ID A5FUF2_ACICJ Unreviewed; 378 AA.
AC A5FUF2;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ABQ29234.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:ABQ29234.1};
GN OrderedLocusNames=Acry_0005 {ECO:0000313|EMBL:ABQ29234.1};
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ29234.1, ECO:0000313|Proteomes:UP000000245};
RN [1] {ECO:0000313|EMBL:ABQ29234.1, ECO:0000313|Proteomes:UP000000245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5 {ECO:0000313|EMBL:ABQ29234.1,
RC ECO:0000313|Proteomes:UP000000245};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000697; ABQ29234.1; -; Genomic_DNA.
DR RefSeq; WP_011941205.1; NC_009484.1.
DR AlphaFoldDB; A5FUF2; -.
DR STRING; 349163.Acry_0005; -.
DR KEGG; acr:Acry_0005; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_5; -.
DR Proteomes; UP000000245; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ABQ29234.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000245};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABQ29234.1}.
FT DOMAIN 5..248
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 256..376
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 334
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 364
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 378 AA; 38176 MW; 1433B387E3E79E3B CRC64;
MPSAVIAAYA RSPFALARKG GLSRVRPDEM AAAVVRELVN RSGIAAGDVE DLIVGCAFPE
AEQGLNVARL IGLMADLPIS VAGATVNRFC GSSMYSIHMA AGAIAMGAGE AFIAAGVESM
TRVPMGGFNP MPSPTLFAKM PAAYMGMGET AENVAKRWQI PREAQEEFAL ASHIKAAAAQ
KAGKLAGEIV PISLSGAMVS EDGCIRHDAS REALAGLKPA FDAEGTVTAG TSSPLTDGAS
AVLVCSEDYA AKHGLAPLAR IRSVAVAGCA PDIMGMGPVA ASRKALARAG IEASALDVVE
LNEAFASQAL ACIGELGLDP ARVNLDGGAI ALGHPLGATG ARITGKAAQL LQREGGKFAL
ATQCIGGGQG IATVLEAL
//
