OLED_STRMK
ID OLED_STRMK Reviewed; 330 AA.
AC B2FI29;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=2-alkyl-3-oxoalkanoate reductase {ECO:0000303|PubMed:21958090};
DE EC=1.1.1.412 {ECO:0000269|PubMed:21958090};
GN Name=oleD {ECO:0000303|PubMed:21958090};
GN OrderedLocusNames=Smlt0209 {ECO:0000312|EMBL:CAQ43817.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP SUBUNIT, AND SUBSTRATE SPECIFICITY.
RX PubMed=21958090; DOI=10.1021/bi201096w;
RA Bonnett S.A., Papireddy K., Higgins S., del Cardayre S., Reynolds K.A.;
RT "Functional characterization of an NADPH dependent 2-alkyl-3-ketoalkanoic
RT acid reductase involved in olefin biosynthesis in Stenotrophomonas
RT maltophilia.";
RL Biochemistry 50:9633-9640(2011).
CC -!- FUNCTION: Involved in olefin biosynthesis. Catalyzes the reversible
CC stereospecific NADPH-dependent reduction of 2-alkyl-3-oxoalkanoic acids
CC to 2-alkyl-3-hydroxyalkanoic acids. In the oxidative direction, syn-2-
CC decyl-3-hydroxytetradecanoic acid is the preferred substrate. In the
CC reductive direction, (2R/S)-2-hexyl-3-ketodecanoic acid is accepted as
CC substrate. {ECO:0000269|PubMed:21958090}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2R,3S)-2-alkyl-3-hydroxyalkanoate + NADP(+) = an (R)-2-
CC alkyl-3-oxoalkanoate + H(+) + NADPH; Xref=Rhea:RHEA:54796,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:138340, ChEBI:CHEBI:138341; EC=1.1.1.412;
CC Evidence={ECO:0000269|PubMed:21958090};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54798;
CC Evidence={ECO:0000269|PubMed:21958090};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24 uM for NADP {ECO:0000269|PubMed:21958090};
CC KM=26 uM for NADPH {ECO:0000269|PubMed:21958090};
CC KM=31 uM for syn-2-decyl-3-hydroxytetradecanoic acid
CC {ECO:0000269|PubMed:21958090};
CC KM=161 uM for (2R/S)-2-hexyl-3-ketodecanoic acid
CC {ECO:0000269|PubMed:21958090};
CC KM=181 uM for (2R,3S)-2-hexyl-3-hydroxydecanoic acid
CC {ECO:0000269|PubMed:21958090};
CC KM=202 uM for syn-2-hexyl-3-hydroxydecanoic acid
CC {ECO:0000269|PubMed:21958090};
CC KM=214 uM for syn-2-octyl-3-hydroxydodecanoic acid
CC {ECO:0000269|PubMed:21958090};
CC Note=kcat is 122 min(-1) for syn-2-octyl-3-hydroxydodecanoic acid as
CC substrate. kcat is 85 min(-1) for syn-2-decyl-3-hydroxytetradecanoic
CC acid as substrate. kcat is 79 min(-1) for (2R,3S)-2-hexyl-3-
CC hydroxydecanoic acid as substrate. kcat is 72 min(-1) for syn-2-
CC hexyl-3-hydroxydecanoic acid as substrate. kcat is 58 min(-1) for
CC (2R/S)-2-hexyl-3-ketodecanoic acid as substrate.
CC {ECO:0000269|PubMed:21958090};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21958090}.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
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DR EMBL; AM743169; CAQ43817.1; -; Genomic_DNA.
DR RefSeq; WP_012478771.1; NC_010943.1.
DR AlphaFoldDB; B2FI29; -.
DR SMR; B2FI29; -.
DR STRING; 522373.Smlt0209; -.
DR EnsemblBacteria; CAQ43817; CAQ43817; Smlt0209.
DR KEGG; sml:Smlt0209; -.
DR PATRIC; fig|522373.3.peg.200; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_6_1_6; -.
DR OMA; WGPGDTQ; -.
DR OrthoDB; 1928091at2; -.
DR BRENDA; 1.1.1.412; 5134.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01073; 3Beta_HSD; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..330
FT /note="2-alkyl-3-oxoalkanoate reductase"
FT /id="PRO_0000442980"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:21958090"
FT BINDING 143
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:21958090"
SQ SEQUENCE 330 AA; 35480 MW; A5329F0F85D161C0 CRC64;
MKILVTGGGG FLGQALCRGL VERGHQVLAF NRSHYPELQV MGVGQIRGDL ADPQAVLHAV
AGVDAVFHNG AKAGAWGSYD SYHQANVIGT DNVIAACRAH GIGRLVYTST PSVTHRATHP
VEGLGADEVP YGEDFQAPYA ATKAIAEQRV LAANDASLAT VALRPRLIWG PGDQQLVPRL
AERARQGRLR LVGDGSNKVD TTYIDNAALA HFLAFEALAP GAACAGKAYF ISNGEPLPMR
ELVNQLLAAV GAPRVDKAIS FKTAYRIGAI CERLWPLLRL RGEPPLTRFL AEQLCTPHWY
SMEPARRDFG YVPQVSIEEG LRRLKASSAA
