ID A0A1G3L3Y3_9SPIR Unreviewed; 449 AA.
AC A0A1G3L3Y3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:OHD12578.1};
GN ORFNames=A2Y41_02645 {ECO:0000313|EMBL:OHD12578.1};
OS Spirochaetes bacterium GWB1_36_13.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1802174 {ECO:0000313|EMBL:OHD12578.1, ECO:0000313|Proteomes:UP000177420};
RN [1] {ECO:0000313|EMBL:OHD12578.1, ECO:0000313|Proteomes:UP000177420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:OHD12578.1}.
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; MIAO01000050; OHD12578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3L3Y3; -.
DR STRING; 1802174.A2Y41_02645; -.
DR Proteomes; UP000177420; Unassembled WGS sequence.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 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; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 5..302
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 330..428
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 449 AA; 47622 MW; E6B8337A30AAAC47 CRC64;
MEKTDVLVIG GSAAGIVAAL TGKSNYPEKE FMVVRKEKQV VVPCGIPYIF GSLENSDKNL
IPDAGITGAG IKLKIGEAVS LDTEKKICQM EDGSEIQYEK IVLAMGSNPS IPSWLKGSSL
ENVFTIPKNK DYLDKALVKI KESKNVVVIG AGFIGVEMSD EINKMGKNVT LVEILPNILG
LAFDSDIALK AEELLKSRGV NLKTNIGVKE IVGNKKAEKV ILTNGEELAA DAVILSMGYT
PNTQLVKNSK IKINEKGCIS VDEYMRTDIP DVFAIGDCAE KRDFFTRKMS GIMLASTATS
EARIAGMNLY TLSAVKTFGG TIAIFSTALG DTGFGAAGLT EKTAKQEGFN VITGSFEGVD
KHPGTLTGTH KQMVKLIAAS ETGTILGGEV SGGASAGELI NIIGLMIQNK MTIGSILTAQ
IGTHPLLTAP PTAYPIIKAA EIIAKKMRE
//
