ID   L9XHB3_9EURY            Unreviewed;       464 AA.
AC   L9XHB3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ELY60987.1};
GN   ORFNames=C492_09605 {ECO:0000313|EMBL:ELY60987.1};
OS   Natronococcus jeotgali DSM 18795.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronococcus.
OX   NCBI_TaxID=1227498 {ECO:0000313|EMBL:ELY60987.1, ECO:0000313|Proteomes:UP000011531};
RN   [1] {ECO:0000313|EMBL:ELY60987.1, ECO:0000313|Proteomes:UP000011531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18795 {ECO:0000313|EMBL:ELY60987.1,
RC   ECO:0000313|Proteomes:UP000011531};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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:ELY60987.1}.
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DR   EMBL; AOIA01000091; ELY60987.1; -; Genomic_DNA.
DR   RefSeq; WP_008422764.1; NZ_AOIA01000091.1.
DR   AlphaFoldDB; L9XHB3; -.
DR   STRING; 1227498.C492_09605; -.
DR   PATRIC; fig|1227498.3.peg.1855; -.
DR   OrthoDB; 213514at2157; -.
DR   Proteomes; UP000011531; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR012951; BBE.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF08031; BBE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
FT   DOMAIN          42..212
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   464 AA;  50504 MW;  64BB827893197526 CRC64;
     MAVTTTPTDD EADVLEEQLR GELLRPGDSG YDEARSVWNG MIDRHPAMIV QARGVSDAIA
     AVSFAREYEL LLSVRGAGHN IAGNAVCDDG LELDLSRMRS VRVDPAGKTA QVEPGATLAD
     VDHETQEFGL ATPLGINSTT GVAGLTLGGG FGWLTRKYGM TVDNLRSVDV VTADGELRHA
     SEGENADLFW GVRGGSGNFG VVTSFEFDLH EVGPEVLSGP IVYSGEDAPA VLRHVRDFNE
     DAPDESAVWT ILRAAPPLPF LPESVHGVGV VIVVAFYAGS LEKGEEVLAP IREFGDPIAD
     AVGPHRYAEF QQAFDPLLAE GARNYWKSHN FDELSDDAID TAIEYAEKLP SPLSEIFFGQ
     VGGAMARVPT DATAYPHRDA AYAMNVHTRW EDPAMDDRCI AWTREFYEDM RTHATGGVYV
     NFISELEGEE SLAYGENHDR LVEVKTRYDP TNLFRMNQNV EPAA
//