ID A0A0G3A7I8_9ACTN Unreviewed; 297 AA.
AC A0A0G3A7I8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Carbon monoxide dehydrogenase {ECO:0000313|EMBL:AKJ09888.1};
GN ORFNames=ABB07_07585 {ECO:0000313|EMBL:AKJ09888.1};
OS Streptomyces incarnatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ09888.1, ECO:0000313|Proteomes:UP000035366};
RN [1] {ECO:0000313|EMBL:AKJ09888.1, ECO:0000313|Proteomes:UP000035366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX PubMed=26159526;
RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA Tamura T.;
RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT the Nucleoside Antibiotic Sinefungin.";
RL Genome Announc. 3:e00715-e00715(2015).
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DR EMBL; CP011497; AKJ09888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3A7I8; -.
DR STRING; 665007.ABB07_07585; -.
DR PATRIC; fig|665007.5.peg.1658; -.
DR Proteomes; UP000035366; 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: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;
FT DOMAIN 1..170
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 297 AA; 31835 MW; 661C512EFC0009D6 CRC64;
MDFLRPASWD EALAAKAEHP TAVPIAGGTD VMVEINFDHR RPEYLLDLNR IGDLYEWEVG
EETVRLGASV PYTRIMEHLR AELPGLALAS HTVASPQIRN RGGVGGNLGT ASPAGDAHPA
LLAAGAEVEV ESAARGTRLI PVDAFYTGVK RNALQPDELI RAVHIKKADG PQQYSKVGTR
NAMVIAVCAF GLALHPGTRT VRTGIGSAAP TPVRAEAAEE FLNAALEEGG FWDNGKIIPP
SVAKQFAQLC SGACNPIDDV RGTASYRRHA VGVMARRTLT WTWESYRGNH RTTEGAA
//
