TOP6A_METMA
ID TOP6A_METMA Reviewed; 369 AA.
AC Q8PUB7;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Type 2 DNA topoisomerase 6 subunit A {ECO:0000255|HAMAP-Rule:MF_00132};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00132};
DE AltName: Full=Type II DNA topoisomerase VI subunit A {ECO:0000255|HAMAP-Rule:MF_00132};
GN Name=top6A {ECO:0000255|HAMAP-Rule:MF_00132}; OrderedLocusNames=MM_2418;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) IN COMPLEX WITH TOP6B, AND SUBUNIT.
RX PubMed=17603498; DOI=10.1038/nsmb1264;
RA Corbett K.D., Benedetti P., Berger J.M.;
RT "Holoenzyme assembly and ATP-mediated conformational dynamics of
RT topoisomerase VI.";
RL Nat. Struct. Mol. Biol. 14:611-619(2007).
CC -!- FUNCTION: Relaxes both positive and negative superturns and exhibits a
CC strong decatenase activity. {ECO:0000255|HAMAP-Rule:MF_00132}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00132};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00132};
CC -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B chains.
CC {ECO:0000255|HAMAP-Rule:MF_00132, ECO:0000269|PubMed:17603498}.
CC -!- INTERACTION:
CC Q8PUB7; Q8PUB8: top6B; NbExp=2; IntAct=EBI-9026768, EBI-9026766;
CC -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000255|HAMAP-
CC Rule:MF_00132}.
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DR EMBL; AE008384; AAM32114.1; -; Genomic_DNA.
DR RefSeq; WP_011034342.1; NC_003901.1.
DR PDB; 2Q2E; X-ray; 4.00 A; A=1-369.
DR PDBsum; 2Q2E; -.
DR AlphaFoldDB; Q8PUB7; -.
DR SMR; Q8PUB7; -.
DR DIP; DIP-29414N; -.
DR IntAct; Q8PUB7; 1.
DR STRING; 192952.MM_2418; -.
DR PRIDE; Q8PUB7; -.
DR EnsemblBacteria; AAM32114; AAM32114; MM_2418.
DR GeneID; 24840017; -.
DR KEGG; mma:MM_2418; -.
DR PATRIC; fig|192952.21.peg.2766; -.
DR eggNOG; arCOG04143; Archaea.
DR HOGENOM; CLU_037229_1_0_2; -.
DR OMA; NWGEARF; -.
DR BRENDA; 5.6.2.2; 3270.
DR EvolutionaryTrace; Q8PUB7; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00132; Top6A; 1.
DR InterPro; IPR002815; Spo11/TopoVI_A.
DR InterPro; IPR013049; Spo11/TopoVI_A_N.
DR InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR InterPro; IPR004085; TopoVI_A.
DR InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10848; PTHR10848; 1.
DR Pfam; PF04406; TP6A_N; 1.
DR PRINTS; PR01550; TOP6AFAMILY.
DR PRINTS; PR01552; TPISMRASE6A.
DR SUPFAM; SSF56726; SSF56726; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA-binding; Isomerase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..369
FT /note="Type 2 DNA topoisomerase 6 subunit A"
FT /id="PRO_0000145450"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00132"
SQ SEQUENCE 369 AA; 42127 MW; CF7FA9AC6F4936CA CRC64;
MEGEKGSKTR KGDALAREKL LEIAEKIYNQ FEEEVVPSVS LPSRTKANLE YSDESDVWVY
GDRESERSAK TVKGAFQLLK TTYATDFLIN EHLARNRGST LRELYYISEG WDYAKFKEQG
ESDRLIEDLE ILTSLQREYF HMRPEEDGAT MFGPIEITEQ TKRGERNIHC QKDVGEGGYQ
IPFNVENIEF QKHDASMIIA IETGGMYARL MENGFDEAYN AILVHLKGQP ARSTRRIIKR
MNEELGIPVA VFTDGDPWSY RIYASVAYGA IKSAHLSEFM ATPAAKFLGL QPSDIVEYEL
STDKLTEQDV SALRSELSDP RFESDYWKEQ IQLQLDIGKK AEQQAFAGKG LDFVTEVYLP
NRLKEMGMI
