ID A0A1Y0EI54_9RHOB Unreviewed; 450 AA.
AC A0A1Y0EI54;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Glutathione reductase {ECO:0000313|EMBL:ARU03283.1};
DE EC=1.8.1.7 {ECO:0000313|EMBL:ARU03283.1};
GN Name=gor {ECO:0000313|EMBL:ARU03283.1};
GN ORFNames=LOKVESSMR4R_03921 {ECO:0000313|EMBL:ARU03283.1};
OS Yoonia vestfoldensis.
OG Plasmid psmr4r-2 {ECO:0000313|Proteomes:UP000195273}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=245188 {ECO:0000313|EMBL:ARU03283.1, ECO:0000313|Proteomes:UP000195273};
RN [1] {ECO:0000313|EMBL:ARU03283.1, ECO:0000313|Proteomes:UP000195273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMR4r {ECO:0000313|EMBL:ARU03283.1,
RC ECO:0000313|Proteomes:UP000195273};
RC PLASMID=Plasmid psmr4r-2 {ECO:0000313|Proteomes:UP000195273};
RA Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA Clarke A.K.;
RT "Genome Sequence of Loktanella vestfoldensis Strain SMR4r Isolated from a
RT Culture of the Diatom Skeletonema marinoi.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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; CP021433; ARU03283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0EI54; -.
DR KEGG; lvs:LOKVESSMR4R_03921; -.
DR OrthoDB; 9776382at2; -.
DR Proteomes; UP000195273; Plasmid psmr4r-2.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
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};
KW Oxidoreductase {ECO:0000313|EMBL:ARU03283.1};
KW Plasmid {ECO:0000313|EMBL:ARU03283.1}.
FT DOMAIN 5..321
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 341..443
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 173..180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 304
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 42..47
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 450 AA; 47090 MW; 578D25A7B10CA8BA CRC64;
MSENYDLIVI GAGMAGVAAA NKCGAAGWRV AIVDALPYGG TCALRGCDPK KILRRGAEII
DSARLMQGKG IDPGDLSINW ADLMAHKRGF TDPVPDKMEK GLLGNGVETL HGAARFTGSN
TLEVDGTAYR SERFLVAAGA MPRPLSFTGA DLAIDSTDFL NLEALPKRVL FIGGGFVSFE
FAHIAARAGA NPIIVDRGAR PLRGFDPDLV EMLIERGTGI GVDLMRETEI VSVAETNGAF
TVEVKSGDQT WTVETDLVVH GAGRVAALAD LNLEAAGVDY SDKGIVVAPH LQSTTSSAVY
AAGDSADTDG MPLTPVAVIE GKVAASNMLK DAQAVPDYAG IPTAVFTVPE VARVGMLESE
AKDAGHDVDV RFTDTGGWYS NYRIGETSAA AKVLVDKSNG KILGAHLFGP EYGELINFFG
LAIKLGLTAK QLRSMTAAYP SVGSDLGSLL
//
