Back to PBIL home page
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}.
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; 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
//
Back to PBIL home page