ID   V2UD15_9GAMM            Unreviewed;       502 AA.
AC   V2UD15;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Acetyl-CoA C-acetyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=P253_01045 {ECO:0000313|EMBL:ESK48402.1};
OS   Acinetobacter indicus CIP 110367.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1341679 {ECO:0000313|EMBL:ESK48402.1, ECO:0000313|Proteomes:UP000018415};
RN   [1] {ECO:0000313|EMBL:ESK48402.1, ECO:0000313|Proteomes:UP000018415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 110367 {ECO:0000313|EMBL:ESK48402.1,
RC   ECO:0000313|Proteomes:UP000018415};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Grillot-Courvalin C.,
RA   Clermont D., Rocha E., Yoon E.-J., Nemec A., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter indicus CIP 110367.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {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:ESK48402.1}.
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DR   EMBL; AYET01000002; ESK48402.1; -; Genomic_DNA.
DR   RefSeq; WP_016659065.1; NZ_KI530754.1.
DR   AlphaFoldDB; V2UD15; -.
DR   PATRIC; fig|1341679.3.peg.1029; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_031026_2_0_6; -.
DR   OrthoDB; 1402717at2; -.
DR   Proteomes; UP000018415; Unassembled WGS sequence.
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; IPR020617; Thiolase_C.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR   PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018415};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          85..352
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          379..502
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  53346 MW;  CF05326AD354D803 CRC64;
     MSKTTQENPA VENSATETVS NTSKSTTRTT KSSGTANSSA NPAAKPARTR AASTRKKSTT
     PPSETTTETS GQQDNTMSQN TVRRVAIIGG NRIPFARSNG AYFTASNIDM FTAALNGLVE
     RYRLEGQRLG EVVAGAVLKH SRDFNMTREC VLNTELAPET PAYDIQQACG TGLQAAFLVA
     NKIALGQIEV GIAGGVDTTS DAPIAFGDGL RKALLELNIA KTGKDRLKAL TKINIKDLMD
     APKNGEPRTG LSMGDHQAIT ALEWGISREA QDELAASSHQ KMAAAYEAGF FDDLITPFLG
     LERDNNLRPD SSVEKLAKLK PAFGKGDART MTAGNSTPLT DGASCVLLAS EEWAKANGHD
     VLAYLTFQET AAVDFVEKKE GLLMAPAYAV PRMLERAGLT LQDFDYYEIH EAFASQVLST
     LKAWEDPKFC KDRLGLEAPL GSIDRNKLNV KGSSLAAGHP FAATGGRILA TAAKLLNEKG
     SGRVLISICA AGGQGVTAIV EK
//