ID A0A178GGT1_9GAMM Unreviewed; 389 AA.
AC A0A178GGT1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:OAL83303.1};
GN ORFNames=AY605_10930 {ECO:0000313|EMBL:OAL83303.1};
OS Acinetobacter sp. SFD.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1805635 {ECO:0000313|EMBL:OAL83303.1, ECO:0000313|Proteomes:UP000186186};
RN [1] {ECO:0000313|EMBL:OAL83303.1, ECO:0000313|Proteomes:UP000186186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFD {ECO:0000313|EMBL:OAL83303.1,
RC ECO:0000313|Proteomes:UP000186186};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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:OAL83303.1}.
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DR EMBL; LSZJ01000015; OAL83303.1; -; Genomic_DNA.
DR RefSeq; WP_064096837.1; NZ_LSZJ01000015.1.
DR AlphaFoldDB; A0A178GGT1; -.
DR STRING; 1805635.AY605_10930; -.
DR Proteomes; UP000186186; 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; -; 2.
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; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF144; ACYL-COA THIOLASE-RELATED; 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; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:OAL83303.1}.
FT DOMAIN 2..258
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 266..387
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 86
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 389 AA; 40334 MW; 90FF5E3619E1F8B1 CRC64;
MIVIVDAVRT AMGGFQGSLS SCTAPDLGAV VIKEAVARAG LSANDIDEVI MGCVLPAGLK
QGPARQAMRQ AGLPDSTGAT TINKICGSGM KAVMQAADAI KAGSAEIVVA GGMESMSNAP
YLMDKARAGF RMGHGKVIDH MFQEGLEDAE TGLSMGILAQ EMADKKGYTR EQQDDYAIGS
LNKAVTAVQQ GFFKDEIVPV TVSSRKGDVV VEQDEQPLNA KADKIPTLRP AFKKDGTITA
ANASSISDGA SALVITSSEI AAQRNLKPLA NIVAYASHSQ HPSEFTIAPV GAIEKVLKKT
GWDAQEVDLW EINEAFAMVT MLAIDAFKLD PAKVNVNGGA CALGHPLGSS GSRIIVSLIH
ALMRTGGKKG IAALCIGGGE ATAIAVELI
//
