ID A0A0R1YMB6_9LACO Unreviewed; 234 AA.
AC A0A0R1YMB6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Mercury(II) reductase {ECO:0000313|EMBL:KRM43247.1};
GN ORFNames=FD40_GL000261 {ECO:0000313|EMBL:KRM43247.1}, LA20533_03170
GN {ECO:0000313|EMBL:APT18332.1};
OS Amylolactobacillus amylophilus DSM 20533 = JCM 1125.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Amylolactobacillus.
OX NCBI_TaxID=1423721 {ECO:0000313|EMBL:KRM43247.1, ECO:0000313|Proteomes:UP000051230};
RN [1] {ECO:0000313|EMBL:KRM43247.1, ECO:0000313|Proteomes:UP000051230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20533 {ECO:0000313|EMBL:KRM43247.1,
RC ECO:0000313|Proteomes:UP000051230};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
RN [2] {ECO:0000313|EMBL:APT18332.1, ECO:0000313|Proteomes:UP000185499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20533 {ECO:0000313|EMBL:APT18332.1,
RC ECO:0000313|Proteomes:UP000185499};
RA Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT "The whole genome sequencing and assembly of Lactobacillus amylophilus DSM
RT 20533T strain.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP018888; APT18332.1; -; Genomic_DNA.
DR EMBL; AYYS01000007; KRM43247.1; -; Genomic_DNA.
DR RefSeq; WP_056945920.1; NZ_AYYS01000007.1.
DR AlphaFoldDB; A0A0R1YMB6; -.
DR STRING; 1423721.LA20533_03170; -.
DR KEGG; lah:LA20533_03170; -.
DR PATRIC; fig|1423721.4.peg.262; -.
DR Proteomes; UP000051230; Unassembled WGS sequence.
DR Proteomes; UP000185499; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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 PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051230}.
FT DOMAIN 10..95
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 123..229
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 234 AA; 25266 MW; 8065AEDA8730FB3B CRC64;
MDSCATCVGA GLKQVRDVAD QVELTYEVGG VSEKLVVDGL LVATGRTPNT KELVLENTSL
NVGPRGSVPV NEKLETNVPG VWALGDLNGG PQFTYISLDD YRIVNNQLFG DQTRTLTNRP
IYPNTTFLHP AVATIGLSAK AAKEQNLAVD VVSVLTKTAP KYKVIGDPRG IFQAIVGKKT
KLILGATIYD EESYEIINLI SLAMNQQIPA TALRDQIYSH PTMAETFNDL FAGI
//
