ID D7B2X4_NOCDD Unreviewed; 458 AA.
AC D7B2X4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ADH68664.1};
GN OrderedLocusNames=Ndas_3258 {ECO:0000313|EMBL:ADH68664.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH68664.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH68664.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; CP002040; ADH68664.1; -; Genomic_DNA.
DR RefSeq; WP_013154271.1; NC_014210.1.
DR AlphaFoldDB; D7B2X4; -.
DR STRING; 446468.Ndas_3258; -.
DR KEGG; nda:Ndas_3258; -.
DR eggNOG; COG1252; Bacteria.
DR HOGENOM; CLU_021377_7_1_11; -.
DR OrthoDB; 9781621at2; -.
DR Proteomes; UP000002219; Chromosome 1.
DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR Gene3D; 3.50.50.100; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR045024; NDH-2.
DR PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR PANTHER; PTHR43706:SF45; NADH DEHYDROGENASE-LIKE PROTEIN RV1812C; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002219}.
FT DOMAIN 5..328
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 458 AA; 49359 MW; 1A61768B5C8BA0EF CRC64;
MSRPRIVVVG AGFGGLHTLR HLERRIPAGA ADIALVAPHD YMLYSPLLPQ VASGLLTPQS
VAMSVHRLTR QTRFVPGHAV GVDPGDRVVV VRRPTGELAP VRYDRLVLAP GGVTRAFDIP
GLAEHAYGAK TLAEAVLLRD HVLAQLELAN DSRDPAEREE RCRFVVVGGG YTGVETAASL
MRLCQEAAKR YPDLRSVIRW HLVDIAPKVL PELGDRLGRK ALDLLRSIGV EVKLKVSVRE
VTDDKVVLTD GRALPCRTLI WTAGVSPSPL MATLDKPTQK GRLEVGADLR VPGLDDVFAV
GDAAAVPNLS HEDSDYCPPT AQYATRQAAT VADNVVSSVL GRPMKEFRHR DMGLVVDLSG
NDALARVMQL ELSGLPALGV TRGYHLMAVP SATARARILA NWGIRKATGG DTSRLGFADG
GRPSSFVANE SVDYLDAEGS RREGARLLEN LHARYGVH
//
