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Database: UniProt
Entry: M0FT48_9EURY
LinkDB: M0FT48_9EURY
Original site: M0FT48_9EURY 
ID   M0FT48_9EURY            Unreviewed;       289 AA.
AC   M0FT48;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=C460_01060 {ECO:0000313|EMBL:ELZ61754.1};
OS   Haloferax sp. ATCC BAA-646.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=1227464 {ECO:0000313|EMBL:ELZ61754.1, ECO:0000313|Proteomes:UP000011677};
RN   [1] {ECO:0000313|Proteomes:UP000011677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-646 {ECO:0000313|Proteomes:UP000011677};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA   Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ELZ61754.1, ECO:0000313|Proteomes:UP000011677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-646 {ECO:0000313|EMBL:ELZ61754.1,
RC   ECO:0000313|Proteomes:UP000011677};
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:ELZ61754.1}.
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DR   EMBL; AOLD01000013; ELZ61754.1; -; Genomic_DNA.
DR   RefSeq; WP_008572895.1; NZ_AOLD01000013.1.
DR   AlphaFoldDB; M0FT48; -.
DR   PATRIC; fig|1227464.4.peg.194; -.
DR   Proteomes; UP000011677; 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;
FT   DOMAIN          2..177
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   289 AA;  30468 MW;  F315A7A2A3313BE1 CRC64;
     MTAFESVEYV EPETVSEAVE RLADAAETRV IAGGYSLVPL LKDGIETPDR LIDVSGLNEL
     RGITERGDGV AIGALVTHDE IATDATVAER ARALADATDS VGDFQARNRG TIAGNLVFAD
     PKYDAPAAFL ALGGRVVTRG PAGRRAIAAD DWFRGPGTTA LDADELVTGI EVPSVERSGY
     VRTSEYSGYA VVGAAAAFET EDGVVRSARV AVNGAKPYPI RLPNVERALV DEAVGRVVDG
     DVATEAATAA LDDVETASLL ANDAATEEYR RRLVRTYCRQ AIERAASEP
//
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