ID TOP1_ECOLI STANDARD; PRT; 865 AA. AC P06612; DT 01-JAN-1988 (REL. 06, CREATED) DT 01-FEB-1995 (REL. 31, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE DNA TOPOISOMERASE I (EC 5.99.1.2) (OMEGA-PROTEIN) (RELAXING ENZYME) DE (UNTWISTING ENZYME) (SWIVELASE). GN TOPA OR SUPX. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 87141163. RA TSE-DINH Y.-C., WANG J.C.; RL J. MOL. BIOL. 191:321-331(1986). RN [2] RP REVISIONS, SEQUENCE FROM N.A. RA LYNCH D.A., WANG J.C.; RL SUBMITTED (SEP-1991) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [3] RP SEQUENCE OF 698-865 FROM N.A. RX MEDLINE; 87194810. RA OSTROWSKI J., JAGURA-BURDZY G., KREDICH N.M.; RL J. BIOL. CHEM. 262:5999-6005(1987). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-590. RX MEDLINE; 94159070. RA LIMA C.D., WANG J.C., MONDRAGON A.; RL NATURE 367:138-146(1994). CC -!- FUNCTION: THE REACTION CATALYZED BY TOPOISOMERASES LEADS TO THE CC CONVERSION OF ONE TOPOLOGICAL ISOMER OF DNA TO ANOTHER. CC -!- CATALYTIC ACTIVITY: ATP-INDEPENDENT BREAKAGE OF SINGLE-STRANDED CC DNA, FOLLOWED BY PASSAGE AND REJOINING. CC -!- WHEN A TOPOISOMERASE TRANSIENTLY BREAKS A DNA BACKBONE BOND, IT CC SIMULTANEOUSLY FORMS A PROTEIN-DNA LINK, IN WHICH A TYROSYL OXYGEN CC IN THE ENZYME IS JOINED TO A DNA PHOSPHORUS AT ONE END OF THE CC ENZYME-SEVERED DNA STRAND. CC -!- SUBUNIT: MONOMER. CC -!- SIMILARITY: BELONGS TO PROKARYOTIC TYPE I/III TOPOISOMERASE CC FAMILY. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04475; G415338; -. DR EMBL; M15041; G145664; -. DR PIR; A25786; ISECTP. DR ECO2DBASE; I115.0; 6TH EDITION. DR ECOGENE; EG11013; TOPA. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK. KW ISOMERASE; TOPOISOMERASE; DNA-BINDING; ZINC-FINGER. FT ACT_SITE 319 319 DNA CLEAVAGE. FT ZN_FING 599 630 C4-TYPE (POTENTIAL). FT ZN_FING 662 689 C4-TYPE (POTENTIAL). FT ZN_FING 711 736 C4-TYPE (POTENTIAL). FT CONFLICT 787 787 P -> R (IN REF. 3). SQ SEQUENCE 865 AA; 97349 MW; 0333884D CRC32; MGKALVIVES PAKAKTINKY LGSDYVVKSS VGHIRDLPTS GSAAKKSADS TSTKTAKKPK KDERGALVNR MGVDPWHNWE AHYEVLPGKE KVVSELKQLA EKADHIYLAT DLDREGEAIA WHLREVIGGD DARYSRVVFN EITKNAIRQA FNKPGELNID RVNAQQARRF MDRVVGYMVS PLLWKKIARG LSAGRVQSVA VRLVVERERE IKAFVPEEFW EVDASTTTPS GEALALQVTH QNDKPFRPVN KEQTQAAVSL LEKARYSVLE REDKPTTSKP GAPFITSTLQ QAASTRLGFG VKKTMMMAQR LYEAGYITYM RTDSTNLSQD AVNMVRGYIS DNFGKKYLPE SPNQYASKEN SQEAHEAIRP SDVNVMAESL KDMEADAQKL YQLIWRQFVA CQMTPAKYDS TTLTVGAGDF RLKARGRILR FDGWTKVMPA LRKGDEDRIL PAVNKGDALT LVELTPAQHF TKPPARFSEA SLVKELEKRG IGRPSTYASI ISTIQDRGYV RVENRRFYAE KMGEIVTDRL EENFRELMNY DFTAQMENSL DQVANHEAEW KAVLDHFFSD FTQQLDKAEK DPEEGGMRPN QMVLTSIDCP TCGRKMGIRT ASTGVFLGCS GYALPPKERC KTTINLVPEN EVLNVLEGED AETNALRAKR RCPKCGTAMD SYLIDPKRKL HVCGNNPTCD GYEIEEGEFR IKGYDGPIVE CEKCGSEMHL KMGRFGKYMA CTNEECKNTR KILRNGEVAP PKEDPVPLPE LPCEKSDAYF VLRDGAAGVF LAANTFPKSR ETRAPLVEEL YRFRDRLPEK LRYLADAPQQ DPEGNKTMVR FSRKTKQQYV SSEKDGKATG WSAFYVDGKW VEGKK //