ID A0A2A7US65_COMTR Unreviewed; 394 AA.
AC A0A2A7US65;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Acetyl-CoA C-acyltransferase {ECO:0000313|EMBL:PEH88084.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:PEH88084.1};
GN ORFNames=CRM82_05245 {ECO:0000313|EMBL:PEH88084.1};
OS Comamonas terrigena.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=32013 {ECO:0000313|EMBL:PEH88084.1, ECO:0000313|Proteomes:UP000220246};
RN [1] {ECO:0000313|Proteomes:UP000220246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_394 {ECO:0000313|Proteomes:UP000220246};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PEH88084.1}.
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DR EMBL; PDEA01000001; PEH88084.1; -; Genomic_DNA.
DR RefSeq; WP_066539896.1; NZ_UIGV01000002.1.
DR AlphaFoldDB; A0A2A7US65; -.
DR STRING; 1219032.GCA_001515545_03172; -.
DR GeneID; 80799994; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000220246; 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; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919:SF138; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:PEH88084.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000220246};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:PEH88084.1}.
FT DOMAIN 6..264
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 272..392
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 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 40999 MW; B3D93F0C830817FF CRC64;
MHQDPVVIVS AARTPMGAFQ GDFSDLAAHD LGGAAIAAAV QRAGIRPEQV EEVLFGNCLM
AGQGQAPARQ AGFKGGLPQS TGAVTLSKMC GAGMEATILA HDQLIAGSRE VMVAGGMESM
TNAPYLLKKG RGGYRMGHDK VYDHMMLDGL EDAYEAGRSM GTFGEDCAAK YQFTREAQDA
FAIASVQRAQ HATQSGAFAA EITPVTLKTR KGDVTVSVDE GPAKAKLDKI TALKPAFKKD
GTITAASSSS INDGAAAMVL MRESTAKQLG CKPLARIVAH ASHAQAPEWF TTAPVGATEK
ALKKAGWKVD DVDLWEVNEA FAVVPMALMA ELKVPHDKVN VHGGACALGH PIGASGARIL
VTLIHALQTH GKKKGLATLC IGGGEGTAMA IELV
//
