ID   OLEA_SHEON              Reviewed;         349 AA.
AC   Q8EG66;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Acyl-CoA:acyl-CoA alkyltransferase {ECO:0000305};
DE            EC=2.3.3.20 {ECO:0000250|UniProtKB:Q8PDX2};
GN   Name=oleA {ECO:0000303|PubMed:20418444};
GN   OrderedLocusNames=SO_1742 {ECO:0000312|EMBL:AAN54796.1};
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       a non-decarboxylative head-to-head Claisen condensation of two acyl-CoA
CC       molecules, generating an (R)-2-alkyl-3-oxoalkanoate (By similarity).
CC       The S.oneidensis oleABCD genes produce 3,6,9,12,15,19,22,25,28-
CC       hentriacontanonaene, which may aid the cells in adapting to a sudden
CC       drop in temperature (PubMed:20418444). {ECO:0000250|UniProtKB:Q8PDX2,
CC       ECO:0000269|PubMed:20418444}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-saturated acyl-CoA + an acyl-CoA + H2O = an (R)-2-alkyl-
CC         3-oxoalkanoate + 2 CoA + H(+); Xref=Rhea:RHEA:55980,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:138341, ChEBI:CHEBI:142092;
CC         EC=2.3.3.20; Evidence={ECO:0000250|UniProtKB:Q8PDX2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55981;
CC         Evidence={ECO:0000250|UniProtKB:Q8PDX2};
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 thiolase-like superfamily. OleA family.
CC       {ECO:0000305}.
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DR   EMBL; AE014299; AAN54796.1; -; Genomic_DNA.
DR   RefSeq; NP_717352.1; NC_004347.2.
DR   RefSeq; WP_011071874.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EG66; -.
DR   SMR; Q8EG66; -.
DR   STRING; 211586.SO_1742; -.
DR   PaxDb; Q8EG66; -.
DR   KEGG; son:SO_1742; -.
DR   PATRIC; fig|211586.12.peg.1676; -.
DR   eggNOG; COG0332; Bacteria.
DR   HOGENOM; CLU_039592_4_2_6; -.
DR   OMA; VITHQTS; -.
DR   OrthoDB; 872193at2; -.
DR   PhylomeDB; Q8EG66; -.
DR   BioCyc; MetaCyc:MON-17299; -.
DR   BioCyc; SONE211586:G1GMP-1597-MON; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR013747; ACP_syn_III_C.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020616; Thiolase_N.
DR   Pfam; PF08541; ACP_syn_III_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..349
FT                   /note="Acyl-CoA:acyl-CoA alkyltransferase"
FT                   /id="PRO_0000446911"
FT   ACT_SITE        97
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8PDX2"
FT   ACT_SITE        123
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8PDX2"
FT   SITE            276
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8PDX2"
SQ   SEQUENCE   349 AA;  37831 MW;  4EE8649750BB1641 CRC64;
     MKYSRVFINS LAYELAPVVV SSSELESRLA PLYQKFRIPM GQLAALTGIT ERRWWPKGHQ
     LSDGAINAAH KAIAETGIDV AELGAVVYTG VCRDQHEPAT ACRIAAALGV SKDTAIYDIS
     NACLGVLSGI LDIANRIELG QIKAGMVVSC ESARDIVDVT IDNMLADPTM QNFAQSLATL
     TGGSGAVAVI LTDGSLPLTN VRKHQLLGAS HLSAPQHHQL CQWGLQEVGH NIYREFMRTD
     AVTLLKEGVE LAKHTWEHFL AQRNWLVEQV DKVICHQVGA SNRKQVLSAL NIPPEKEFPT
     YQLLGNMGTV SLPVTAAMAH DQGFLRPGDQ VSFLGIGSGL NCMMLGIKW