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Database: UniProt
Entry: D2RYX8_HALTV
LinkDB: D2RYX8_HALTV
Original site: D2RYX8_HALTV 
ID   D2RYX8_HALTV            Unreviewed;       413 AA.
AC   D2RYX8;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ADB61946.1};
GN   OrderedLocusNames=Htur_3081 {ECO:0000313|EMBL:ADB61946.1};
OS   Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS   13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena.
OX   NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB61946.1, ECO:0000313|Proteomes:UP000001903};
RN   [1] {ECO:0000313|EMBL:ADB61946.1, 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};
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).
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DR   EMBL; CP001860; ADB61946.1; -; Genomic_DNA.
DR   RefSeq; WP_012944207.1; NC_013743.1.
DR   AlphaFoldDB; D2RYX8; -.
DR   STRING; 543526.Htur_3081; -.
DR   GeneID; 8743701; -.
DR   KEGG; htu:Htur_3081; -.
DR   eggNOG; arCOG00570; Archaea.
DR   HOGENOM; CLU_664998_0_0_2; -.
DR   OrthoDB; 6062at2157; -.
DR   Proteomes; UP000001903; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   NCBIfam; NF041385; Dggglyphlred_Halo; 1.
DR   PANTHER; PTHR42685; GERANYLGERANYL DIPHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR42685:SF23; GERANYLGERANYL REDUCTASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          5..306
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   413 AA;  46171 MW;  BB0EA2FA48B50A2D CRC64;
     MNNRYDVVIA GAGPAGGQCA RDLVARGYDV VVLETESEDE FPRQSNKSTA GTFPSMMASF
     GIPDDVVMQY TDSVVLESPT DHYVQEQPGA VLEFADFKRF LVEDGRDGGA EYLFDARVTA
     PIMENGEIVG VRYNGDEEVY GDIVIDATGP SAPLAKKLDV VDLKRENHAI GIEYEFEGID
     IDRPGFADLN DAMMLRLDHE IAPGGYSWVF HTGEDTAKVG LCYLQNEHHS RYAKDGHTVD
     DYLEHWLETD PRFANAERLE GKQHRGSAHL QLPERMHTDR FMAIGDTVPT VDPLWGEGIN
     KCMQSGRVAA VAVDSCLKHG LEPTAENLEV YDTLWHRDVA PNQRKRLLMT QLLYLAPNER
     YDQFMADLHR LDEETLAAAN NGNILALAKL FDIDDAPLLA RFAKQHLKLD QFL
//
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