ID A0A158KYG8_9BURK Unreviewed; 394 AA.
AC A0A158KYG8;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00012352};
DE EC=2.3.1.176 {ECO:0000256|ARBA:ARBA00012352};
DE AltName: Full=Propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00032316};
GN ORFNames=AWB68_07686 {ECO:0000313|EMBL:SAL85451.1};
OS Caballeronia choica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=326476 {ECO:0000313|EMBL:SAL85451.1, ECO:0000313|Proteomes:UP000054770};
RN [1] {ECO:0000313|Proteomes:UP000054770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Peeters C.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; FCON02000189; SAL85451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158KYG8; -.
DR OrthoDB; 9785768at2; -.
DR Proteomes; UP000054770; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd00829; SCP-x_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; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR PANTHER; PTHR42870; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR42870:SF1; NON-SPECIFIC LIPID-TRANSFER PROTEIN-LIKE 2; 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; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Transferase {ECO:0000256|RuleBase:RU003557};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 22..117
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 275..364
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 394 AA; 41844 MW; D632B77C435897C6 CRC64;
MSRKTFVAGV GMIPFRKPGM SEPYDVMGAG AVRQALADAG IDYADVQQAY AGYVYGDSTC
GQKALYHVGM TGVPVINVNN NCATGSSALF LARQAVQSGA VDCALAVGFE FMQPGALSSK
WNDRAPALER ALDLVNELVD RTDLPPAIRQ FSGAGRAHME KYGTKIETFA KIRAKASQHA
ARNPLAVFRN VVTTEDVLAS PMIWEGVLTR LMACPPTCGA AAAIVVSEEF ARKRGLRTDV
LIAGQSLTTD LPSTYDSRDM IRVVGFDMTR SGAKLAYEQA GVGPEDIDVI ELHDCFAQNE
LLTYEGLGLC GEGEAERLVN DGDNTYGGKW VVNPSGGLLS KGHPLGATGL AQCYELTHQM
RGTAEQRQVE GAKVALAHNL GLGGACVTTV YKAA
//
