ID A0A0F7JTS0_9DEIO Unreviewed; 264 AA.
AC A0A0F7JTS0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Carbon monoxide dehydrogenase {ECO:0000313|EMBL:AKH18053.1};
GN ORFNames=SY84_14670 {ECO:0000313|EMBL:AKH18053.1};
OS Deinococcus soli (ex Cha et al. 2016).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH18053.1, ECO:0000313|Proteomes:UP000034024};
RN [1] {ECO:0000313|EMBL:AKH18053.1, ECO:0000313|Proteomes:UP000034024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N5 {ECO:0000313|EMBL:AKH18053.1,
RC ECO:0000313|Proteomes:UP000034024};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Deinococcus soli/N5/whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011389; AKH18053.1; -; Genomic_DNA.
DR RefSeq; WP_046844620.1; NZ_CP011389.1.
DR AlphaFoldDB; A0A0F7JTS0; -.
DR KEGG; dch:SY84_14670; -.
DR PATRIC; fig|1309411.5.peg.2989; -.
DR OrthoDB; 9774454at2; -.
DR Proteomes; UP000034024; 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 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; 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:UP000034024}.
FT DOMAIN 1..171
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 264 AA; 28010 MW; 202FCD2469A3AEA3 CRC64;
MYPASFEYHK AESVDQALAA LAENPDLKVI AGGHSLLPAM KLRLAQPPAL LDIWGIQEMK
GITRDGDHWV VGAMTTHADV LRSDLPLFPE VAGWVGDPMV RNRGTIGGSL AHADPSADYP
AAALALGVEF VIRGPGGERT LHADDMFQGM FESAVQPGEL LTHIRIPATT QASAYEKFRH
PASHYAVVGV AVVRHADGSV RAAYTGAAEK AHRLTKLEDA VNASQSVPTG LVDAGDLLGD
RFASAEYRAH LVDVLAARAV GRLG
//
