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Database: UniProt
Entry: E3C933_9LACO
LinkDB: E3C933_9LACO
Original site: E3C933_9LACO 
ID   E3C933_9LACO            Unreviewed;       444 AA.
AC   E3C933;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EFQ52755.1};
GN   ORFNames=HMPREF9265_1703 {ECO:0000313|EMBL:EFQ52755.1};
OS   Limosilactobacillus oris PB013-T2-3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=908339 {ECO:0000313|EMBL:EFQ52755.1, ECO:0000313|Proteomes:UP000003070};
RN   [1] {ECO:0000313|EMBL:EFQ52755.1, ECO:0000313|Proteomes:UP000003070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB013-T2-3 {ECO:0000313|EMBL:EFQ52755.1,
RC   ECO:0000313|Proteomes:UP000003070};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) 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:EFQ52755.1}.
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DR   EMBL; AEKL01000062; EFQ52755.1; -; Genomic_DNA.
DR   RefSeq; WP_003713636.1; NZ_AEKL01000062.1.
DR   AlphaFoldDB; E3C933; -.
DR   eggNOG; COG1249; Bacteria.
DR   OrthoDB; 9800167at2; -.
DR   Proteomes; UP000003070; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
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   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;
FT   DOMAIN          4..313
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   444 AA;  48140 MW;  0E1FC8167BF914FD CRC64;
     MKNYDYIILG TGPAGYKLVQ LLAKTGKSLL AVEGGLFGGT CPNVGCEPKI FLSGAVHTAL
     ASQQLVGRGI AQPAQVDWDQ LMTVKKARFD SWPAETKAIY EKMCDVAVGY GEFVDAHTIQ
     VNGHQYHGTH IIIATGHRPH RLDIPGKEYL HDSTDVLSLS HRPDHAVFIG GGYVAIELAT
     FLAAAGTKVD LLIRSERILR GFYGKYAQEM VDQLTARGLT FHFQTTASAV AKTGGRVTVT
     TNHGEQLTTD YVVDASGRVP NVEKLKLTAA GIKYSRRGID VDDHLQTSVA GVYAIGDITS
     QPVPKLTTVA ELEADYLYRQ LVRGGQEPLR YPTIGTAAFA FPEIAQAGVN PEEAVDDSRY
     QVVEHDLSFG SFYAGLNEQG AKLTVVYDRD QRLVGASEIG ATAADDINNL VPVIGLQPSS
     REWQRKVLPA YPALADKVFG LLKR
//
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