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Database: UniProt
Entry: A0A157SIG9_9BORD
LinkDB: A0A157SIG9_9BORD
Original site: A0A157SIG9_9BORD 
ID   A0A157SIG9_9BORD        Unreviewed;       395 AA.
AC   A0A157SIG9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
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   Name=thlA_3 {ECO:0000313|EMBL:SAI70239.1};
GN   ORFNames=SAMEA3906486_02977 {ECO:0000313|EMBL:SAI70239.1};
OS   Bordetella ansorpii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI70239.1, ECO:0000313|Proteomes:UP000076848};
RN   [1] {ECO:0000313|EMBL:SAI70239.1, ECO:0000313|Proteomes:UP000076848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H050680373 {ECO:0000313|EMBL:SAI70239.1,
RC   ECO:0000313|Proteomes:UP000076848};
RG   Pathogen Informatics;
RL   Submitted (APR-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; FKIF01000006; SAI70239.1; -; Genomic_DNA.
DR   RefSeq; WP_016452565.1; NZ_FKIF01000006.1.
DR   AlphaFoldDB; A0A157SIG9; -.
DR   STRING; 288768.SAMEA3906486_02977; -.
DR   GeneID; 75273069; -.
DR   OrthoDB; 9785768at2; -.
DR   Proteomes; UP000076848; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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; 2.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:SAI70239.1};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076848};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SAI70239.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          5..192
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          272..366
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   395 AA;  41706 MW;  BC04DC1AC6BBDC2E CRC64;
     MQEPVLVAGV GMTPFKKPGD NLPYPEMAAQ AIREALQDAG LTYSDVQDVY AGYVYGDSAS
     GQRAVYEVGM TGVPVINVNN NCSSGSTALY MARKAVANGS ADCALAVGFE QMPAGALRAY
     WDDRPDPLDH FNGVMDEIFG HPELPMAIRY FGAAGREHME RYGTPLDTFA RIRAKASRHA
     ARNPLALFRK EVTVEEVLAS SPLVPGAMTR LMACPPTCGA AAAVFVSKKF AQKMGLSANV
     QVLAQSLVSD RPGAFADKSA ISVVGFDMTR EAARQVYEAA GVGPQDIDVC ELHDCFAQNE
     LLSYEGLGFC AVGEGRAFVE SDSNTYGGAV VVNPSGGLLS KGHPLGATGL AQCYELTHQL
     RGSAEARQVE GARLALQHNA GLGGATVVTL YGRAD
//
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