ID A0A0A1H0X9_9LACO Unreviewed; 546 AA.
AC A0A0A1H0X9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Mercuric reductase {ECO:0000256|ARBA:ARBA00014791, ECO:0000256|PIRNR:PIRNR000350};
DE EC=1.16.1.1 {ECO:0000256|ARBA:ARBA00012661, ECO:0000256|PIRNR:PIRNR000350};
DE AltName: Full=Hg(II) reductase {ECO:0000256|ARBA:ARBA00031725, ECO:0000256|PIRNR:PIRNR000350};
GN Name=merA {ECO:0000256|RuleBase:RU361223,
GN ECO:0000313|EMBL:BAP86366.1};
GN ORFNames=LOOC260_118600 {ECO:0000313|EMBL:BAP86366.1};
OS Paucilactobacillus hokkaidonensis JCM 18461.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1291742 {ECO:0000313|EMBL:BAP86366.1, ECO:0000313|Proteomes:UP000031620};
RN [1] {ECO:0000313|EMBL:BAP86366.1, ECO:0000313|Proteomes:UP000031620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LOOC260 {ECO:0000313|EMBL:BAP86366.1,
RC ECO:0000313|Proteomes:UP000031620};
RA Tanizawa Y., Tohno M., Kaminuma E., Nakamura Y., Arita M.;
RT "Complete genome sequence and analysis of Lactobacillus hokkaidonensis
RT LOOC260T.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|PIRNR:PIRNR000350}.
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:0000256|ARBA:ARBA00000896,
CC ECO:0000256|PIRNR:PIRNR000350, ECO:0000256|RuleBase:RU361223};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRNR:PIRNR000350,
CC ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU361223};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRNR:PIRNR000350,
CC ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU361223};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|PIRNR:PIRNR000350, ECO:0000256|RuleBase:RU361223}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|PIRNR:PIRNR000350, ECO:0000256|RuleBase:RU361223}.
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DR EMBL; AP014680; BAP86366.1; -; Genomic_DNA.
DR RefSeq; WP_041094406.1; NZ_AP014680.1.
DR AlphaFoldDB; A0A0A1H0X9; -.
DR STRING; 1291742.LOOC260_118600; -.
DR KEGG; lho:LOOC260_118600; -.
DR HOGENOM; CLU_016755_1_1_9; -.
DR Proteomes; UP000031620; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016152; F:mercury (II) reductase activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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; 3.30.70.100; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; 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 NCBIfam; TIGR02053; MerA; 1.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
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 PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS50846; HMA_2; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000350};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000350};
KW Mercuric resistance {ECO:0000256|ARBA:ARBA00022466,
KW ECO:0000256|PIRNR:PIRNR000350};
KW Mercury {ECO:0000256|ARBA:ARBA00022914, ECO:0000256|PIRNR:PIRNR000350};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000350}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000350};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000350};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 2..66
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT BINDING 131
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 256..263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 346
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 387
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 122..127
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 546 AA; 58673 MW; 7D3AFE324E7255CF CRC64;
MNKFKVNIQG MTCAGCEKHV ESALEKIGAK NIESSFRRGE AVFELPNEIE VESAIKAIDE
ANYKAREIEE VSSLENVALS NEDNYDLLII GSGAAAFSSA IKAIEYGAKV GMIERGTVGG
TCVNIGCVPS KTLLRAGEIN HLSKDNPFIG LQTSAGEVDL ASLITQKDKL VSELRNQKYV
DLIDEYNFDL IKGEAKFVDA STVEVNGAKL SAKRFLIATG ASPSLPQISG LEEMDYLTST
TLLELKKIPK RLTVIGSGYI GMELGQLFHH LGSEITLMQR SERLLKEYDP EISESVEKAL
IEQGISLVKG ATFERVVQSG EIKKVYVTVN GSKEVIESDQ LLVATGRKPN TDSLNLSAAG
VETGKNNEIL INDFGQTSNE KIYAAGDVTL GPQFVYVAAY EGGIITDNAI GGLNKKIDLS
VVPAVTFTNP TVATVGLTEE QAKEKGYDVK TSVLPLDAVP RAIVNRETTG VFKLVADAET
LKVLGVHIVS ENAGDVIYAA SLAVKFNLTI EDLTETLAPY LTMAEGLKLA ALTFDKNVSK
LSCCAV
//
