ID G2KMJ4_MICAA Unreviewed; 375 AA.
AC G2KMJ4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN Name=fadA3 {ECO:0000313|EMBL:AEP10687.1};
GN OrderedLocusNames=MICA_2385 {ECO:0000313|EMBL:AEP10687.1};
OS Micavibrio aeruginosavorus (strain ARL-13).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Micavibrio.
OX NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP10687.1, ECO:0000313|Proteomes:UP000009286};
RN [1] {ECO:0000313|EMBL:AEP10687.1, ECO:0000313|Proteomes:UP000009286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARL-13 {ECO:0000313|EMBL:AEP10687.1,
RC ECO:0000313|Proteomes:UP000009286};
RX PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA Wang Z., Kadouri D., Wu M.;
RT "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT aeruginosavorus ARL-13.";
RL BMC Genomics 12:453-453(2011).
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; CP002382; AEP10687.1; -; Genomic_DNA.
DR RefSeq; WP_014103910.1; NC_016026.1.
DR AlphaFoldDB; G2KMJ4; -.
DR STRING; 856793.MICA_2385; -.
DR KEGG; mai:MICA_2385; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_1_1_5; -.
DR OrthoDB; 7181944at2; -.
DR Proteomes; UP000009286; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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:AEP10687.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009286};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AEP10687.1}.
FT DOMAIN 6..245
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 253..373
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 375 AA; 38305 MW; 5E5DAC81D4484AB2 CRC64;
MTETAVICGF KRSPMHLATK GALAKVRPDD IAAAVISALV KETGVKPEDI EDLIMGCAFP
EAEQGFNLAR IVVQLAGLPV SVGGVTMNRF CGSSMTAIHM AAGAIAMGAG DVFICAGVES
MTRIPMGGFN PMPNPTLAKT FPQAYMSMGE TAENLASKYQ ITRGEQDQFA ANSQAKAAAA
AASGKFDAEI VPIGDIKTDG IIRPETTVEV LAGLKPAFLS DGTVTAGTSS PLTDGAAAVL
VTSESYARKH NLPIMARIKS IGVSGCAAEI MGIGPVPSSQ KALARAGLSI KDIGLFELNE
AFAAQSLSVV KELGIDQSRL NIDGGAIALG HPLGASGARI TGKLASLMQR EGIKTGLATM
CIGGGQGTAI VLEAA
//
