ID   L9XKC1_9EURY            Unreviewed;      1026 AA.
AC   L9XKC1;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=FAD-linked oxidase domain protein {ECO:0000313|EMBL:ELY62007.1};
GN   ORFNames=C492_08800 {ECO:0000313|EMBL:ELY62007.1};
OS   Natronococcus jeotgali DSM 18795.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronococcus.
OX   NCBI_TaxID=1227498 {ECO:0000313|EMBL:ELY62007.1, ECO:0000313|Proteomes:UP000011531};
RN   [1] {ECO:0000313|EMBL:ELY62007.1, ECO:0000313|Proteomes:UP000011531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18795 {ECO:0000313|EMBL:ELY62007.1,
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   -!- 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:ELY62007.1}.
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DR   EMBL; AOIA01000078; ELY62007.1; -; Genomic_DNA.
DR   RefSeq; WP_008422424.1; NZ_AOIA01000078.1.
DR   AlphaFoldDB; L9XKC1; -.
DR   STRING; 1227498.C492_08800; -.
DR   PATRIC; fig|1227498.3.peg.1728; -.
DR   OrthoDB; 2837at2157; -.
DR   Proteomes; UP000011531; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02754; CCG; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
FT   DOMAIN          65..297
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          658..691
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          996..1015
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1026 AA;  111217 MW;  D99FF9D7AFEEBDFA CRC64;
     MTASPDTALD DIDAEPATDE RADYDYVSDG VDRPDLVADL RDRIDGDVRF DTYTRQLYAT
     DASAYRETPI GVIFPTSTAD VASVVSYCAD REIPVLPRGG GTSLAGQAIN EAVVLDFTRY
     MDDVLSITPD DRRASVQSGV VLEELNDALA THGLKFAPDP AAGNRSVIGG AIGNNSTGAH
     SLIYGKTDAY VEECEAVLAD GTVATLGDVE VEELRERADP NGDLLERVSA EVVRIIDEDA
     DAVRERFPDL KRNVSGYNLD VLVEEAETGT VNLAHLLAGS EGTLAVITEA EVALEPVPET
     KAVSLLFYQS VLEAVTDVQH VLEHDPAAVE LIDDVLLGLA RNTAEFEDIA ALAPENAQAA
     LLVEFYAEDD DHGRKRTAGL LADRVPGSDS EAAPPTDRPE TDEVNAFEGL EAHAADERDQ
     FWKLRKAGLP ILLSRTSDEK HISFIEDCAI PPEHLPEFVE RFQSLLVEKN RDVDAAFYAH
     AGPGVLHVRP LVNTKAAADR EDMVEIADEV TDMVVEFGGS VSGEHGDGHA RTQWNRKLYG
     EELWKTFRDL KTAFDPNWLL NPGNVCGDHN MTENLRYDDE YSHDAGFDPA LNWENENGMQ
     GMVELCHGCG GCRGEQETTG GVMCPTYRAA DEEITATRGR ANLLRDAMSG NLPDDPTDDE
     FVEEVLDLCI GCKGCARDCP SEVDMAKLKT EVKHARHQEH GSSLRDKLFA NFDRLAPLGS
     ALAPLSNLAQ EFPGVGTITE KTVGIARERS LPEFHRETVK EWFEDRGGSQ IPESDATRKA
     VFFVDSYSNY SHPSVGKATV RVLEAAGVHV DVAKRTDSGR PALSKGFIDT ARETMRSNVA
     ELAPRVDDGW DVVLAEPSDA VMFQSDALDL LGGRAVESVA ANSYGICEYL DAFRLDANVD
     WNTPAESLAY HGHCHQKATK KDHHAVGVLR RAGYAVDPLD SGCCGMAGAF GYEAEHYSLS
     QSIGDILVDQ IDDSDATVVT APGTSCRTQL GDKRLEPVPA DSSLAGSALD DDEPPTPIEL
     LAYAVQ
//