ID D2S020_HALTV Unreviewed; 646 AA.
AC D2S020;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=NADH:flavin oxidoreductase/NADH oxidase {ECO:0000313|EMBL:ADB62717.1};
GN OrderedLocusNames=Htur_3858 {ECO:0000313|EMBL:ADB62717.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OG Plasmid pHTUR01 {ECO:0000313|EMBL:ADB62717.1,
OG ECO:0000313|Proteomes:UP000001903}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB62717.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB62717.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RC PLASMID=pHTUR01 {ECO:0000313|EMBL:ADB62717.1,
RC ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP001861; ADB62717.1; -; Genomic_DNA.
DR RefSeq; WP_012944961.1; NC_013744.1.
DR AlphaFoldDB; D2S020; -.
DR GeneID; 8744486; -.
DR KEGG; htu:Htur_3858; -.
DR HOGENOM; CLU_012153_1_2_2; -.
DR OrthoDB; 24876at2157; -.
DR Proteomes; UP000001903; Plasmid pHTUR01.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 4: Predicted;
KW Plasmid {ECO:0000313|EMBL:ADB62717.1}.
FT DOMAIN 5..333
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 383..607
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 646 AA; 71090 MW; 8D586028690336BC CRC64;
MSELLFTPKS IGPVTVPNRT VFLAHETGFA EDGLPTERDA AYYEARARGG VGLIVGPSSM
LVHPSSSNPM YATGYDPEVI PRLEMIADAC HEHGTKVFAQ LQHTGGEDSG EYAMRETWAP
SAVPTQYGYE MPKRMEIEDI EEIKLGFAKT AEHVKRGGLD GVELKAGHDG ILRQFISPKY
NRREDKYGGS VENRVRLVNE VVEAIRDRVG DEFPIGVRLT LDEMEDGGYD YEYAVEVMRH
LNPDIDFVDS DIATISKLYI TDAPMHAPLG YTQEYYGGAR EILDVPIIAS GRINDLTKGN
DILEEGRADF VGMCRQLICD ADTVRKVRRG ADDEVTHCIA CNQNCLGGIH TNGHVGCIQT
PRSGRETNIP HIEDVDEAPS ERRILVVGGG PAGLSFAVTA ADLGHRVTLR EKEDTLGGQS
NIATEIDSRR EFGDAVRNLL NQLENRDVTV ERGVEVSPSD VDDERWDDVV VATGAREQSP
QFEGRNVHRS WDVLRGETVG ESVIVFDTNK HAAGVGLAEQ LAVDGHDVTL VTTSYHPGDR
LEGTNVPPFL ETLYEHDAEL IEHTTIIGFQ DGEAQLLNVY SEEMTTMTAD SLVVAARREA
RTGLADALRE RVDDPDSVHR IGDCVAPRLI DKAIFDGEML ARRVGE
//
