ID A0A1Y0N7M9_9BURK Unreviewed; 743 AA.
AC A0A1Y0N7M9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Mercuric reductase {ECO:0000313|EMBL:ARV18694.1};
DE EC=1.16.1.1 {ECO:0000313|EMBL:ARV18694.1};
GN Name=merA {ECO:0000313|EMBL:ARV18694.1};
GN ORFNames=AEP_01750 {ECO:0000313|EMBL:ARV18694.1};
OS Curvibacter sp. AEP1-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Curvibacter.
OX NCBI_TaxID=1844971 {ECO:0000313|EMBL:ARV18694.1, ECO:0000313|Proteomes:UP000196261};
RN [1] {ECO:0000313|EMBL:ARV18694.1, ECO:0000313|Proteomes:UP000196261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AEP1-3 {ECO:0000313|EMBL:ARV18694.1,
RC ECO:0000313|Proteomes:UP000196261};
RA Foret S., Pietschke C., Fraune S.;
RT "Curvibacter sp. AEP1.3.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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; CP015698; ARV18694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0N7M9; -.
DR OrthoDB; 178496at2; -.
DR Proteomes; UP000196261; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR032816; VTT_dom.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF2; MERCURIC REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF09335; SNARE_assoc; 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 PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691};
KW Reference proteome {ECO:0000313|Proteomes:UP000196261};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 53..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..184
FT /note="VTT"
FT /evidence="ECO:0000259|Pfam:PF09335"
FT DOMAIN 241..587
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 609..717
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 743 AA; 80332 MW; 52A19A99354BF7F7 CRC64;
MKASKILVLA VAASAIAAFV VFDLGRFLSL EALRQSQDAL AAQYAANPWG LRAAYFALYV
LVASLSLPGA VILTLAGGGV FGLGWGLLLV SFASSLGATV SFLAARFVLR DMVQARFGAR
LADINQGVAR DGALYLFSLR LIPVVPFFVI NLAMGLTTMR TRTFYWVSQL GMLAGTAVYV
NAGTRLAELQ SLKDIASPQL LGAFVLLGVF PLVAKALMNF IQQRKVYARW NAVRPQTFDR
NLVVIGGGAG GLVSAYIAAA VKAKVTLVEA HKMGGDCLNY GCVPSKALIK SAKLAHQMQH
AERYGLYSTP RTSDRRQNLF SFKAVMQRIH DVIATIEPHD SVERYTGLGV EVLQGYAKII
NPWTVEIALN DGGKQTLTTR SIVIAAGARP FVPPLPGLDE VGYVTSDTLW DEFAKLDEVP
KRLVVLGGGP IGCEMAQSFA RLGSAVTQVE MASRVMARED LEVSELAAAS LRADGVDLLT
GHKALRVEKY PHSPEPVEGA STSSARTGGG VLIVEHAGVE KHIPFDQLLC AVGRTARLSG
YGLEELGIPT HKTVQTNEYL QTIYPNIFAA GDVAGPYQFT HTAAHQAWYA AVNALFGDFK
KFKADYSVIP WATFIDPEVA RLGLNEQDAK EQGIAYEVTK YGIDDLDRAI ADSEAHGFVK
VLTVPGKDKI LGVTIVGTHA GDLLAEYVLA MKHGLGLNKI LGTIHTYPTL AEANKYAAGE
WKRAHQPHKL LEWVRKFHDW KRG
//
