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Database: UniProt
Entry: A0A024JXN3_9MYCO
LinkDB: A0A024JXN3_9MYCO
Original site: A0A024JXN3_9MYCO 
ID   A0A024JXN3_9MYCO        Unreviewed;       400 AA.
AC   A0A024JXN3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=ltp1_1_2 {ECO:0000313|EMBL:CDO88580.1};
GN   ORFNames=BN973_02949 {ECO:0000313|EMBL:CDO88580.1};
OS   Mycobacterium triplex.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium simiae complex.
OX   NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO88580.1};
RN   [1] {ECO:0000313|EMBL:CDO88580.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO88580.1};
RX   PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA   Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT   "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL   Genome Announc. Announc.2:e00499-e00414(2014).
RN   [2] {ECO:0000313|EMBL:CDO88580.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO88580.1};
RA   Urmite Genomes U.;
RL   Submitted (APR-2014) 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; HG964446; CDO88580.1; -; Genomic_DNA.
DR   RefSeq; WP_036468942.1; NZ_LQPY01000008.1.
DR   AlphaFoldDB; A0A024JXN3; -.
DR   STRING; 47839.BN973_02949; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_035425_4_0_11; -.
DR   OrthoDB; 9785768at2; -.
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; 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; 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          6..196
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          273..376
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   400 AA;  41520 MW;  3CD039826706D17F CRC64;
     MSSGDVWVVG AAMTKIGRYP DKDVIDLASD AVLGALRDAS IEMSQVQFLA CGNAYESNSG
     VAQRLQKQVG QMGIPAYNVF NACATGASAV RLAILAIKAE ECDVALAVGA EQMGKMGLLG
     NKGKRGDRKS FVPKGRYGGV LPTEGILGTQ LMPGVFAQAG MEYALQHGVT REQFAMIAVK
     NHRNSVRNPY AQYRKEFSLD EVLGAEVIAY PNTLPMCCPT GDGAAAVLVV SDRRLAQLDP
     DVRRRAVKIS ASVITTDPWT DSAQVQPDIN TLTRNAAALA YEAAGLGPGD LSLVELHDCF
     ATAELLHYDN LGLCPPGGAG DFISSGAADA DGRTPVNVSG GLLSKGHPIG ATGVAGLYEI
     ATQLRGEAGD RQVGGANVGL AHVIGLGSAC GIHILEKGAA
//
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