OLEC_SHEON
ID OLEC_SHEON Reviewed; 614 AA.
AC Q8EG64;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Olefin beta-lactone synthetase {ECO:0000305};
DE EC=6.1.3.1 {ECO:0000250|UniProtKB:Q8PDW6};
GN Name=oleC {ECO:0000303|PubMed:20418444};
GN OrderedLocusNames=SO_1744 {ECO:0000312|EMBL:AAN54798.1};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2]
RP FUNCTION IN OLEFIN BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=MR-1;
RX PubMed=20418444; DOI=10.1128/aem.00433-10;
RA Sukovich D.J., Seffernick J.L., Richman J.E., Hunt K.A., Gralnick J.A.,
RA Wackett L.P.;
RT "Structure, function, and insights into the biosynthesis of a head-to-head
RT hydrocarbon in Shewanella oneidensis strain MR-1.";
RL Appl. Environ. Microbiol. 76:3842-3849(2010).
CC -!- FUNCTION: Involved in olefin biosynthesis (PubMed:20418444). Catalyzes
CC the conversion of 2-alkyl-3-hydroxyalkanoic acids to beta-lactones in
CC the presence of ATP (By similarity). The S.oneidensis oleABCD genes
CC produce 3,6,9,12,15,19,22,25,28-hentriacontanonaene, which may aid the
CC cells in adapting to a sudden drop in temperature (PubMed:20418444).
CC {ECO:0000250|UniProtKB:Q8PDW6, ECO:0000269|PubMed:20418444}.
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:0000250|UniProtKB:Q8PDW6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23061;
CC Evidence={ECO:0000250|UniProtKB:Q8PDW6};
CC -!- DISRUPTION PHENOTYPE: Deletion of the entire oleABCD gene cluster leads
CC to the complete absence of nonpolar extractable products. The oleABCD
CC deletion strain shows a significantly longer lag phase than the wild-
CC type strain when shifted to a lower temperature.
CC {ECO:0000269|PubMed:20418444}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AE014299; AAN54798.1; -; Genomic_DNA.
DR RefSeq; NP_717354.1; NC_004347.2.
DR RefSeq; WP_011071876.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EG64; -.
DR SMR; Q8EG64; -.
DR STRING; 211586.SO_1744; -.
DR PaxDb; Q8EG64; -.
DR KEGG; son:SO_1744; -.
DR PATRIC; fig|211586.12.peg.1678; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_12_6; -.
DR OMA; WFCGRKS; -.
DR OrthoDB; 377638at2; -.
DR PhylomeDB; Q8EG64; -.
DR BioCyc; MetaCyc:MON-20168; -.
DR BioCyc; SONE211586:G1GMP-1599-MON; -.
DR BRENDA; 6.1.3.1; 5706.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12780; -; 1.
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..614
FT /note="Olefin beta-lactone synthetase"
FT /id="PRO_0000446915"
FT BINDING 229..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 371..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q08AH3"
SQ SEQUENCE 614 AA; 66991 MW; DC8DF210B2F447B5 CRC64;
MTKVDDALFE HGASAVAVEQ NNGRDNPTKP KDANICRHLK LAAHHIPHHL AVAVQQGKGK
SFANLTYQEL DFISLNKQSD AIAFALNAYG LTRGMKAVLM VTPSLDFFAL TFALFKAGII
PVLVDPGMGI KNLKQCFIEA APDAFIGIPK AHIARRLLGW GKASVKRLIN VDANQSGVTD
TLSRLLTGAP SLASMLSFTT KSSSAKLPEQ VEYPMALLEH DEMAAILFTS GSTGTPKGVV
YSHGMFEAQI QALKQDYGIA HGERDLATFP LFSLFGPALG MTSIVPEMDA SKPITANPEF
LFAAIEKYQC SNIFVNPALL ERLGRAGEQT DSKNQHKLSS VKRVISAGAP ATIASIARFS
KMLSDGVPVL NSYGATESLP ISMIASDELF TTTQVTDNGG GICVGRAIDG VKIEIIAITE
ADIPEWDNRL CLNAGEIGEI VVTGQMVSQS YYHREKATAA SKIWDSERQT FRHRMGDLGY
LDDSGRLWMC GRKAHRVDAT QGGQFAKRYY SIPCERIFNT HPNVKRSALV GVTVKGQHGV
GEIKPLICIE LDQSLVCNKS AQLYQELMVI AEQYSQTQGI RRFLIHPDFP VDVRHNAKIF
REKLAVWAQS QTKG
