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Database: UniProt
Entry: A0A1C4J2H1_9ACTN
LinkDB: A0A1C4J2H1_9ACTN
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ID   A0A1C4J2H1_9ACTN        Unreviewed;       297 AA.
AC   A0A1C4J2H1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=CO or xanthine dehydrogenase, FAD-binding subunit {ECO:0000313|EMBL:SCD43349.1};
GN   ORFNames=GA0115251_10747 {ECO:0000313|EMBL:SCD43349.1};
OS   Streptomyces sp. TverLS-915.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839763 {ECO:0000313|EMBL:SCD43349.1, ECO:0000313|Proteomes:UP000198957};
RN   [1] {ECO:0000313|EMBL:SCD43349.1, ECO:0000313|Proteomes:UP000198957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TverLS-915 {ECO:0000313|EMBL:SCD43349.1,
RC   ECO:0000313|Proteomes:UP000198957};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMCE01000066; SCD43349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4J2H1; -.
DR   Proteomes; UP000198957; 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:SF1; BLR6160 PROTEIN; 1.
DR   PANTHER; PTHR42659; 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:UP000198957}.
FT   DOMAIN          1..169
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   297 AA;  31515 MW;  81BF54B8079B46C3 CRC64;
     MEFLRPASWE EALAAKAAHP AAVPLAGGTD VMVELNFDHR RPAHLIDLGR VAALSAWERD
     GDTVRLGASV PYTRIMTELS AELPGLARAA HTVASPQIRN RGGVGGNLGT ASPAGDAHPA
     LLASGADIEV ASVRGTRRVP VDDFYTGVKR NALAPDELIR AIHLPAARGP QQFSKVGTRN
     AMVIAVCAFG LALHPDRRTL RTGIGSAAPT PVRAKAAEEF LTSVLDEERC WETGRPPGEA
     ALRQFGQLAS GACNPIDDVR GSAAYRRHAV GVMARRTFTW AWQALGTEQR RNGASCA
//
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