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Database: UniProt
Entry: D6Y277_THEBD
LinkDB: D6Y277_THEBD
Original site: D6Y277_THEBD 
ID   D6Y277_THEBD            Unreviewed;       320 AA.
AC   D6Y277;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=NAD(P)H quinone oxidoreductase, PIG3 family {ECO:0000313|EMBL:ADG86812.1};
GN   OrderedLocusNames=Tbis_0076 {ECO:0000313|EMBL:ADG86812.1};
OS   Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM
OS   10125 / KCTC 9307 / NBRC 14880 / R51).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Thermobispora.
OX   NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG86812.1, ECO:0000313|Proteomes:UP000006640};
RN   [1] {ECO:0000313|EMBL:ADG86812.1, ECO:0000313|Proteomes:UP000006640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 /
RC   NBRC 14880 / R51 {ECO:0000313|Proteomes:UP000006640};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Jando M., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Thermobispora bispora DSM 43833.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001874; ADG86812.1; -; Genomic_DNA.
DR   RefSeq; WP_013130345.1; NC_014165.1.
DR   AlphaFoldDB; D6Y277; -.
DR   STRING; 469371.Tbis_0076; -.
DR   KEGG; tbi:Tbis_0076; -.
DR   eggNOG; COG0604; Bacteria.
DR   HOGENOM; CLU_026673_3_4_11; -.
DR   OrthoDB; 9780520at2; -.
DR   Proteomes; UP000006640; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd05276; p53_inducible_oxidoreductase; 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; IPR014189; Quinone_OxRdtase_PIG3.
DR   NCBIfam; TIGR02824; quinone_pig3; 1.
DR   PANTHER; PTHR48106:SF8; QUINONE OXIDOREDUCTASE PIG3; 1.
DR   PANTHER; PTHR48106; QUINONE OXIDOREDUCTASE PIG3-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   Reference proteome {ECO:0000313|Proteomes:UP000006640}.
FT   DOMAIN          10..318
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   320 AA;  33606 MW;  59BEC66506740656 CRC64;
     MRAIVIPEHG GPEVLTWQEM PDPHPAPGEV VIEVAASAVN RADVLQRQGL YPPPPGASEI
     PGLECSGVIA EIGENVEGFS VGDRVCALLA GGGYAERVAV PYQQVMPIPD GVSLTEAAAF
     PEVACTVWSN VFMTAGLREG ETLLVHGGGS GIGTFAIQLA KARGARVLVT AGSAEKLQRC
     FELGADDGVN YRVEDFAERF AGQADVILDI IGAAYLPRNI AALATGGRLV VIGLQGGTRG
     ELNLGTLLAK RASVHASGLR ARPVAEKAVI CREVVEHVWP LIGAGRIRPV VHAEVPLQEA
     ARAHRMLEAS EHVGKILLVR
//
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