ID MERA_PSEFL STANDARD; PRT; 548 AA. AC Q51772; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 21-FEB-2006, entry version 46. DE Mercuric reductase (EC 1.16.1.1) (Hg(II) reductase). GN Name=merA; OS Pseudomonas fluorescens. OG Plasmid pMER327. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=294; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=94341572; PubMed=8063107; DOI=10.1016/0378-1119(94)90835-4; 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: Binds 1 FAD per subunit (By similarity). CC -!- SUBUNIT: Homodimer (By similarity). CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. CC -!- SIMILARITY: Contains 1 HMA domain. 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; -; Genomic_DNA. DR HSSP; P04129; 1AFJ. DR SMR; Q51772; 86-548. DR InterPro; IPR001327; FAD_pyr_redox. DR InterPro; IPR006121; HeavyMe_transpt. DR InterPro; IPR000815; Hg_reductase. DR InterPro; IPR011796; MerA. DR InterPro; IPR001100; Pyr_redox. DR InterPro; IPR004099; Pyr_redox_dim. DR InterPro; IPR012999; Pyr_redox_I_AS. DR Pfam; PF00403; HMA; 1. DR Pfam; PF00070; Pyr_redox; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00945; HGRDTASE. DR PRINTS; PR00411; PNDRDTASEI. DR ProDom; PD000139; FAD_pyr_redox; 1. DR TIGRFAMs; TIGR02053; MerA; 1. DR PROSITE; PS01047; HMA_1; 1. DR PROSITE; PS50846; HMA_2; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. KW FAD; Flavoprotein; Mercuric resistance; Mercury; Metal-binding; NADP; KW Oxidoreductase; Plasmid; Redox-active center. FT CHAIN 1 548 Mercuric reductase. FT /FTId=PRO_0000067998. FT DOMAIN 1 66 HMA. FT NP_BIND 115 123 FAD (ADP part) (By similarity). FT METAL 545 545 Mercury (Potential). FT METAL 546 546 Mercury (Potential). FT DISULFID 123 128 Redox-active. SQ SEQUENCE 548 AA; 57567 MW; C3AC40203F9E86A7 CRC64; 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 //