ID C7LI56_BRUMC Unreviewed; 324 AA.
AC C7LI56;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Quinone oxidoreductase {ECO:0000313|EMBL:ACU49694.1};
GN Name=qor {ECO:0000313|EMBL:ACU49694.1};
GN OrderedLocusNames=BMI_II565 {ECO:0000313|EMBL:ACU49694.1};
OS Brucella microti (strain CCM 4915).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=568815 {ECO:0000313|EMBL:ACU49694.1, ECO:0000313|Proteomes:UP000002188};
RN [1] {ECO:0000313|EMBL:ACU49694.1, ECO:0000313|Proteomes:UP000002188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 4915 {ECO:0000313|EMBL:ACU49694.1,
RC ECO:0000313|Proteomes:UP000002188};
RX PubMed=19653890; DOI=10.1186/1471-2164-10-352;
RA Audic S., Lescot M., Claverie J.-M., Scholz H.C.;
RT "Brucella microti: the genome sequence of an emerging pathogen.";
RL BMC Genomics 10:352-352(2009).
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DR EMBL; CP001579; ACU49694.1; -; Genomic_DNA.
DR RefSeq; WP_004689000.1; NC_013118.1.
DR AlphaFoldDB; C7LI56; -.
DR GeneID; 45053607; -.
DR KEGG; bmr:BMI_II565; -.
DR HOGENOM; CLU_026673_3_1_5; -.
DR PhylomeDB; C7LI56; -.
DR Proteomes; UP000002188; Chromosome 2.
DR GO; GO:0003960; F:NADPH:quinone reductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
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.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 11..322
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 324 AA; 34977 MW; D2C685226A24538E CRC64;
MINAIRVHRT GGPDVLHYEQ VEIGEPGPGE ARVRHEAVGL NFIDVYFRTG LYKAAKMPFT
PGNEGAGIVV AVGAGVENVR VGERVAYAAT PGSYADERIL PADRLVKVPD TIDLKTAASM
MLKGMTAQYL LRRTFRVEPG QTILFHAAAG GVGLIAGQWA KHLGATVIGT AGSEEKIALA
RKHGYDHVIN YRSENFVERV RELTNGEGVD VVYDSVGRDT YMGSLDVLKP LGMFACFGQS
SGVIPPFDLG ILAQKGSLFA TRPTLFNYIA RRADLEKTTA ELFDVVESGA VKIEINQTYA
LKDACKAHEA LEARKTTGTS ILLP
//
