ID   OLEB_SHEON              Reviewed;         318 AA.
AC   Q8EG65;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Cis-3-alkyl-4-alkyloxetan-2-one decarboxylase {ECO:0000305};
DE            EC=4.1.1.114 {ECO:0000250|UniProtKB:Q8PDW8};
GN   Name=oleB {ECO:0000303|PubMed:20418444};
GN   OrderedLocusNames=SO_1743 {ECO:0000312|EMBL:AAN54797.1};
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 elimination of carbon dioxide from beta-lactones to form the final
CC       olefin product (By similarity). The S.oneidensis oleABCD genes produce
CC       3,6,9,12,15,19,22,25,28-hentriacontanonaene, which may aid the cells in
CC       adapting to a sudden drop in temperature (PubMed:20418444).
CC       {ECO:0000250|UniProtKB:Q8PDW8, ECO:0000269|PubMed:20418444}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cis-3-alkyl-4-alkyloxetan-2-one = a cis-alkene + CO2;
CC         Xref=Rhea:RHEA:18345, ChEBI:CHEBI:16526, ChEBI:CHEBI:138483,
CC         ChEBI:CHEBI:139021; EC=4.1.1.114;
CC         Evidence={ECO:0000250|UniProtKB:Q8PDW8};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18346;
CC         Evidence={ECO:0000250|UniProtKB:Q8PDW8};
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 AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; AE014299; AAN54797.1; -; Genomic_DNA.
DR   RefSeq; NP_717353.1; NC_004347.2.
DR   RefSeq; WP_011071875.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EG65; -.
DR   SMR; Q8EG65; -.
DR   STRING; 211586.SO_1743; -.
DR   ESTHER; sheon-SO1743; Haloalkane_dehalogenase-HLD1.
DR   PaxDb; Q8EG65; -.
DR   KEGG; son:SO_1743; -.
DR   PATRIC; fig|211586.12.peg.1677; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_020336_13_3_6; -.
DR   OMA; HATVHEF; -.
DR   OrthoDB; 1890883at2; -.
DR   PhylomeDB; Q8EG65; -.
DR   BioCyc; MetaCyc:MON-20169; -.
DR   BioCyc; SONE211586:G1GMP-1598-MON; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   Pfam; PF00561; Abhydrolase_1; 2.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..318
FT                   /note="Cis-3-alkyl-4-alkyloxetan-2-one decarboxylase"
FT                   /id="PRO_0000446913"
FT   DOMAIN          30..275
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   318 AA;  36114 MW;  6204F71A8B2270DD CRC64;
     MLDTLLPFKR HFLSRNGNKL HYINEGQGEP VVMVHGNPSW SFYYRNLVSA LKDTHQCIVP
     DHIGCGLSDK PDDSGYDYTL KNRIDDLEAL LDSLNVKENI TLVVHDWGGM IGMGYAARYP
     ERIKRLVILN TGAFHLPDTK PLPLALWICR NTLLGTVLVR GFNAFSSIAS YVGVKRQPMS
     KYIREAYVAP FNSWANRIST LRFVQDIPLK PGDRNYQLVS DIAASLPKFA KVPTLICWGL
     QDFVFDKHFL VKWREHMPHA QVHEFADCGH YILEDASDEV ITHIKHFMTE TETLATQVNP
     ADSITEFESA SQAPQAER