711; -.
DR HOGENOM; CLU_002929_4_3_14; -.
DR OMA; PECKYTR; -.
DR OrthoDB; 223233at2; -.
DR Proteomes; UP000001418; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03363; TOPRIM_TopoIA_TopoI; 1.
DR Gene3D; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 2.70.20.10; -; 1.
DR HAMAP; MF_00952; Topoisom_1_prok; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR023406; Topo_IA_AS.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR013498; Topo_IA_Znf.
DR InterPro; IPR005733; TopoI_bac-type.
DR InterPro; IPR028612; Topoisom_1_IA.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034149; TOPRIM_TopoI.
DR PANTHER; PTHR42785; PTHR42785; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF01396; zf-C4_Topoisom; 2.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; SSF56712; 1.
DR TIGRFAMs; TIGR01051; topA_bact; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding; Isomerase; Magnesium; Metal-binding; Reference proteome;
KW Repeat; Topoisomerase; Zinc; Zinc-finger.
FT CHAIN 1..719
FT /note="DNA topoisomerase 1"
FT /id="PRO_0000145154"
FT DOMAIN 6..137
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT ZN_FING 620..646
FT /note="C4-type 1"
FT ZN_FING 667..699
FT /note="C4-type 2"
FT REGION 189..194
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT ACT_SITE 334
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT BINDING 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT BINDING 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 36
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 166
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 167
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 170
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 336
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 532
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT CONFLICT 68
FT /note="V -> T (in Ref. 1; AAF36767)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="F -> Y (in Ref. 1; AAF36767)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="A -> P (in Ref. 1; AAF36767)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="K -> E (in Ref. 1; AAF36767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 719 AA; 82773 MW; F9699B867C942796 CRC64;
MTNHSSKILV IESPNKVKTI KKYLTDDYEI VATVGHIRDL PKYTLGFNTE DFVPKWEIIQ
EKKPAKGVSA TKKAKTVKKA VKNKKEIIDE LVDKAKKADE IYLATDPDRE GEAISWHVYD
VLKEKGVNVN KCKRIIFNEI SEKAVKNAIA NPREIQKDWV SSQITRRRLD RLIGFKLSSL
MKSKINADSA GRVQSIALKF ITEREELINK FVPRFWWTLD VILKDGTELM LRKIDEKLKD
KLGFKELEEV SGIDFNTKED AELVKQHLSD KYRVYAIDTP KLKSSYPKEV YKTSTLQQDA
INKLKWRSMK ITSVAQELYE GVTIDDEQIA LISYPRTDST RLSPEYGKTV LDFVAKTYGK
DYVATQSQLN GETKANKKQK AKVQDAHEAI HPIDISITPD SVKNKISSDQ YSLYKLIWTR
TVAHYMAAAV YELVNIRFIN NNNKFYAVNN TLKFDGYKKI YTHYDDKDHL RKLDLNHFAI
DKEFEAKDVL LNEHQTKPPA RFTQATLIEA LETEGIGRPS TYSTILDIVL KRNYAELVNG
RYYKTTDLGQ KLAFELDKNF PTIINKEFTK NMETTLDEIA QGTVNDVSYL QAFWNDFSEV
LNEAKTNIVK KVEYIEGKNC PNCSSQLVRR EGRYGPFVGC SNFPKCKFIE KSEQKAKEIV
YEEGVKCELC HAKLIRRVAK KKGRNKDNTF LGCSNFPKCK YTKSLEPEKD ETIRDSTII
