ID A0A1I3WI82_9PSEU Unreviewed; 391 AA.
AC A0A1I3WI82;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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 ORFNames=SAMN05421835_11336 {ECO:0000313|EMBL:SFK07070.1};
OS Amycolatopsis sacchari.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=115433 {ECO:0000313|EMBL:SFK07070.1, ECO:0000313|Proteomes:UP000199025};
RN [1] {ECO:0000313|EMBL:SFK07070.1, ECO:0000313|Proteomes:UP000199025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44468 {ECO:0000313|EMBL:SFK07070.1,
RC ECO:0000313|Proteomes:UP000199025};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FORP01000013; SFK07070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3WI82; -.
DR STRING; 115433.SAMN05421835_11336; -.
DR OrthoDB; 9785768at2; -.
DR Proteomes; UP000199025; 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:0017000; P:antibiotic biosynthetic process; 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 ECO:0000313|EMBL:SFK07070.1};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
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:UP000199025};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SFK07070.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 14..189
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 268..359
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 391 AA; 41008 MW; AC0C4AA80D8E328C CRC64;
MGRRAAVAGV GMVPFATPSR SKSYDVLAET AVRAALTDAG IGLDRVEQAY AGYVYGDSTS
GQNALYRVGM TGVPVINVSN NCSTGSSALF LARQAVTSGA ADCVLAFGFE QMRRGALKGY
WDDRPSPFAR FDAVLGDDGA DVPMAPRYFG GAGAAYCERY GLDPRVFARI AVKARRHAAN
NPYAVFTGQV TVEEVLASPR ITGPLTRLQC CPPTCGAAAA VVVSEEFARR HGLRTGVVIT
AQAMTTDTPA SFGGDLMKLV GYDMTKSAAH QVYETAGVSP EDIPVVELHD CFTTNELLSY
EALGLTPEGT AEKFIADGDN TYGGRVVTNP SGGLLSKGHP LGATGLAQCA ELVWQLRGEA
GPRQVEGANI ALQHNIGLGG AAVVTLYEKV R
//
