ID C4LHI7_CORK4 Unreviewed; 340 AA.
AC C4LHI7;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Quinone oxidoreductase {ECO:0000313|EMBL:ACR17292.1};
DE EC=1.6.5.5 {ECO:0000313|EMBL:ACR17292.1};
GN Name=qor {ECO:0000313|EMBL:ACR17292.1};
GN OrderedLocusNames=ckrop_0519 {ECO:0000313|EMBL:ACR17292.1};
OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS CCUG 35717).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR17292.1, ECO:0000313|Proteomes:UP000001473};
RN [1] {ECO:0000313|EMBL:ACR17292.1, ECO:0000313|Proteomes:UP000001473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC {ECO:0000313|Proteomes:UP000001473};
RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT revealed insights into the physiology of a lipophilic corynebacterium that
RT lacks mycolic acids.";
RL J. Biotechnol. 136:22-30(2008).
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DR EMBL; CP001620; ACR17292.1; -; Genomic_DNA.
DR AlphaFoldDB; C4LHI7; -.
DR STRING; 645127.ckrop_0519; -.
DR KEGG; ckp:ckrop_0519; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_026673_3_1_11; -.
DR Proteomes; UP000001473; Chromosome.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IEA:UniProtKB-EC.
DR CDD; cd05286; QOR2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR047618; QOR-like.
DR PANTHER; PTHR48106; QUINONE OXIDOREDUCTASE PIG3-RELATED; 1.
DR PANTHER; PTHR48106:SF13; QUINONE OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACR17292.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001473}.
FT DOMAIN 22..338
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 340 AA; 35709 MW; 88D06EFF809FCA27 CRC64;
MSSSQTVTIP NTMHAIRVSH TGGADVLEYK DDVPVPQPGP GEVLVKIDAA GVNYIDTYFR
EGIYPTDMPY TPGVEGVGRV VAKGEDNGDA SSSGELSVGD RVAFYNTNCS YADYAAVPAS
AAVAIEETID DPTAASLMTQ GITAHYLSDG CYSLGEGDTC VITAGSGGVG LLLTQMAKAR
GATVISITST EEKAQLSRDN GADYTINYDD YSPEKIRELT DGRGADVVYD GVGKTTFDTS
IHSLRPTGTM VLFGAASGPV PPIDPQLLNE AGSVFLTRPS IKDWTSRPGE LQSRVQAVVG
MVANGSVKFR IGGTFPLSEA RTAHEQLQAR KTTGSLVLIP
//
