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Database: UniProt
Entry: A0A0M8SVT2_9ACTN
LinkDB: A0A0M8SVT2_9ACTN
Original site: A0A0M8SVT2_9ACTN 
ID   A0A0M8SVT2_9ACTN        Unreviewed;       367 AA.
AC   A0A0M8SVT2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
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};
DE   Flags: Fragment;
GN   ORFNames=ADK54_20540 {ECO:0000313|EMBL:KOU41488.1};
OS   Streptomyces sp. WM6378.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU41488.1, ECO:0000313|Proteomes:UP000037774};
RN   [1] {ECO:0000313|Proteomes:UP000037774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6378 {ECO:0000313|Proteomes:UP000037774};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOU41488.1}.
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DR   EMBL; LGDD01000268; KOU41488.1; -; Genomic_DNA.
DR   RefSeq; WP_053727123.1; NZ_LGDD01000268.1.
DR   AlphaFoldDB; A0A0M8SVT2; -.
DR   OrthoDB; 9785768at2; -.
DR   Proteomes; UP000037774; 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; 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   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          4..229
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          274..364
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   NON_TER         367
FT                   /evidence="ECO:0000313|EMBL:KOU41488.1"
SQ   SEQUENCE   367 AA;  38417 MW;  F9FF16892542B2B5 CRC64;
     MKSYIVGVGM TKFEKPESRD WQYWDMAKEA GSAALADAGI DYGSVEQVPV GYCFQASTAG
     QRAVYELGLT GVPVYNVNNN CATGSSALML ARQFVEGGIS DCVLALGFEK MKRGALGGGS
     DGGDFATSPV ARHYGIMAAR HGFEMTPPTA QIFGNAAREH MERYGTTAAQ LAAVGAKNHR
     HSVNNPNAQF QDAYSVEEIL AAKEIHRPLT KLQCSPTSDG SAAAVVVSER FVDRNGLRGK
     AVEIAGQSMT TDTEESFASG SCIDAVGAPM SRSAGRQAFA AAGLGIEDVD VIELHDCFSI
     NELLTYEALG MCGAGESGKL IESGATTYGG RWVVNPSGGL ISKGHPLGAT GLAQAAELVW
     QLRGEAG
//
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