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Database: UniProt
Entry: L9W7F2_9EURY
LinkDB: L9W7F2_9EURY
Original site: L9W7F2_9EURY 
ID   L9W7F2_9EURY            Unreviewed;       288 AA.
AC   L9W7F2;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Molybdopterin dehydrogenase FAD-binding protein {ECO:0000313|EMBL:ELY44263.1};
GN   ORFNames=C495_10189 {ECO:0000313|EMBL:ELY44263.1};
OS   Natronorubrum sulfidifaciens JCM 14089.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronorubrum.
OX   NCBI_TaxID=1230460 {ECO:0000313|EMBL:ELY44263.1, ECO:0000313|Proteomes:UP000011661};
RN   [1] {ECO:0000313|EMBL:ELY44263.1, ECO:0000313|Proteomes:UP000011661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14089 {ECO:0000313|EMBL:ELY44263.1,
RC   ECO:0000313|Proteomes:UP000011661};
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   -!- 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:ELY44263.1}.
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DR   EMBL; AOHX01000039; ELY44263.1; -; Genomic_DNA.
DR   RefSeq; WP_008162532.1; NZ_AOHX01000039.1.
DR   AlphaFoldDB; L9W7F2; -.
DR   STRING; 1230460.C495_10189; -.
DR   PATRIC; fig|1230460.4.peg.2066; -.
DR   eggNOG; arCOG01926; Archaea.
DR   OrthoDB; 19205at2157; -.
DR   Proteomes; UP000011661; 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; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
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; IPR002346; Mopterin_DH_FAD-bd.
DR   PANTHER; PTHR42659; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR   PANTHER; PTHR42659:SF2; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000011661}.
FT   DOMAIN          1..176
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   288 AA;  30255 MW;  0CAA6BB957CFBF75 CRC64;
     MYANDFEYYH AESVAEAVDL LEEHEGAELL AGSHGLLPRM RTGEEAPPVL VDINAVDGLS
     SIEVTDGDLS VGALVTHAEL ADSDLVREHA PALADAAGEV GDIQVRNGGT IGGNLAHGDA
     RTDHPAAVLA LGSSLDVTGS DGDRSIDAAD LFTGHFETAV GEHELVTALR IPIEDGASST
     YHKHRNPLSG YPLIGVGAWA RIDGETIERV RVAATGNLSH PRRLSAVEAA LEGEALEPAS
     ITAAAEQTTA LDDDEFRPDV QASPAYCRHL LSVNTEHALR DVLDVDGE
//
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