ID A9ITD9_BORPD Unreviewed; 329 AA.
AC A9ITD9;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Quinone oxidoreductase {ECO:0000313|EMBL:CAP43412.1};
DE EC=1.6.5.5 {ECO:0000313|EMBL:CAP43412.1};
GN Name=qor2 {ECO:0000313|EMBL:CAP43412.1};
GN OrderedLocusNames=Bpet3070 {ECO:0000313|EMBL:CAP43412.1};
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:CAP43412.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP43412.1, 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; CAP43412.1; -; Genomic_DNA.
DR AlphaFoldDB; A9ITD9; -.
DR STRING; 94624.Bpet3070; -.
DR KEGG; bpt:Bpet3070; -.
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:CAP43412.1}.
FT DOMAIN 15..326
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 329 AA; 35240 MW; 8BD9A24B6FA8D2DA CRC64;
MASNLVKAVR IEQHGGPEVL KIVDVEVPPP APNEVTIRQH VAGLNFIDIY YRTGLYPHPL
PHGLGFEAAG VVEAVGADVA HLKKGDRVAY GQSPIGAYAQ ARNVPAAQVV KLPKGVAFDE
AAALMLKGLT VQYLFRQTYR LQGHETILFH AAAGGVGLIA CQWAKALGVK LIGTVSSPEK
AELARANGAW QTIDYSRENV VERVLELTGG KKVPVVYDGV GKDTWETSLD CIEPRGLMVS
FGNASGPVSG VNLATLNQKG CLYVTRPSLG LHVNTQEKLN AAASEMFDLV LKKKIKVRID
QRYTLEQAGE AQTALAARKT TGATVLTLD
//
