ID A0A1Q4DUT1_9PSEU Unreviewed; 417 AA.
AC A0A1Q4DUT1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=BGP03_04085 {ECO:0000313|EMBL:OJY48104.1};
OS Pseudonocardia sp. 73-21.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1895809 {ECO:0000313|EMBL:OJY48104.1, ECO:0000313|Proteomes:UP000186163};
RN [1] {ECO:0000313|EMBL:OJY48104.1, ECO:0000313|Proteomes:UP000186163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73-21 {ECO:0000313|EMBL:OJY48104.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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 -!- 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:OJY48104.1}.
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DR EMBL; MKVV01000042; OJY48104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4DUT1; -.
DR STRING; 1895809.BGP03_04085; -.
DR Proteomes; UP000186163; Unassembled WGS sequence.
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; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
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 Transferase {ECO:0000256|RuleBase:RU003557};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..246
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 287..385
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 417 AA; 43222 MW; 22122AF59D32A4B4 CRC64;
MSEAVHVVGV SCTRFGRHPD RGAGTMARQA LSDVLADAGT HLRDVGAVFY ANVSQKAVEG
QHMIPGQVAL RPAGVTGIPV VNVENACAGG ATAFWLAVAH VRSGQSPAAV AVGVDKLVLP
DAAAALAVFD GALDRAHRCT ALRTLNRVAG VAHEPGEHEG AQDRRSVFMD IYAALALAHM
NRFGTTARQL ATVAAKNHLH SVDNERAQYR RPFTVDDVLA ARTVAHPLTV PMCSPVSDGA
AAVLVGNTDF AASLPTPDRH VTVRASVLVS GSDREPDDVE AHLGRRAAIA AYEQAGLGPR
DVDVAEVHDA TAFGEIQQTE NLGFCPIGDG GQWAESGASA LGGRLPVNPS GGLVSRGHPV
SATGLAQLFE LVTQLRGEAG ARQVDGARIA VAENGGALYG VEEAVAAISV LEKGFRR
//
