ID MERA_PSEFL STANDARD; PRT; 548 AA. AC Q51772; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE MERCURIC REDUCTASE (EC 1.16.1.1) (HG(II) REDUCTASE). GN MERA. OS Pseudomonas fluorescens. OG Plasmid pMER327. OC Bacteria; Proteobacteria; gamma subdivision; Pseudomonas group; OC Pseudomonas. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 94341572. RA HOBMAN J., KHOLODII G., NIKIFOROV V., RITCHIE D.A., STRIKE P., RA YURIEVA O.; RT "The sequence of the mer operon of pMER327/419 and transposon ends of RT pMER327/419, 330 and 05."; RL Gene 146:73-78(1994). CC -!- FUNCTION: RESISTANCE TO HG(2+) IN BACTERIA APPEARS TO BE GOVERNED CC BY A SPECIALIZED SYSTEM WHICH INCLUDES MERCURIC REDUCTASE. MERA CC PROTEIN IS RESPONSIBLE FOR VOLATILIZING MERCURY AS HG(0). CC -!- CATALYTIC ACTIVITY: HG + NADP(+) + H(+) = HG(2+) + NADPH. CC -!- COFACTOR: FAD. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- MISCELLANEOUS: THE ACTIVE SITE IS A REDOX-ACTIVE DISULFIDE BOND. CC -!- SIMILARITY: BELONGS TO THE PYRIDINE NUCLEOTIDE-DISULFIDE CC OXIDOREDUCTASES CLASS-I. CC -!- SIMILARITY: CONTAINS A COPY OF THE HEAVY-METAL-ASSOCIATED CC (HMA) DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; X73112; CAA51542.1; -. DR HSSP; P04129; 1AFI. DR PFAM; PF00070; pyr_redox; 1. DR PFAM; PF00403; HMA; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. DR PROSITE; PS01047; HMA; 1. KW Mercuric resistance; Oxidoreductase; Flavoprotein; FAD; NADP; KW Mercury; Redox-active center; Metal-binding; Plasmid. FT DOMAIN 6 35 HMA. FT NP_BIND 87 117 FAD (ADP PART) (PROBABLE). FT DISULFID 123 128 REDOX-ACTIVE. FT NP_BIND 380 390 FAD (FLAVIN PART) (BY SIMILARITY). FT METAL 545 545 HG(2+) (POTENTIAL). FT METAL 546 546 HG(2+) (POTENTIAL). SQ SEQUENCE 548 AA; 57566 MW; 5C2FB18A CRC32; MTEITVNGMT CTSCATHVKD ALEKIPGVNA AVVSYPESRA QVMADTAVSH NQLLAAIAAL GYQGSIRVGD FKDEPKIRDA LEGAGLHIAI IGSGGAAMAA ALKAVEQGAT VTLIERGTIG GTCVNIGCVP SKIMIRAAHI AHLRRESPFD GGIAATVPAI DRSKLLAQQQ ARVDELRHAK YEGILDGNPA ITVLHGEARF KDDQSLVVRL NEGGEREVTF DRCLVATGAS PAVPPIPGLK ESPYWTSTEA LVSDTIPARL AVIGSSVVAL ELAQAFARLG SQVTILARST LFFREDPAIG EAVTAAFRAE GIEVLEHTQA SQVAHVNGEF VLTTGHGELR ADKLLVATGR APNTRSLALD APGVTVNAQG AIVIDQGMRT SNPNIYAAGD CTDQPQFVYV AAAAGTRAAI NMTGGDRALN LTAMPAVVFT DPQVATVGYS EAEAHHDGIE TDSRTLTLDN VPRALANFDT RGFIKLVIEE GSGRLIGVQA VAPEAGELIQ TAVLAIRNRM TVQELADQLF PYLTMVEGLK LAAQTFNKDV KQLSCCAG //