ID A0A2X4U6Z9_9NOCA Unreviewed; 382 AA.
AC A0A2X4U6Z9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetyl-CoA acyltransferase {ECO:0000313|EMBL:SQI35576.1};
DE EC=2.3.1.- {ECO:0000313|EMBL:SQI35576.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:SQI35576.1};
GN Name=fadA_6 {ECO:0000313|EMBL:SQI35576.1};
GN ORFNames=NCTC10994_03027 {ECO:0000313|EMBL:SQI35576.1};
OS Rhodococcus coprophilus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=38310 {ECO:0000313|EMBL:SQI35576.1, ECO:0000313|Proteomes:UP000249091};
RN [1] {ECO:0000313|EMBL:SQI35576.1, ECO:0000313|Proteomes:UP000249091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10994 {ECO:0000313|EMBL:SQI35576.1,
RC ECO:0000313|Proteomes:UP000249091};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; LS483468; SQI35576.1; -; Genomic_DNA.
DR RefSeq; WP_072703693.1; NZ_LS483468.1.
DR AlphaFoldDB; A0A2X4U6Z9; -.
DR STRING; 1219011.GCA_001895045_03704; -.
DR KEGG; rcr:NCTC10994_03027; -.
DR Proteomes; UP000249091; Chromosome 1.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
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 NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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 ECO:0000313|EMBL:SQI35576.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000249091};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SQI35576.1}.
FT DOMAIN 4..248
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 257..378
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 336
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 366
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 382 AA; 39476 MW; 8C11D947530C60F3 CRC64;
MREVVIVEAI RTPVGKRNGG LSGVHPVDLS AHILQALAER TGIDPAVIDD VVWGCVSQVG
DQSSNVGRYS VLAAGWPESI PGTTVNRACG SSQQALDFAA QAVMSGQQDV VVAGGVEVMS
RVPLGAARGT GMPYGPKALE RYDGFPFNQG ISAEKIAQKW GLSRTRLDEY SVLSHERAAA
AQDRGAFDGQ IVPVATEAGA VSADEGIRRG STVDKLAGLK PAFAEDGVIH AGNSSQISDG
AAALLVTTPE KARELGLTPL ARYRAGAVAG SDPVLMLTGP IPATEKVLAK AGVALGEVGV
FEVNEAFASV PLAWLAETGA DIERVNPLGG AIALGHPLGG SGAVLMTRMI HHMRDQGLRY
GLQTMCEGGG TANATVVELM DR
//
