ID A0A0P1GPV9_9RHOB Unreviewed; 479 AA.
AC A0A0P1GPV9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Glutathione amide reductase {ECO:0000313|EMBL:CUH76156.1};
DE EC=1.8.1.16 {ECO:0000313|EMBL:CUH76156.1};
GN Name=garB {ECO:0000313|EMBL:CUH76156.1};
GN ORFNames=TRN7648_00809 {ECO:0000313|EMBL:CUH76156.1};
OS Tropicibacter naphthalenivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicibacter.
OX NCBI_TaxID=441103 {ECO:0000313|EMBL:CUH76156.1, ECO:0000313|Proteomes:UP000054935};
RN [1] {ECO:0000313|EMBL:CUH76156.1, ECO:0000313|Proteomes:UP000054935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7648 {ECO:0000313|EMBL:CUH76156.1,
RC ECO:0000313|Proteomes:UP000054935};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; CYSE01000001; CUH76156.1; -; Genomic_DNA.
DR RefSeq; WP_058246318.1; NZ_FWXX01000001.1.
DR AlphaFoldDB; A0A0P1GPV9; -.
DR STRING; 441103.TRN7648_00809; -.
DR OrthoDB; 9776382at2; -.
DR Proteomes; UP000054935; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; 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; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 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.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
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:UP000054935}.
FT DOMAIN 6..345
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 365..472
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 462
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 176..183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 289
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 330
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 479 AA; 51854 MW; DE06B3001D299CB6 CRC64;
MSDFDYDLFV IGGGSGGVRA ARVAAGEAGA KVALAEEDRY GGTCVIRGCV PKKLMVFASE
YSEMPGQARA YGWDMADGEF NWTTFRGKLD AELDRLEGVY RKLLAGSGVE TFDARAKLKD
AHTVELSTGE TKTAKHILIA TGGRPVRPDL PNAHLGMVSD DIFHLDELPK SVLIIGGGYI
ACEFACILHG LGVEVTQYYR GAQILRGFDE EARGLIAEAM KERGIKLHTG TDIVAMGTAS
HDDMTLPVEE SQYGHDETAE EAGPNGKPIR VKATNGEEQT FDAVFFATGR KPNSDDLGLE
ELGIKMARNG AIEVDDYSQT AVPSVYAIGD VTDRVNLTPV AIREGMAFVE TVFHGNPTKV
DHELIPSAIF TQPEMGTVGL SEEAAREQEP IEVYCASFRP MQTAFADQPD RVMMKLIVSQ
ETRKVLGCHI VAPGAGEMIQ LAGIAIKMGA TKEDFDRTVA VHPTMSEEIV TMRNPTRKS
//
