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Database: UniProt
Entry: B2FKI4_STRMK
LinkDB: B2FKI4_STRMK
Original site: B2FKI4_STRMK 
ID   B2FKI4_STRMK            Unreviewed;       329 AA.
AC   B2FKI4;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:CAQ46580.1};
GN   OrderedLocusNames=Smlt3135 {ECO:0000313|EMBL:CAQ46580.1};
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ46580.1, ECO:0000313|Proteomes:UP000008840};
RN   [1] {ECO:0000313|EMBL:CAQ46580.1, ECO:0000313|Proteomes:UP000008840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a {ECO:0000313|EMBL:CAQ46580.1,
RC   ECO:0000313|Proteomes:UP000008840};
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
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DR   EMBL; AM743169; CAQ46580.1; -; Genomic_DNA.
DR   RefSeq; WP_012480750.1; NC_010943.1.
DR   AlphaFoldDB; B2FKI4; -.
DR   EnsemblBacteria; CAQ46580; CAQ46580; Smlt3135.
DR   KEGG; sml:Smlt3135; -.
DR   PATRIC; fig|522373.3.peg.2932; -.
DR   eggNOG; COG0604; Bacteria.
DR   HOGENOM; CLU_026673_3_1_6; -.
DR   Proteomes; UP000008840; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd08268; MDR2; 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   PANTHER; PTHR48106:SF5; PKS_ER DOMAIN-CONTAINING PROTEIN; 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:UP000008840}.
FT   DOMAIN          11..327
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   329 AA;  34509 MW;  355FCA7C8E87867B CRC64;
     MSQVVRIHEY GTADVLRIDD IDVPAPSADE VQIRVKAIGL NRAEVMFRNG AYLQEAQFPS
     RLGYEAAGVV EAIGSAVSGF AAGDAVSVIP PLDIARWGTY GELANVPAQL VVKHPQALGF
     ETAAAVWMQY VTAWGALLQQ AHLAAGDFVI ITAASSSVGL AAIQIANAVG ATPIAVTRGP
     GKRQALLDAG AAHVIATQEQ DLVAEVARIT SGAGARVVFD PIGGPQLVPL TEAMARGGIL
     LEYGALSSEP TPFPLFNVLG KSLTLKGYLY SEIVSDDAAL ARAKAFIVDG LDKGMLTPKI
     AKVFPFAQIQ EAHRYLESNE QIGKVVVTV
//
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