ID A0A1Q8YJQ6_9BURK Unreviewed; 398 AA.
AC A0A1Q8YJQ6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=BLL52_0579 {ECO:0000313|EMBL:OLP08291.1};
OS Rhodoferax antarcticus ANT.BR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1111071 {ECO:0000313|EMBL:OLP08291.1, ECO:0000313|Proteomes:UP000185911};
RN [1] {ECO:0000313|EMBL:OLP08291.1, ECO:0000313|Proteomes:UP000185911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANT.BR {ECO:0000313|EMBL:OLP08291.1,
RC ECO:0000313|Proteomes:UP000185911};
RA Baker J., Riester C., Skinner B., Newell A., Swingley W., Madigan M.,
RA Jung D., Asao M., Chen M., Loughlin P., Pan H., Lin S., Li N., Shaw J.,
RA Prado M., Sherman C., Li X., Tang J., Blankenship R., Zhao T., Touchman J.,
RA Sattley M.;
RT "Genome sequence of Rhodoferax antarcticus ANT.BR, a psychrophilic purple
RT nonsulfur bacterium from an Antarctic microbial mat.";
RL Submitted (JAN-2017) 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 -!- 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:OLP08291.1}.
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DR EMBL; MSYM01000005; OLP08291.1; -; Genomic_DNA.
DR RefSeq; WP_075585160.1; NZ_MSYM01000005.1.
DR AlphaFoldDB; A0A1Q8YJQ6; -.
DR STRING; 81479.RA876_16910; -.
DR Proteomes; UP000185911; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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:OLP08291.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185911};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OLP08291.1}.
FT DOMAIN 8..267
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 275..397
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 94
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 354
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 398 AA; 41438 MW; 24AE750F90E299B2 CRC64;
MKQVQDAYIV AATRSPIGKS HRGFFRNTRP DDLLVKVLQS ALAQVPGLDP GAIEDVVCGC
AIPEGQQGLN IARIGAVLAG LPVSVGGITV NRFCASGLSA IQMAADRIRV GEADVMIAAG
VESMSMVPMM GNSPSMSPAM FDNDENIGIA YGMGLTAEKV ANQWKVSREA QDAFAVESHR
RALAAQAAGY FAAEITPIEV IDRSPNLQTG EVIEKKRIVS LDEGARADTS LEGLAKLRTV
FAARGSVTAG NSSQTSDGAG ALILVSEKAL KQYGLTPLAR FVSFAAKGVP PQFMGIGPIE
AIPVALRNAG LSLSDIDWIE LNEAFAAQSL AVINTLGLDV AKVNPMGGAI ALGHPLGATG
AIRAATVIHA LQRQQLKYGM VSMCIGMGQG AAGIFERV
//
