ID F4D026_PSEUX Unreviewed; 298 AA.
AC F4D026;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Carbon-monoxide dehydrogenase (Acceptor) {ECO:0000313|EMBL:AEA24859.1};
DE EC=1.2.99.2 {ECO:0000313|EMBL:AEA24859.1};
GN OrderedLocusNames=Psed_2656 {ECO:0000313|EMBL:AEA24859.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA24859.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA24859.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002593; AEA24859.1; -; Genomic_DNA.
DR RefSeq; WP_013674783.1; NC_015312.1.
DR AlphaFoldDB; F4D026; -.
DR STRING; 675635.Psed_2656; -.
DR KEGG; pdx:Psed_2656; -.
DR eggNOG; COG1319; Bacteria.
DR HOGENOM; CLU_058050_3_0_11; -.
DR OrthoDB; 9793944at2; -.
DR Proteomes; UP000007809; 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 Oxidoreductase {ECO:0000313|EMBL:AEA24859.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007809}.
FT DOMAIN 1..182
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 298 AA; 31450 MW; AD845772B7FFCC94 CRC64;
MQVPAFFEYQ RATSVEHVVT LLERFGPEAR IVAGGHSLIP MMKLRLAQPE LLVDVNDLHE
LAGITVDGSV DAGHLRIGAL TRHAELLASS VAGEHFPILH DAERVIADPV VRNRGTIGGS
VCQADPSEDL SGVFTALRAV AVIRGADGDR TVPMREFFHG PYETAVRPAE ILVELRVPLR
TGAGSAYVKV DRRAGDWAVA AAGAVVSLGP GGVVDEVGIG LTAVGDADFT AVEAEDLLRG
RVADEDAFAA AGAVAAEHCR PTADQRGPVD YKRHLAGELT VRALRDAVAR ARRGRSAG
//