ID Q1LRH7_CUPMC Unreviewed; 266 AA.
AC Q1LRH7;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Carbon-monoxide dehydrogenase (Acceptor) {ECO:0000313|EMBL:ABF07249.1};
DE EC=1.2.99.2 {ECO:0000313|EMBL:ABF07249.1};
GN Name=coxM {ECO:0000313|EMBL:ABF07249.1};
GN OrderedLocusNames=Rmet_0363 {ECO:0000313|EMBL:ABF07249.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF07249.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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DR EMBL; CP000352; ABF07249.1; -; Genomic_DNA.
DR RefSeq; WP_011515241.1; NC_007973.1.
DR AlphaFoldDB; Q1LRH7; -.
DR STRING; 266264.Rmet_0363; -.
DR KEGG; rme:Rmet_0363; -.
DR eggNOG; COG1319; Bacteria.
DR HOGENOM; CLU_058050_3_0_4; -.
DR Proteomes; UP000002429; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Oxidoreductase {ECO:0000313|EMBL:ABF07249.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002429}.
FT DOMAIN 1..170
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 266 AA; 27655 MW; D38A4A3CA3178D86 CRC64;
MYAFQYERAA DANAAVAKLK ADGDAKFLAG GQSLLAAMKL RLASPSTLVD VSRIPGMNGI
RVEGDALVIG AATRHADVAA NADVMRRIPA LAALANGIGD RQVRAMGTIG GSLANDDPAA
DYPAAVLGLN ATVVTDRRSI AADDFFKGLY ETALEPDELI TAVRFPSPDQ AAYIKFRNPA
SRFALVGVMV ARTGKTVRVA VTGAADSVFR APALEQALAA SFTPAAARAV KMDPSGLNVD
LHASAEYRAH LIPVLAARAV EQALKG
//
