ID C2E3Y2_LACJH Unreviewed; 444 AA.
AC C2E3Y2;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EEJ60434.1};
GN ORFNames=HMPREF0528_0456 {ECO:0000313|EMBL:EEJ60434.1};
OS Lactobacillus johnsonii ATCC 33200.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=525330 {ECO:0000313|EMBL:EEJ60434.1, ECO:0000313|Proteomes:UP000003491};
RN [1] {ECO:0000313|EMBL:EEJ60434.1, ECO:0000313|Proteomes:UP000003491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33200 {ECO:0000313|EMBL:EEJ60434.1,
RC ECO:0000313|Proteomes:UP000003491};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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:EEJ60434.1}.
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DR EMBL; ACGR01000024; EEJ60434.1; -; Genomic_DNA.
DR RefSeq; WP_004896275.1; NZ_GG670121.1.
DR PATRIC; fig|525330.7.peg.350; -.
DR HOGENOM; CLU_016755_2_0_9; -.
DR Proteomes; UP000003491; 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..315
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 444 AA; 49463 MW; 9EC66C4B8E54C7A7 CRC64;
MKKYDYIILG TGPAAYKLVK LLDTQHKSIL TVESGLFGGT CPNVGCEPKI YLDGAAQTIL
SNWQFEKDGI ISQGGKLNWA QLMKDKKARF ASWPNETRKN ISKISDVISG SAHFVDRQTI
EVNRQYFQGN RIIIATGRRP HELSIPGAKF LHDSSDVLSL STLPEHTTFI GGGYVAIELA
TFLAAAGSQV TILVRGDRVL RHFYQKYSRE LVVRMKQRGI QFEFETEPTR ITQLSDKYVV
ELNQGGPIVT DYVVNASGRM PNIEKLDLSA AQINYSTRGI DVDLHLQTNV KNIYAIGDVT
SQDVPNLTPV AEFQAQYLFN SLEKGLTQTI NYPAMGTGVF AFPQLAQAGI NPDSVLEDGD
NFEIREYELS QSSLYAGQKE RGLLTVVYDK ANYIVGVSEI SMSAVNDINY FVPIIGLRIN
KNEWHRNVLP IYPALADKIE GILR
//