ID A0A0K2YF22_9NOCA Unreviewed; 441 AA.
AC A0A0K2YF22;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=3-ketoacyl-CoA thiolase {ECO:0000313|EMBL:CRK50587.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:CRK50587.1};
GN Name=fadI {ECO:0000313|EMBL:CRK50587.1};
GN ORFNames=RHCRD62_20026 {ECO:0000313|EMBL:CRK50587.1};
OS Rhodococcus sp. RD6.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=260936 {ECO:0000313|EMBL:CRK50587.1, ECO:0000313|Proteomes:UP000044872};
RN [1] {ECO:0000313|EMBL:CRK50587.1, ECO:0000313|Proteomes:UP000044872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RD6.2 {ECO:0000313|EMBL:CRK50587.1,
RC ECO:0000313|Proteomes:UP000044872};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CVQP01000005; CRK50587.1; -; Genomic_DNA.
DR RefSeq; WP_050063928.1; NZ_CVQP01000005.1.
DR AlphaFoldDB; A0A0K2YF22; -.
DR STRING; 260936.RHCRD62_20026; -.
DR OrthoDB; 1402717at2; -.
DR Proteomes; UP000044872; Unassembled WGS sequence.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; 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; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:CRK50587.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000044872};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:CRK50587.1}.
FT DOMAIN 22..289
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 300..441
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 106
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 398
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 428
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 441 AA; 46557 MW; F6B6B3654972C337 CRC64;
MTPRARTTKK PAAPTGRQLR PVAIVGGNRI PFARSDKAYA QASNQDMFTA TLDGLVSRFN
LQGEQLGMVV GGAVLKHARD FNLIRESVLG SALSPYTPAY DLQQACGTGL QSIVAVGDAI
AAGRIDAGIG GGTDTTSDAP IGVNNELREF LLSINRARTT GERVKLLGHV RPSMVGIEIP
RNGEPRTGLS MGDHAAITAK EFGVRREDQD ELAAASHKNM AAAYDRGFFD DLVTPFLGLT
RDDNLRPGST VEKLATLKPV FGTKLGDATM TAGNSTPLTD GASAVLLSTD EWAAQRNLPV
LAHLVDSETA AVDYVHGDDG LLMAPTYAVP RLLARNGLTL QDFDYYEIHE AFASVVLATL
QAWESDEYCK ERLGLDSALG KIDRSKLNVN GSSLAAGHPF AATGGRIVAS LAKMLAEKGS
GRGLISICAA GGQGVTAIIE R
//