ID A9I6Q1_BORPD Unreviewed; 318 AA.
AC A9I6Q1;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Quinone oxidoreductase {ECO:0000313|EMBL:CAP44329.1};
DE EC=1.6.5.5 {ECO:0000313|EMBL:CAP44329.1};
GN Name=qor4 {ECO:0000313|EMBL:CAP44329.1};
GN OrderedLocusNames=Bpet3983 {ECO:0000313|EMBL:CAP44329.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP44329.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP44329.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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DR EMBL; AM902716; CAP44329.1; -; Genomic_DNA.
DR AlphaFoldDB; A9I6Q1; -.
DR STRING; 94624.Bpet3983; -.
DR KEGG; bpt:Bpet3983; -.
DR eggNOG; COG0604; Bacteria.
DR Proteomes; UP000001225; 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:CAP44329.1}.
FT DOMAIN 11..316
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 318 AA; 32646 MW; 077E83B095BC0D58 CRC64;
MDQQVQLVAT GDVGNFIVVD CAPQAPGPGE IRLRHDGIGV NFIDIYHRMG LYPLPLPAVL
GVEGAGTVEA VGEGVSNVRV GERVAYAGIP GAYAATRLLP AWRAISLPDG IDTKVAAVSF
LRGMTAHMLL TRVYPAARGT IVLVHAAAGG LGATLTRWAH DLGCTVIGTA SSPEKASLAR
EHGADHVIVG RAADVAAEVA RLTDSRGVDF AVDGIGGDML RKTLASTRPL GVVASVGQAG
GPIPPVAVSE LRPMLVRPSI MAYAADQEAY AVAAQAVIAA IRQGIVRGAA HEYPLARAAQ
AHGDLESGKT TGSVMLAP
//
