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Database: UniProt
Entry: B3Y1I7_ECO11
LinkDB: B3Y1I7_ECO11
Original site: B3Y1I7_ECO11 
ID   B3Y1I7_ECO11            Unreviewed;       327 AA.
AC   B3Y1I7;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Quinone oxidoreductase {ECO:0000313|EMBL:BAG66811.1};
GN   Name=qor {ECO:0000313|EMBL:BAG66811.1};
OS   Escherichia coli O111:H-.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=168927 {ECO:0000313|EMBL:BAG66811.1};
RN   [1] {ECO:0000313|EMBL:BAG66811.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B171-8 {ECO:0000313|EMBL:BAG66811.1};
RX   PubMed=18757547; DOI=10.1128/JB.00625-08;
RA   Ogura Y., Abe H., Katsura K., Kurokawa K., Asadulghani M., Iguchi A.,
RA   Ooka T., Nakayama K., Yamashita A., Hattori M., Tobe T., Hayashi T.;
RT   "Systematic identification and sequence analysis of the genomic islands of
RT   the enteropathogenic Escherichia coli strain B171-8 by the combined use of
RT   whole-genome PCR scanning and fosmid mapping.";
RL   J. Bacteriol. 190:6948-6960(2008).
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DR   EMBL; AB426062; BAG66811.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3Y1I7; -.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          11..325
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   327 AA;  35173 MW;  85BA63B4049F5016 CRC64;
     MATRIEFHKH GGPEVLQAVE FTPADPAENE IQVENKAIGI NFIDTYIRSG LYPPPSLPSG
     LGTEAAGIVS KVGSGVKHIK AGDRVVYAQS ALGAYSSVHN INADKAAILP AAISFEQAAA
     SFLKGLTVYY LLRKTYEIKP DEQFLFHAAA GGVGLIACQW AKALGAKLIG TVGTAQKAQS
     ALKAGAWQVI NYREEDLVER LKEITGGKKV RVVYDSVGRD TWERSLDCLQ RRGLMVSFGN
     SSGAVTGVNL GILNQKGSLY VTRPSLQGYI TTREELTEAS NELFSLIASG VIKVDVAEQQ
     KYPLKDAQRA HEILESRATQ GSSLLIP
//
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