ID   OLEB_XANCP              Reviewed;         300 AA.
AC   Q8PDW8;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Cis-3-alkyl-4-alkyloxetan-2-one decarboxylase {ECO:0000305};
DE            EC=4.1.1.114 {ECO:0000269|PubMed:28029240};
GN   Name=oleB {ECO:0000303|PubMed:28029240};
GN   OrderedLocusNames=XCC0216 {ECO:0000312|EMBL:AAM39535.1};
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
RN   [2]
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   [3]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=28223313; DOI=10.1128/jb.00890-16;
RA   Christenson J.K., Jensen M.R., Goblirsch B.R., Mohamed F., Zhang W.,
RA   Wilmot C.M., Wackett L.P.;
RT   "Active multienzyme assemblies for long-chain olefinic hydrocarbon
RT   biosynthesis.";
RL   J. Bacteriol. 199:E00890-E00890(2017).
CC   -!- FUNCTION: Involved in olefin biosynthesis (PubMed:28029240,
CC       PubMed:28223313). Catalyzes the elimination of carbon dioxide from
CC       beta-lactones to form the final olefin product (PubMed:28029240).
CC       {ECO:0000269|PubMed:28029240, ECO:0000269|PubMed:28223313}.
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:0000269|PubMed:28029240};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18346;
CC         Evidence={ECO:0000269|PubMed:28029240};
CC   -!- SUBUNIT: Homotetramer. Forms a complex with OleC and OleD.
CC       {ECO:0000269|PubMed:28223313}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:28223313}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; AE008922; AAM39535.1; -; Genomic_DNA.
DR   RefSeq; NP_635611.1; NC_003902.1.
DR   RefSeq; WP_011035472.1; NC_003902.1.
DR   AlphaFoldDB; Q8PDW8; -.
DR   SMR; Q8PDW8; -.
DR   STRING; 340.xcc-b100_0235; -.
DR   ESTHER; xancp-OleB; Haloalkane_dehalogenase-HLD1.
DR   EnsemblBacteria; AAM39535; AAM39535; XCC0216.
DR   KEGG; xcc:XCC0216; -.
DR   PATRIC; fig|190485.4.peg.242; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_020336_13_3_6; -.
DR   OMA; HATVHEF; -.
DR   BioCyc; MetaCyc:MON-20174; -.
DR   BRENDA; 4.1.1.114; 9230.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 1.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lyase; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Cis-3-alkyl-4-alkyloxetan-2-one decarboxylase"
FT                   /id="PRO_0000446914"
FT   DOMAIN          33..282
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   300 AA;  34080 MW;  39702E388B035767 CRC64;
     MTYPGYSFTP KRLDVRPGIA MSYLDEGPSD GEVVVMLHGN PSWGYLWRHL VSGLSDRYRC
     IVPDHIGMGL SDKPDDAPDA QPRYDYTLQS RVDDLDRLLQ HLGITGPITL AVHDWGGMIG
     FGWALSHHAQ VKRLVITNTA AFPLPPEKPM PWQIAMGRHW RLGEWFIRTF NAFSSGASWL
     GVSRRMPAAV RRAYVAPYDN WKNRISTIRF MQDIPLSPAD QAWSLLERSA QALPSFADRP
     AFIAWGLRDI CFDKHFLAGF RRALPQAEVM AFDDANHYVL EDKHEVLVPA IRAFLERNPL