ID Q5ZTR0_LEGPH Unreviewed; 711 AA.
AC Q5ZTR0;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Mercuric reductase {ECO:0000313|EMBL:AAU28167.1};
DE EC=1.16.1.1 {ECO:0000313|EMBL:AAU28167.1};
GN Name=merA1 {ECO:0000313|EMBL:AAU28167.1};
GN OrderedLocusNames=lpg2101 {ECO:0000313|EMBL:AAU28167.1};
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624 {ECO:0000313|EMBL:AAU28167.1, ECO:0000313|Proteomes:UP000000609};
RN [1] {ECO:0000313|EMBL:AAU28167.1, ECO:0000313|Proteomes:UP000000609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513
RC {ECO:0000313|Proteomes:UP000000609};
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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; AE017354; AAU28167.1; -; Genomic_DNA.
DR RefSeq; WP_010947814.1; NC_002942.5.
DR RefSeq; YP_096114.1; NC_002942.5.
DR AlphaFoldDB; Q5ZTR0; -.
DR STRING; 272624.lpg2101; -.
DR PaxDb; 272624-lpg2101; -.
DR GeneID; 66491236; -.
DR KEGG; lpn:lpg2101; -.
DR PATRIC; fig|272624.6.peg.2200; -.
DR eggNOG; COG0398; Bacteria.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_0_6; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000000609; 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:UP000000609};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..187
FT /note="VTT"
FT /evidence="ECO:0000259|Pfam:PF09335"
FT DOMAIN 245..560
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 580..684
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 711 AA; 77559 MW; F5909567B6DA8878 CRC64;
MKISAIKTWL PLLIIIVLLG LFLGLGLNKY VSFASLRDNH EWLIAITKSH FYLVSFVFII
IYTVAVALSI PGAIFLTLIG GFLFGILWGT FLVVLSATLG ATILFFAVQS SLGEVFSKRA
SGWVKRMRSG FKDNAFSYLL TLRLIPLFPF WVINIVSAVL GVSASTFIIA TFIGIIPGSI
VYVSVGNGLG ELFAASLQPN LGIIFEPKFI LPLLGLAALS LIPVFYKKKG KQGTEKMKDK
DLFCDLAIIG GGSAGLSIAA GCSQLGLQVV LVEPNKMGGD CLNYGCIPSK TLLNTAKIFY
QTKHSTVLGI QAKSVKIDFL QVMQQVHNVI ACIAKNDSVE RFTSLGVQVI QEAGHFIGPK
QFKLKRKIIR AKHFVIATGS SPAIPPIQNL NKVSYLTNET IFNLKVQPEH LIVIGGGPIG
CELAQAFAML GSKVTILEAF TILPKDDADC VAIIRSQLES MQIALYEQIK INKIEESADK
TISVHLENQD NPITITGSHL LVSTGRVANV DGLGLEKAGV QYTTRGINTN ARLQTTNKKI
YAIGDVTGPY QFTHMASYQA GIALRNIAFK WPAKVDYKAV PWVTYTEPEL AHVGLLASEA
LKDPTLKITE FAFAEVDRAQ AENKVNGKIK IITGKKAKIL GVSIVGAHAG ELILPWVIAV
KERKSLRTFT DAIAAYPTFS EISKRVAGEY YKPFIFSSKI RTFVRWLNKL G
//
