OLEC_STRMK
ID OLEC_STRMK Reviewed; 552 AA.
AC B2FI28;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Olefin beta-lactone synthetase {ECO:0000305};
DE EC=6.1.3.1 {ECO:0000269|PubMed:28029240};
GN Name=oleC {ECO:0000303|PubMed:20823539};
GN OrderedLocusNames=Smlt0208 {ECO:0000312|EMBL:CAQ43816.1};
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, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=27238740; DOI=10.1002/cbic.201600063;
RA Kancharla P., Bonnett S.A., Reynolds K.A.;
RT "Stenotrophomonas maltophilia OleC-catalyzed ATP-dependent formation of
RT long-chain Z-olefins from 2-alkyl-3-hydroxyalkanoic acids.";
RL ChemBioChem 17:1426-1429(2016).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28029240; DOI=10.1021/acs.biochem.6b01199;
RA Christenson J.K., Richman J.E., Jensen M.R., Neufeld J.Y., Wilmot C.M.,
RA Wackett L.P.;
RT "beta-lactone synthetase found in the olefin biosynthesis pathway.";
RL Biochemistry 56:348-351(2017).
RN [4]
RP CRYSTALLIZATION, AND SUBUNIT.
RC STRAIN=ATCC 17679;
RX PubMed=20823539; DOI=10.1107/s1744309110031751;
RA Frias J.A., Goblirsch B.R., Wackett L.P., Wilmot C.M.;
RT "Cloning, purification, crystallization and preliminary X-ray diffraction
RT of the OleC protein from Stenotrophomonas maltophilia involved in head-to-
RT head hydrocarbon biosynthesis.";
RL Acta Crystallogr. F 66:1108-1110(2010).
CC -!- FUNCTION: Involved in olefin biosynthesis (PubMed:27238740,
CC PubMed:28029240). Catalyzes the conversion of beta-hydroxy acid
CC substrates to beta-lactones in the presence of ATP (PubMed:28029240).
CC Can use all four stereoisomers of 2-hexyl-3-hydroxydecanoic acid
CC (PubMed:27238740). {ECO:0000269|PubMed:27238740,
CC ECO:0000269|PubMed:28029240}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2R,3S)-2-alkyl-3-hydroxyalkanoate + ATP = a cis-3-alkyl-4-
CC alkyloxetan-2-one + AMP + diphosphate; Xref=Rhea:RHEA:23060,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138340,
CC ChEBI:CHEBI:138483, ChEBI:CHEBI:456215; EC=6.1.3.1;
CC Evidence={ECO:0000269|PubMed:28029240};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23061;
CC Evidence={ECO:0000269|PubMed:28029240};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.0 uM for (2R,3S)-2-hexyl-3-hydroxydecanoic acid
CC {ECO:0000269|PubMed:27238740};
CC KM=8.8 uM for (2S,3S)-2-hexyl-3-hydroxydecanoic acid
CC {ECO:0000269|PubMed:27238740};
CC KM=5.14 uM for (2S,3R)-2-hexyl-3-hydroxydecanoic acid
CC {ECO:0000269|PubMed:27238740};
CC KM=7.12 uM for (2R,3R)-2-hexyl-3-hydroxydecanoic acid
CC {ECO:0000269|PubMed:27238740};
CC KM=6.23 uM for ATP {ECO:0000269|PubMed:27238740};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20823539}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AM743169; CAQ43816.1; -; Genomic_DNA.
DR RefSeq; WP_012478770.1; NC_010943.1.
DR AlphaFoldDB; B2FI28; -.
DR SMR; B2FI28; -.
DR STRING; 522373.Smlt0208; -.
DR EnsemblBacteria; CAQ43816; CAQ43816; Smlt0208.
DR KEGG; sml:Smlt0208; -.
DR PATRIC; fig|522373.3.peg.199; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_12_6; -.
DR OMA; WFCGRKS; -.
DR OrthoDB; 377638at2; -.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..552
FT /note="Olefin beta-lactone synthetase"
FT /id="PRO_0000446916"
FT BINDING 182..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 316..321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 425
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
SQ SEQUENCE 552 AA; 58578 MW; B8BAD2444E976710 CRC64;
MNRPCNIAAR LPELARERPD QIAIRCPGRR GAGNGMAAYD VTLDYRQLDA RSDAMAAGLA
GYGIGRGVRT VVMVRPSPEF FLLMFALFKL GAVPVLVDPG IDRRALKQCL DEAQPEAFIG
IPLAHVARLV LRWAPSAARL VTVGRRLGWG GTTLAALERA GAKGGPMLAA TDGEDMAAIL
FTSGSTGVPK GVVYRHRHFV GQIQLLGSAF GMEAGGVDLP TFPPFALFDP ALGLTSVIPD
MDPTRPAQAD PVRLHDAIQR FGVTQLFGSP ALMRVLAKHG RPLPTVTRVT SAGAPVPPDV
VATIRSLLPA DAQFWTPYGA TECLPVAVVE GRELERTRAA TEAGAGTCVG SVVAPNEVRI
IAIDDAPLAD WSQARVLAVG EVGEITVAGP TATDSYFNRP QATAAAKIRE TLADGSTRVV
HRMGDVGYFD AQGRLWFCGR KTQRVETARG PLYTEQVEPV FNTVAGVART ALVGVGAAGA
QVPVLCVELL RGQSDSPALQ EALRAHAAAR TPEAGLQHFL VHPAFPVDIR HNAKIGREKL
AVWASAELEK RA
