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Database: UniProt
Entry: A8R8K9_9FIRM
LinkDB: A8R8K9_9FIRM
Original site: A8R8K9_9FIRM 
ID   A8R8K9_9FIRM            Unreviewed;       277 AA.
AC   A8R8K9;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=FAD binding domain in molybdopterin dehydrogenase {ECO:0000313|EMBL:EDP12093.1};
GN   ORFNames=EUBDOL_00339 {ECO:0000313|EMBL:EDP12093.1};
OS   Amedibacillus dolichus DSM 3991.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Amedibacillus.
OX   NCBI_TaxID=428127 {ECO:0000313|EMBL:EDP12093.1, ECO:0000313|Proteomes:UP000004090};
RN   [1] {ECO:0000313|EMBL:EDP12093.1, ECO:0000313|Proteomes:UP000004090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3991 {ECO:0000313|EMBL:EDP12093.1,
RC   ECO:0000313|Proteomes:UP000004090};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Eubacterium dolichum (DSM 3991).";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDP12093.1, ECO:0000313|Proteomes:UP000004090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3991 {ECO:0000313|EMBL:EDP12093.1,
RC   ECO:0000313|Proteomes:UP000004090};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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:EDP12093.1}.
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DR   EMBL; ABAW02000013; EDP12093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8R8K9; -.
DR   STRING; 428127.EUBDOL_00339; -.
DR   eggNOG; COG1319; Bacteria.
DR   HOGENOM; CLU_073026_0_0_9; -.
DR   Proteomes; UP000004090; 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   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; 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   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          20..183
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   277 AA;  31326 MW;  44DE36D04DC00272 CRC64;
     MAAALLLIQR KIEYKKGEIL MLRIQQYVKA QSLEEAYTLL TKNRNNQILG GMCWLKMEDR
     LIPCAIDLGD LGLDKIEESE DVFTIGAMTT LRTLETHASL NAWCDHIIRD SVKDIVGVQL
     RNLATLGGSL YSRFGFSDVL TAFLCLDCDV VLYHGGVIPL AKFVQMPYMR DIITHVIVHK
     NKERKAFACV RKSATDLSLL NISASTYEKG YVICVGARPY KAVRFEIEKL AVEEVCQVVS
     EQVELDDNMR ASKEYRRKLV GALCRRVLEQ LEGKVCK
//
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