ID R4WNZ0_9BURK Unreviewed; 453 AA.
AC R4WNZ0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Mercuric reductase putative {ECO:0000313|EMBL:BAN26363.1};
GN ORFNames=BRPE64_CCDS02800 {ECO:0000313|EMBL:BAN26363.1};
OS Caballeronia insecticola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=758793 {ECO:0000313|EMBL:BAN26363.1, ECO:0000313|Proteomes:UP000013966};
RN [1] {ECO:0000313|Proteomes:UP000013966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23833137; DOI=10.1128/genomeA.00441-13;
RA Shibata T.F., Maeda T., Nikoh N., Yamaguchi K., Oshima K., Hattori M.,
RA Nishiyama T., Hasebe M., Fukatsu T., Kikuchi Y., Shigenobu S.;
RT "Complete Genome Sequence of Burkholderia sp. Strain RPE64, Bacterial
RT Symbiont of the Bean Bug Riptortus pedestris.";
RL Genome Announc. 1:340-344(2013).
RN [2] {ECO:0000313|EMBL:BAN26363.1, ECO:0000313|Proteomes:UP000013966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RPE64 {ECO:0000313|EMBL:BAN26363.1};
RX PubMed=29863457; DOI=10.1099/ijsem.0.002848;
RA Takeshita K., Tamaki H., Ohbayashi T., Meng X.-Y., Sone T., Mitani Y.,
RA Peeters C., Kikuchi Y., Vandamme P.;
RT "Burkholderia insecticola sp. nov., a gut symbiotic bacterium of the bean
RT bug Riptortus pedestris.";
RL Int. J. Syst. Evol. Microbiol. 68:2370-2374(2018).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; AP013060; BAN26363.1; -; Genomic_DNA.
DR RefSeq; WP_016347073.1; NC_021288.1.
DR AlphaFoldDB; R4WNZ0; -.
DR STRING; 758793.BRPE64_CCDS02800; -.
DR KEGG; buo:BRPE64_CCDS02800; -.
DR PATRIC; fig|758793.3.peg.4602; -.
DR HOGENOM; CLU_016755_1_2_4; -.
DR OrthoDB; 178496at2; -.
DR Proteomes; UP000013966; Chromosome 3.
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; 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; IPR001100; Pyr_nuc-diS_OxRdtase.
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 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3}.
FT DOMAIN 8..313
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 335..440
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 433
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 106
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 172..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 260
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 307..310
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 44..49
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 453 AA; 48121 MW; 85E0753FFA4EE037 CRC64;
MSDVEHYEYV FLGGGKGGKT LAMELANAGR RVALIERGMI GGSCINVACI PTKTLIQQAR
VAHVSKTAKP DMAQVRRNVQ AVVEGMVDIN MKAFVDSGFE LLLGTGHFIG PRRIHVRMND
GSERQLEGEH VFINTGTTAA IPDVPGLRAA APLTHVEALQ LDVTPDHLIV IGGGYIGLEM
AQAFHRLGAP VTLIQEAPRV AMREDEDVTS LIEASLKEEG IDVRVGVKPV KVTGTSGQAV
KIELDNGDIV SGSHVLVATG RTPVTKTLGL DAAGVEVDAR GFIKVDERLA TTAQNTWAIG
EVAGTPMFTH ASFDDYRVLK SQLAGGSKTT TGRVIPYALF IEPELGRIGL NEAEAKAQGI
AVRVAKLPMA AIPRARTNGA TNGFMKILID AHSDRILGFT MLGTNAGDVV TAVQMAMLGN
LPYTAVRDAI ISHPLISEGL NILLAKVPPR KTD
//
