ID A0A157P924_9BORD Unreviewed; 391 AA.
AC A0A157P924;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN Name=fadA5_1 {ECO:0000313|EMBL:SAI69239.1};
GN ORFNames=SAMEA3906487_01706 {ECO:0000313|EMBL:SAI69239.1};
OS Bordetella trematum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI69239.1, ECO:0000313|Proteomes:UP000076825};
RN [1] {ECO:0000313|EMBL:SAI69239.1, ECO:0000313|Proteomes:UP000076825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H044680328 {ECO:0000313|EMBL:SAI69239.1,
RC ECO:0000313|Proteomes:UP000076825};
RG Pathogen Informatics;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; LT546645; SAI69239.1; -; Genomic_DNA.
DR RefSeq; WP_033535531.1; NZ_UFUJ01000001.1.
DR AlphaFoldDB; A0A157P924; -.
DR STRING; 123899.SAMEA3906487_01706; -.
DR GeneID; 56591010; -.
DR KEGG; btrm:SAMEA390648701706; -.
DR PATRIC; fig|123899.6.peg.1692; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 8951704at2; -.
DR Proteomes; UP000076825; Chromosome 1.
DR GO; GO:0033812; F:3-oxoadipyl-CoA thiolase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
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 NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:SAI69239.1}; Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000076825};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 5..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..389
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 391 AA; 41223 MW; 300253D6C06A0584 CRC64;
MRQAVIVSTA RTPLAKSHRG EFNITPGPTL ASFAVRAAVE RSGVDPQQIE DLILGCGFPE
GTTGRNVARQ TVVRSELPLS IGGTTVNRYC ASGLQALAFA ASRIVCDGAP AMIAGGVESI
SALRNQGDSG RDPWIVAHKP ALYMEMIDTA DVVARRYGIT REAQDRFALE SQRKTAQAQA
AGRFDEEIVS VTTVMAVTDR QSGAVSEREV TISADGCNRP DTRLEGLAAL TPVKGEGAFV
TAGNASQLSD GASASVLMEA RLAERLGLQP LGALRGFVVA GCEPDEMGIG PVLAVPRLLQ
RHGLTVEDID LWELNEAFAS QALYCQEQLG IPDERLNVDG GAISVGHPFG MTGARLAGHL
LLEGRRRKAR LGVVTMCVGG GMGAAALFEI F
//