ID   OLEC_XANCP              Reviewed;         556 AA.
AC   Q8PDW6;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 81.
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:21266575};
GN   OrderedLocusNames=XCC0218 {ECO:0000312|EMBL:AAM39537.1};
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 IN OLEFIN BIOSYNTHESIS.
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=21266575; DOI=10.1074/jbc.m110.216127;
RA   Frias J.A., Richman J.E., Erickson J.S., Wackett L.P.;
RT   "Purification and characterization of OleA from Xanthomonas campestris and
RT   demonstration of a non-decarboxylative Claisen condensation reaction.";
RL   J. Biol. Chem. 286:10930-10938(2011).
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   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:21266575,
CC       PubMed:28029240, PubMed:28223313). Catalyzes the conversion of 2-alkyl-
CC       3-hydroxyalkanoic acids to beta-lactones in the presence of ATP
CC       (PubMed:28029240). {ECO:0000269|PubMed:21266575,
CC       ECO:0000269|PubMed:28029240, ECO:0000269|PubMed:28223313}.
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   -!- SUBUNIT: Monomer. Forms a complex with OleB and OleD.
CC       {ECO:0000269|PubMed:28223313}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:28223313}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE008922; AAM39537.1; -; Genomic_DNA.
DR   RefSeq; NP_635613.2; NC_003902.1.
DR   AlphaFoldDB; Q8PDW6; -.
DR   SMR; Q8PDW6; -.
DR   STRING; 340.xcc-b100_0237; -.
DR   EnsemblBacteria; AAM39537; AAM39537; XCC0218.
DR   KEGG; xcc:XCC0218; -.
DR   PATRIC; fig|190485.4.peg.245; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_12_6; -.
DR   OMA; WFCGRKS; -.
DR   BioCyc; MetaCyc:MON-20173; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
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; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..556
FT                   /note="Olefin beta-lactone synthetase"
FT                   /id="PRO_0000446917"
FT   BINDING         187..195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         321..326
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         430
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
FT   BINDING         445
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q08AH3"
SQ   SEQUENCE   556 AA;  59170 MW;  024740D49113F9D7 CRC64;
     MGDNGRMTTL CNIAASLPRL ARERPDQIAI RCPGGRGANG MAAYDVTLSY AELDARSDAI
     AAGLALHGIG RGVRAVVMVR PSPEFFLLMF ALFKAGAVPV LVDPGIDKRA LKQCLDEAQP
     QAFIGIPLAQ LARRLLRWAP SATQIVTVGG RYCWGGVTLA RVERDGAGAG SQLADTAADD
     VAAILFTSGS TGVPKGVVYR HRHFVGQIEL LRNAFDMQPG GVDLPTFPPF ALFDPALGLT
     SVIPDMDPTR PATADPRKLH DAMTRFGVTQ LFGSPALMRV LADYGQPLPN VRLATSAGAP
     VPPDVVAKIR ALLPADAQFW TPYGATECLP VAAIEGRTLD ATRTATEAGA GTCVGQVVAP
     NEVRIIAIDD AAIPEWSGVR VLAAGEVGEI TVAGPTTTDT YFNRDAATRN AKIRERCSDG
     SERVVHRMGD VGYFDAEGRL WFCGRKTHRV ETATGPLYTE QVEPIFNVHP QVRRTALVGV
     GTPGQQQPVL CVELQPGVAA SAFAEVETAL RAVGAAHPHT AGIARFLRHS GFPVDIRHNA
     KIGREKLAIW AAQQRV