(data stored in SCRATCH zone)

SWISSPROT: D3UZ83_XENBS

ID   D3UZ83_XENBS            Unreviewed;       387 AA.
AC   D3UZ83;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   SubName: Full=3-ketoacyl-CoA thiolase (Thiolase I, acetyl-CoA transferase), in complex with FadB catalyzes {ECO:0000313|EMBL:CBJ79665.1};
DE            EC=2.3.1.16 {ECO:0000313|EMBL:CBJ79665.1};
GN   Name=fadA {ECO:0000313|EMBL:CBJ79665.1};
GN   OrderedLocusNames=XBJ1_0516 {ECO:0000313|EMBL:CBJ79665.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79665.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79665.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79665.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the final step of fatty acid oxidation in
CC       which acetyl-CoA is released and the CoA ester of a fatty acid two
CC       carbons shorter is formed. {ECO:0000256|SAAS:SAAS00848546}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC         Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC         Evidence={ECO:0000256|SAAS:SAAS01118753};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|SAAS:SAAS00848504}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta
CC       chains (FadA). {ECO:0000256|SAAS:SAAS00848610}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00848528}.
CC   -!- SIMILARITY: Belongs to the thiolase family.
CC       {ECO:0000256|RuleBase:RU003557, ECO:0000256|SAAS:SAAS00850636}.
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DR   EMBL; FN667741; CBJ79665.1; -; Genomic_DNA.
DR   RefSeq; WP_012987121.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0516; -.
DR   EnsemblBacteria; CBJ79665; CBJ79665; XBJ1_0516.
DR   GeneID; 8830139; -.
DR   KEGG; xbo:XBJ1_0516; -.
DR   PATRIC; fig|406818.4.peg.476; -.
DR   eggNOG; ENOG4105CHU; Bacteria.
DR   eggNOG; COG0183; LUCA.
DR   HOGENOM; HOG000012239; -.
DR   KO; K00632; -.
DR   OMA; DYYWGMG; -.
DR   BioCyc; XBOV406818:XBJ1_RS02235-MONOMER; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR012805; FadA.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020610; Thiolase_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR   TIGRFAMs; TIGR02445; fadA; 1.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UZ83.
DR   SWISS-2DPAGE; D3UZ83.
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000256|SAAS:SAAS00850626, ECO:0000313|EMBL:CBJ79665.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00848560};
KW   Fatty acid metabolism {ECO:0000256|SAAS:SAAS00848562};
KW   Lipid degradation {ECO:0000256|SAAS:SAAS00848580};
KW   Lipid metabolism {ECO:0000256|SAAS:SAAS00848599};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Transferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000256|SAAS:SAAS00850637, ECO:0000313|EMBL:CBJ79665.1}.
FT   DOMAIN        4    254       Thiolase_N. {ECO:0000259|Pfam:PF00108}.
FT   DOMAIN      262    386       Thiolase_C. {ECO:0000259|Pfam:PF02803}.
FT   ACT_SITE     91     91       Acyl-thioester intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR000429-1}.
FT   ACT_SITE    343    343       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000429-1}.
FT   ACT_SITE    373    373       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000429-1}.
SQ   SEQUENCE   387 AA;  41094 MW;  8945117A2D09AB69 CRC64;
     MENVVIIDGI RTPMGRSKGG VFRQVRAEDL SAHLMKSILK RNPSVQPEHI DDISWGCVQQ
     TLEQGFNIAR NSALLAGIPH SVPAVTVNRL CGSSMQSLHD GARMIMTGDA SIAMIGGVEH
     MGHIPMTHGV DFHSKLNRNV AKAAGVMGLT AEMLAKMHGI SREMQDEFAL RSHLRAAQAT
     ESKAFSNEIA PIHGHDADGN LKFIDFDEVI RPDTNLKNLA GLRPVFDPVT GSVTAGNSSA
     LSDGASAMLI MSESKAKELG LKARARIRSM AVVGCDPSIM GYGPVPATQM ALKKAGLSLA
     DIGLIELNEA FAAQSLACMK GLNLLDSMDD RINLNGGAIA LGHPLGCSGA RITTTLLNLM
     ERKDVQFGLA TMCIGLGQGI ATIIERV
//

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