ID E0IB40_9BACL Unreviewed; 400 AA.
AC E0IB40;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=PaecuDRAFT_2767 {ECO:0000313|EMBL:EFM10331.1};
OS Paenibacillus curdlanolyticus YK9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM10331.1, ECO:0000313|Proteomes:UP000005387};
RN [1] {ECO:0000313|EMBL:EFM10331.1, ECO:0000313|Proteomes:UP000005387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK9 {ECO:0000313|EMBL:EFM10331.1,
RC ECO:0000313|Proteomes:UP000005387};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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; AEDD01000007; EFM10331.1; -; Genomic_DNA.
DR RefSeq; WP_006038757.1; NZ_AEDD01000007.1.
DR AlphaFoldDB; E0IB40; -.
DR STRING; 717606.PaecuDRAFT_2767; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 9764892at2; -.
DR Proteomes; UP000005387; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:EFM10331.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005387};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EFM10331.1}.
FT DOMAIN 10..266
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 275..395
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 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 383
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 400 AA; 42219 MW; A82074A9D2D9FEE5 CRC64;
MPNDWERDPV IVSAVRTAVG KAKRGALSQT RAEDMGRAVL RAAVDRVPGL RASDIEDVII
GCAMPEGEQG LNFARLMSLY AGFPHSVPAV TVNRFCASGL QAIAYASERI RLGEAEVIVA
GGVESMSHVP MTGFRLSPHP AIVDMMPEAY MGMGHTAEEV ALRYGVSRQD QDAFAAGSHR
KAAAAIAEGR FQDEIVPMEV KLASVDASGR PIERSFTFQV DEGVRPDTTE ARLAALKPSF
ARAGTVTAGN ASQMSDGAAA VVVMSRARAV RLGVQPLASF RSYAVAGVAP EVMGIGPIEA
IPKAVARARI SLDQVDLFEL NEAFAAQCVP IIRELGLAEE RVNVNGGAIA LGHPLGCTGA
KLTVSLLHEL RRRDARYGIV SMCVGGGMGA AGVFELERSV
//
