ID M0GH27_9EURY Unreviewed; 289 AA.
AC M0GH27;
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=C458_02490 {ECO:0000313|EMBL:ELZ71510.1};
OS Haloferax sp. ATCC BAA-644.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1227462 {ECO:0000313|EMBL:ELZ71510.1, ECO:0000313|Proteomes:UP000011507};
RN [1] {ECO:0000313|Proteomes:UP000011507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-644 {ECO:0000313|Proteomes:UP000011507};
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:ELZ71510.1, ECO:0000313|Proteomes:UP000011507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-644 {ECO:0000313|EMBL:ELZ71510.1,
RC ECO:0000313|Proteomes:UP000011507};
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:ELZ71510.1}.
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DR EMBL; AOLF01000002; ELZ71510.1; -; Genomic_DNA.
DR RefSeq; WP_008572895.1; NZ_AOLF01000002.1.
DR AlphaFoldDB; M0GH27; -.
DR PATRIC; fig|1227462.4.peg.490; -.
DR Proteomes; UP000011507; 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
//