ID   M0CUD1_9EURY            Unreviewed;      1046 AA.
AC   M0CUD1;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:ELZ25484.1};
GN   ORFNames=C475_10649 {ECO:0000313|EMBL:ELZ25484.1};
OS   Halosimplex carlsbadense 2-9-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halosimplex.
OX   NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ25484.1, ECO:0000313|Proteomes:UP000011626};
RN   [1] {ECO:0000313|EMBL:ELZ25484.1, ECO:0000313|Proteomes:UP000011626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ25484.1,
RC   ECO:0000313|Proteomes:UP000011626};
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:ELZ25484.1}.
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DR   EMBL; AOIU01000025; ELZ25484.1; -; Genomic_DNA.
DR   RefSeq; WP_006883803.1; NZ_AOIU01000025.1.
DR   AlphaFoldDB; M0CUD1; -.
DR   STRING; 797114.C475_10649; -.
DR   PATRIC; fig|797114.5.peg.2165; -.
DR   eggNOG; arCOG00337; Archaea.
DR   OrthoDB; 2837at2157; -.
DR   Proteomes; UP000011626; 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   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000011626}.
FT   DOMAIN          60..298
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          692..723
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1006..1046
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1022..1046
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1046 AA;  111954 MW;  2F7F50DA77A3640E CRC64;
     MGTSDRPESD PAGDPRAGYD YAADAVARPG LVADLDERVA GEVRFDDYSR QLYATDASIY
     EVTPVGVVYP ESTADVASVV SYCAERSIPV LPRGGGTSLA GQTVNEAVVL DFTRHMDGVL
     TVDADERLAR AEPGAILGEL NAELAAHDLK FAPDPAWGDK SALGGAIGNN STGAHSLQYG
     KTDAYVEECE VVLADGTVTR FGEVTLEELR ERADPDGDLE ARIYAELAGV VDEEIDAVEA
     AFPELKRNVS GYNLDAFVAE AREALDGERE TVNVARLLAG SEGTLAIVTE ATVSLEPVPE
     TKGLALLTYE SLLDALEDVQ PILDHDPAAV EVLDDVLLDL AADTEEFGEL VDSVLPDGTG
     SVLLVEFYAE TDDEGRQRVA DLIADRVGDT AAAEQLGDAL VGAATTETAP AEGAADVTDA
     PIRAFAAREA HEEADRARFW KLRKSGLPIL LSRTTDAKHG SFIEDTAVPP ANLPEFVADF
     QAVLDEHDTY ASFYAHAGPG CLHIRPLIDT KSVDGVAAME SIADAVTDLV VEYDGSVSGE
     HGDGRARTQW NRKLYGEEVW DLFRDIKATF DPDWLLNPGQ VVGVDAADVK AGEAPERART
     VDMTEDLRFD PDYAFDAGFE PDLNWDNDNG MQGMVELCHG CGGCRGGQDT TGGVMCPTYR
     AADEEVTATR GRANMLRQAM SGDLPEDPTD DEFVSEVMDL CIGCKGCAKD CPSEVDMAKL
     KAEVEHAHHE EHGTSLRERV FANVDRLSAL GSATAPVSNW LQKLPGSGLV AEKVLGIARE
     RALPTFERES FVDWFAGREA GVSEAEAERK ALVFPDTYTN YSHPEAGKAA VRVLEAAGVH
     VDVPDDVASS GRAAHSKGFL DTSRERAERN VDELAPRVAD GWDLVVVEPS DAVMFQHDYL
     DLLSGAAAET VAANAYGVCE YVDRFRLDGD IDFDAPAASL TYHGHCHQKA TKKDHHAVGV
     LRRAGYEVDA LDSGCCGMAG SFGYEAEHYS MSKAIGSILF DQVDDSPGDE VVAPGASCRS
     QLDDHEGSES PPHPVERLAD AVAPEE
//