ID A0A1D8T207_9NOCA Unreviewed; 301 AA.
AC A0A1D8T207;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Carbon monoxide dehydrogenase {ECO:0000313|EMBL:AOW91728.1};
GN ORFNames=BFN03_00910 {ECO:0000313|EMBL:AOW91728.1};
OS Rhodococcus sp. WMMA185.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=679318 {ECO:0000313|EMBL:AOW91728.1, ECO:0000313|Proteomes:UP000178767};
RN [1] {ECO:0000313|EMBL:AOW91728.1, ECO:0000313|Proteomes:UP000178767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMMA185 {ECO:0000313|EMBL:AOW91728.1,
RC ECO:0000313|Proteomes:UP000178767};
RA Bugni T.S., Adnani N., Braun D., Chevrette M., McDonald B., Rajski S.;
RT "Draft Genome of Rhodococcus sp. WMMA185.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP017014; AOW91728.1; -; Genomic_DNA.
DR RefSeq; WP_070377429.1; NZ_CP017014.1.
DR AlphaFoldDB; A0A1D8T207; -.
DR STRING; 679318.BFN03_00910; -.
DR KEGG; rhw:BFN03_00910; -.
DR OrthoDB; 9793944at2; -.
DR Proteomes; UP000178767; 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; 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:UP000178767}.
FT DOMAIN 2..179
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 301 AA; 32642 MW; A08480CA4B15FAAF CRC64;
MQVPGNFEYE RATRVEDAIS LLDRLGDEAR LVAGGHSLLP MMKLRLANPE YLIDINDLER
ELGYITTEPK KVRIGAMTRH RRLLESDELA AVFPLFRDAE KVIADPVVRN RGTIGGSLCQ
ADPAEDLTTV CEVIDATCVV QGPRGRREIP VSDFEVGPYE TALEHNEMLI EVVIPVRSHS
SSAYAKVERR TGDWAVTAAG SAVTVEGGEI ARAAVGLTAV DADPSGLASV ADYLVGRPPS
EETFEQAGRL ASQACAPVGD ARGTADYKRH LASELTIRTL RTAVDRVLRS EVGHEPSQEE
A
//
