ID A0A166C2B5_9EURY Unreviewed; 484 AA.
AC A0A166C2B5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Glutathione amide reductase {ECO:0000313|EMBL:KZX14056.1};
DE EC=1.8.1.16 {ECO:0000313|EMBL:KZX14056.1};
GN Name=garB {ECO:0000313|EMBL:KZX14056.1};
GN ORFNames=MBORA_01340 {ECO:0000313|EMBL:KZX14056.1};
OS Methanobrevibacter oralis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=66851 {ECO:0000313|EMBL:KZX14056.1, ECO:0000313|Proteomes:UP000077428};
RN [1] {ECO:0000313|EMBL:KZX14056.1, ECO:0000313|Proteomes:UP000077428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7256 {ECO:0000313|EMBL:KZX14056.1,
RC ECO:0000313|Proteomes:UP000077428};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter oralis DSM 7256.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZX14056.1}.
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DR EMBL; LWMU01000033; KZX14056.1; -; Genomic_DNA.
DR RefSeq; WP_042694327.1; NZ_LWMU01000033.1.
DR AlphaFoldDB; A0A166C2B5; -.
DR STRING; 66851.MBORA_01340; -.
DR PATRIC; fig|66851.6.peg.175; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000077428; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 4.
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 Oxidoreductase {ECO:0000313|EMBL:KZX14056.1}.
FT DOMAIN 4..349
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 370..470
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 484 AA; 53798 MW; 72602A77D0AC8C3A CRC64;
MDKYDVIYIG SGNAAWQGAR FLVKEGLKVL IVEEGLYGGT CANRGCNSKA LLDAPYELKA
AIDNFEGVGK AGNFNVDWPA LMKFKQKRIA NMAKFLDGKF DEYNIDVANA KGVILDEHTV
QVEDKKYYTD KIVICTGLKA IMPNIKGKEY LHDSNDFLDI SELPKHTIII GGGFIAMEFA
SIIAEAGLEA DVIIRSDMAL RDFHQPYVQN IIKILEEKNI RFHFNENVKE VIKNDDRISD
SQVKVGNVEK GINIDEEFKD PEAKSENKAY EDGFTVVTES GVSLNGDYVI AAIGREANVE
DIGLENIALE YTKDGIPVNN HLQTKIPNIY AAGDVADTGL AKLVTVAIHH SKYLIDEILG
KAGEITYPVV PAVVYTIPRI ATVGVPVYKA LESDDYEVFR LQYGRAYSLE LKNDTTAEVT
VVVDNELNIV GAEIYAADAE NIVNMFTFII NKKVTLEELD YMIYAFPSSS SVCLYKLHNI
HYDL
//
