ID C8PDF2_9LACO Unreviewed; 448 AA.
AC C8PDF2;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:EEW51392.1};
DE EC=1.6.99.3 {ECO:0000313|EMBL:EEW51392.1};
GN Name=noxE {ECO:0000313|EMBL:EEW51392.1};
GN ORFNames=HMPREF0520_1122 {ECO:0000313|EMBL:EEW51392.1};
OS Lactobacillus iners DSM 13335.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=525328 {ECO:0000313|EMBL:EEW51392.1, ECO:0000313|Proteomes:UP000004115};
RN [1] {ECO:0000313|EMBL:EEW51392.1, ECO:0000313|Proteomes:UP000004115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13335 {ECO:0000313|EMBL:EEW51392.1,
RC ECO:0000313|Proteomes:UP000004115};
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 (SEP-2009) to the EMBL/GenBank/DDBJ databases.
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:EEW51392.1}.
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DR EMBL; ACLN01000019; EEW51392.1; -; Genomic_DNA.
DR RefSeq; WP_006729147.1; NZ_GG700804.1.
DR AlphaFoldDB; C8PDF2; -.
DR GeneID; 69784903; -.
DR PATRIC; fig|525328.13.peg.95; -.
DR HOGENOM; CLU_003291_1_0_9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000004115; 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; 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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Oxidation {ECO:0000256|ARBA:ARBA00023097};
KW Oxidoreductase {ECO:0000313|EMBL:EEW51392.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004115}.
FT DOMAIN 2..307
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 334..431
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 448 AA; 49274 MW; 6725B3C1A2364FD5 CRC64;
MKFVIVGTNH AGIAAANTLL DNYGKNNEVI MIDRNNNLSY LGCGTALWVG RQISSYKKLF
YTKPADFEAK GARISLETTV NKIDFENKIV YATIKNHTEI TETYDKLILA EGSAPIAPDL
PGKDLAGIHF LKLFQEGMAV DQELDKSDVK TVAVVGAGYI GVEIAEAARR RGKQVLLFDA
AKTCLSSYYD PEFSTLMDQN LRDHDIETHY GELAQEYLGK DGHVCALKTN KGKYQADIVI
NCIGFRPNAI LGGDHLKRFS NGAYLVNRNF QTSDPDVFAV GDCATNYSNA LQDTTYIALA
SNAVRSGIVG AHNAAGTVIE GAGVQGSNGI EIYDLKLVST GLSVKAADKF GLSVKYVDYE
DKQLPDFMPA SENAKVKIRI VYEKKTNRIV GAQLASLYDM HELIHMFSLA IQEGLTMDKL
QLLDIFFLPH YNQPYNYVTM AALKADKN
//
