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Database: UniProt
Entry: A4J873_DESRM
LinkDB: A4J873_DESRM
Original site: A4J873_DESRM 
ID   A4J873_DESRM            Unreviewed;       283 AA.
AC   A4J873;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Molybdopterin dehydrogenase, FAD-binding protein {ECO:0000313|EMBL:ABO51276.1};
GN   OrderedLocusNames=Dred_2772 {ECO:0000313|EMBL:ABO51276.1};
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO51276.1, ECO:0000313|Proteomes:UP000001556};
RN   [1] {ECO:0000313|EMBL:ABO51276.1, ECO:0000313|Proteomes:UP000001556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MI-1 {ECO:0000313|EMBL:ABO51276.1,
RC   ECO:0000313|Proteomes:UP000001556};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000612; ABO51276.1; -; Genomic_DNA.
DR   RefSeq; WP_011879071.1; NC_009253.1.
DR   AlphaFoldDB; A4J873; -.
DR   STRING; 349161.Dred_2772; -.
DR   KEGG; drm:Dred_2772; -.
DR   eggNOG; COG1319; Bacteria.
DR   HOGENOM; CLU_058050_0_1_9; -.
DR   OrthoDB; 9789842at2; -.
DR   Proteomes; UP000001556; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001556}.
FT   DOMAIN          1..171
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   283 AA;  30977 MW;  AD2FE64443DF2D6B CRC64;
     MEVITPVHLE EALGELYRDS SQSILAGGTD FLVKRKNGQI NPSRAINIYN LQELKFIRKE
     QGQLIIGPLM THQELVESSM VGQYAPLLAA ACSQVGSLQI RNRGTLGGNL VTASPAGDTM
     PALVVSNATL LLRSAHSERE VSIVDFINGP GKTVLQPGEL LTAIKIPCWE PEQIGFYRKL
     GQRKAMAISI VSVAFKARLV NQVLEDVRIA CGSVGPTVME LKRTAQNLTR YSLWGEELWT
     LVSDAGAETS PISDVRASQE YRRKMVGALL YEGLQDLSIN KRC
//
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