ID P74250 PRELIMINARY; PRT; 169 AA. AC P74250; DT 01-FEB-1997 (TREMBLREL. 02, CREATED) DT 01-FEB-1997 (TREMBLREL. 02, LAST SEQUENCE UPDATE) DT 01-JAN-1998 (TREMBLREL. 05, LAST ANNOTATION UPDATE) DE GLUTATHIONE PEROXIDASE (EC 1.11.1.9). OS SYNECHOCYSTIS SP. OC EUBACTERIA; CYANOBACTERIA; CHROOCOCCALES; SYNECHOCYSTIS. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=PCC6803; RA TABATA S.; RL SUBMITTED (JUN-1996) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=PCC6803; RA KANEKO T., SATO S., KOTANI H., TANAKA A., ASAMIZU E., NAKAMURA Y., RA MIYAJIMA N., HIROSAWA M., SUGIURA M., SASAMOTO S., KIMURA T., RA HOSOUCHI T., MATSUNO A., MURAKI A., NAKAZAKI N., NARUO K., OKUMURA S., RA SHIMPO S., TAKEUCHI C., WADA T., WATANABE A., YAMADA M., YASUDA M., RA TABATA S.; RL DNA RES. 3:109-136(1996). CC -!- FUNCTION: PROTECTS CELLS AND ENZYMES FROM OXIDATIVE DAMAGE, BY CC CATALYSING THE REDUCTION OF HYDROGEN PEROXIDE, LIPID PEROXYDES AND CC ORGANIC HYDROPEROXYDE, BY GLUTATHIONE. CC -!- CATALYTIC ACTIVITY: 2 GLUTATHIONE + H(2)O(2) = OXIDIZED CC GLUTATHIONE + 2 H(2)O. CC -!- COFACTOR: SELENOCYSTEINE. THE ACTIVE-SITE SELENOCYSTEINE IS CC ENCODED BY THE OPAL CODON, UGA (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE GLUTATHIONE PEROXIDASE 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; D90913; G1653430; -. DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1. DR PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1. KW PEROXIDASE; OXIDOREDUCTASE; SELENIUM; SELENOCYSTEINE. FT BINDING 41 41 SELENIUM (BY SIMILARITY). SQ SEQUENCE 169 AA; 18452 MW; 03A20E1C CRC32; MTAQANNTIY GFSANALDGS PVALRDFEGK VLLIVNTASQ CGFTPQYQGL QALYNRFGDR GFTVLGFPCN QFGQQEPGGS GEIKNFCETR YGVTFPLFEK VEVNGPNAHP LFKFLTAASP GMAIPFLGGA EDIKWNFTKF LVDRQGKVVK RYGSIAKPDE IAADIEKLL //