ID C7R004_JONDD Unreviewed; 479 AA.
AC C7R004;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ACV09562.1};
GN OrderedLocusNames=Jden_1919 {ECO:0000313|EMBL:ACV09562.1};
OS Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP
OS 55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134) (Listeria
OS denitrificans).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC Jonesia.
OX NCBI_TaxID=471856 {ECO:0000313|EMBL:ACV09562.1, ECO:0000313|Proteomes:UP000000628};
RN [1] {ECO:0000313|EMBL:ACV09562.1, ECO:0000313|Proteomes:UP000000628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 /
RC NBRC 15587 / NCTC 10816 / Prevot 55134
RC {ECO:0000313|Proteomes:UP000000628};
RX PubMed=21304666; DOI=10.4056/sigs.41646;
RA Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., Glavina Del Rio T.,
RA Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Copeland A.,
RA Saunders E., Brettin T., Detter J.C., Bruce D., Goodwin L., Pati A.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Goker M.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Han C.;
RT "Complete genome sequence of Jonesia denitrificans type strain (Prevot
RT 55134).";
RL Stand. Genomic Sci. 1:262-269(2009).
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; CP001706; ACV09562.1; -; Genomic_DNA.
DR RefSeq; WP_015772190.1; NC_013174.1.
DR AlphaFoldDB; C7R004; -.
DR STRING; 471856.Jden_1919; -.
DR KEGG; jde:Jden_1919; -.
DR eggNOG; COG1252; Bacteria.
DR HOGENOM; CLU_021377_7_1_11; -.
DR OrthoDB; 9781621at2; -.
DR Proteomes; UP000000628; Chromosome.
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 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:UP000000628}.
FT DOMAIN 27..357
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 52263 MW; B13427AB4A338F4A CRC64;
MAQTTELTDN AAETKATTTP RPRKVPRIVV LGGGSVGLYS ARRLRQRLGK REAAIVVIDP
RPYMTYAPFL PEVAAGSISD RDVVAPHNRA LKGIDTLMGR VTQIRHNDRT VEVTPEIGEP
YEITYDHLIV GLGSVSRVLP IPGLAENAIG FKNVEEAVAV RNHVLDRIIV AASTWDKDLR
QRLLTFTFVG GGFAGCEAIA EIEDMAKSAI KQYPTIEPGD LRFVMIEGSN RILPELTEEM
AQYALEEMQK RGIEFHLSTF LSSCEDGHVV TSTGVEFDTD TIVWTAGVKA HPVIGESDLP
TDKMGRVTTN TKLQVIDAEG TVIPDAYAAG DCAAVPDVHG GINGFCVPNA QHAVRQAKLL
GDNLASVLRS GELKEYSHKN LGTVASLGLH KGVAILFGSI KLRGFFAWCA HRGYHLYAMP
TISRRLRITT GWVSVYLMRR ELVPLGPLHD PRAEFRAAAI PPKPKQEQAS SLPDEAKAH
//
