ID W9GPR6_9MICO Unreviewed; 436 AA.
AC W9GPR6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EWT05889.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:EWT05889.1};
GN ORFNames=N864_01440 {ECO:0000313|EMBL:EWT05889.1};
OS Intrasporangium chromatireducens Q5-1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=584657 {ECO:0000313|EMBL:EWT05889.1, ECO:0000313|Proteomes:UP000019494};
RN [1] {ECO:0000313|Proteomes:UP000019494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q5-1 {ECO:0000313|Proteomes:UP000019494};
RA Liu H., Wang G.;
RT "Intrasporangium oryzae NRRL B-24470.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {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:EWT05889.1}.
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DR EMBL; AWQS01000079; EWT05889.1; -; Genomic_DNA.
DR RefSeq; WP_034716534.1; NZ_AWQS01000079.1.
DR AlphaFoldDB; W9GPR6; -.
DR PATRIC; fig|584657.3.peg.2217; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000019494; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase 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:EWT05889.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019494};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EWT05889.1}.
FT DOMAIN 13..280
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 289..435
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 96
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 423
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 436 AA; 46157 MW; FF47A4A3CAF25B25 CRC64;
MPQTSPRPVR RAAILGGNRI PFARAHGAYA RASNQDMLTA TLDGLVARFG LAGERMGEVV
AGAVLKHSRD FNLTRESVLG SQLDPHTPAY DVQQACGTGL EAAILVANKI ALGQVEAGIA
GGTDTASDAP IAVSEGLRQT LLAANRAKTL PDRLKALASL RPADLVPAIP QNVEPRTGLS
MGEHMALTAE EWGVTRAEQD ELAAASHRHL AAAYDRGFFD DLVTPYLGVT RDNNLRPDST
VEQLGKLRTV FGRGPDATMT AGNSTPLTDG ASAVLLASEE WAAEHRLSPL AWFVDAETAA
VDYVHGHEGL LMAPAYAVPR LLARNGLTLQ DFDFYEIHEA FAATVLALLK AWEDPRFSKE
RLGLDAPLGS IDRARLNVTG SSLATGHPFA ATGGRIVATL AKLLHEKKQQ DPGRTVRGLI
SICAAGGQGV TAILEA
//