MERA_PSEAI
ID MERA_PSEAI Reviewed; 561 AA.
AC P00392;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Mercuric reductase;
DE EC=1.16.1.1;
DE AltName: Full=Hg(II) reductase;
GN Name=merA;
OS Pseudomonas aeruginosa.
OG Plasmid pVS1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn501;
RX PubMed=6311258; DOI=10.1021/bi00286a015;
RA Brown N.L., Ford S.J., Pridmore R.D., Fritzinger D.C.;
RT "Nucleotide sequence of a gene from the Pseudomonas transposon Tn501
RT encoding mercuric reductase.";
RL Biochemistry 22:4089-4095(1983).
RN [2]
RP PROTEIN SEQUENCE OF 2-12 AND 130-143, FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=6412751; DOI=10.1021/bi00286a014;
RA Fox B.S., Walsh C.T.;
RT "Mercuric reductase: homology to glutathione reductase and lipoamide
RT dehydrogenase. Iodoacetamide alkylation and sequence of the active site
RT peptide.";
RL Biochemistry 22:4082-4088(1983).
CC -!- FUNCTION: Resistance to Hg(2+) in bacteria appears to be governed by a
CC specialized system which includes mercuric reductase. MerA protein is
CC responsible for volatilizing mercury as Hg(0).
CC {ECO:0000269|PubMed:6412751}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + Hg + NADP(+) = Hg(2+) + NADPH; Xref=Rhea:RHEA:23856,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16170, ChEBI:CHEBI:16793,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.16.1.1;
CC Evidence={ECO:0000269|PubMed:6412751};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6412751}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; Z00027; CAA77323.1; -; Genomic_DNA.
DR PIR; A00406; RDPSHA.
DR RefSeq; WP_003156770.1; NZ_WXZW01000069.1.
DR PDB; 1ZK7; X-ray; 1.60 A; A=96-561.
DR PDB; 1ZX9; X-ray; 1.90 A; A=96-561.
DR PDB; 2KT2; NMR; -; A=1-69.
DR PDB; 2KT3; NMR; -; A=1-69.
DR PDB; 4K7Z; X-ray; 1.50 A; A=96-561.
DR PDB; 4K8D; X-ray; 1.86 A; A=96-561.
DR PDBsum; 1ZK7; -.
DR PDBsum; 1ZX9; -.
DR PDBsum; 2KT2; -.
DR PDBsum; 2KT3; -.
DR PDBsum; 4K7Z; -.
DR PDBsum; 4K8D; -.
DR AlphaFoldDB; P00392; -.
DR BMRB; P00392; -.
DR SMR; P00392; -.
DR PRIDE; P00392; -.
DR GeneID; 61089175; -.
DR KEGG; ag:CAA77323; -.
DR EvolutionaryTrace; P00392; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016152; F:mercury (II) reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0045340; F:mercury ion binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0050787; P:detoxification of mercury ion; IEA:InterPro.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR021179; Mercury_reductase_MerA.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
DR SUPFAM; SSF55424; SSF55424; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW Mercuric resistance; Mercury; Metal-binding; NADP; Oxidoreductase; Plasmid;
KW Redox-active center; Transposable element.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6412751"
FT CHAIN 2..561
FT /note="Mercuric reductase"
FT /id="PRO_0000067997"
FT DOMAIN 2..65
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 11
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 14
FT /ligand="a metal cation"
FT /ligand_id="ChEBI:CHEBI:25213"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 128..136
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 558
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT BINDING 559
FT /ligand="Hg(2+)"
FT /ligand_id="ChEBI:CHEBI:16793"
FT DISULFID 136..141
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:6412751"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2KT2"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:2KT2"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:2KT2"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:2KT2"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:2KT2"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:2KT2"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2KT2"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2KT2"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 141..158
FT /evidence="ECO:0007829|PDB:4K7Z"
FT TURN 161..165
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 175..193
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 204..215
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:4K7Z"
FT TURN 250..254
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:4K7Z"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 310..322
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 350..359
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:1ZX9"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:4K7Z"
FT TURN 403..406
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 411..425
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 443..451
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 454..459
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 475..479
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:4K7Z"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:4K7Z"
FT STRAND 497..505
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 508..520
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 525..529
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 540..547
FT /evidence="ECO:0007829|PDB:4K7Z"
FT TURN 548..550
FT /evidence="ECO:0007829|PDB:4K7Z"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:4K7Z"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:1ZK7"
SQ SEQUENCE 561 AA; 58728 MW; 858669A67A490065 CRC64;
MTHLKITGMT CDSCAAHVKE ALEKVPGVQS ALVSYPKGTA QLAIVPGTSP DALTAAVAGL
GYKATLADAP LADNRVGLLD KVRGWMAAAE KHSGNEPPVQ VAVIGSGGAA MAAALKAVEQ
GAQVTLIERG TIGGTCVNVG CVPSKIMIRA AHIAHLRRES PFDGGIAATV PTIDRSKLLA
QQQARVDELR HAKYEGILGG NPAITVVHGE ARFKDDQSLT VRLNEGGERV VMFDRCLVAT
GASPAVPPIP GLKESPYWTS TEALASDTIP ERLAVIGSSV VALELAQAFA RLGSKVTVLA
RNTLFFREDP AIGEAVTAAF RAEGIEVLEH TQASQVAHMD GEFVLTTTHG ELRADKLLVA
TGRTPNTRSL ALDAAGVTVN AQGAIVIDQG MRTSNPNIYA AGDCTDQPQF VYVAAAAGTR
AAINMTGGDA ALDLTAMPAV VFTDPQVATV GYSEAEAHHD GIETDSRTLT LDNVPRALAN
FDTRGFIKLV IEEGSHRLIG VQAVAPEAGE LIQTAALAIR NRMTVQELAD QLFPYLTMVE
GLKLAAQTFN KDVKQLSCCA G
