ID A0A166SSI7_9RHOB Unreviewed; 391 AA.
AC A0A166SSI7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KZY04248.1};
GN ORFNames=A3721_16740 {ECO:0000313|EMBL:KZY04248.1};
OS Sulfitobacter sp. HI0023.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1822225 {ECO:0000313|EMBL:KZY04248.1, ECO:0000313|Proteomes:UP000077323};
RN [1] {ECO:0000313|EMBL:KZY04248.1, ECO:0000313|Proteomes:UP000077323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI0023 {ECO:0000313|EMBL:KZY04248.1,
RC ECO:0000313|Proteomes:UP000077323};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-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:KZY04248.1}.
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DR EMBL; LWEQ01000102; KZY04248.1; -; Genomic_DNA.
DR RefSeq; WP_067928160.1; NZ_LWEQ01000102.1.
DR AlphaFoldDB; A0A166SSI7; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000077323; 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; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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 Reference proteome {ECO:0000313|Proteomes:UP000077323};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KZY04248.1}.
FT DOMAIN 4..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..390
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 88
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 347
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 391 AA; 40896 MW; 83F75CE5558B6FBA CRC64;
MTNVVIASAA RTPVGSFGGS FSTVPAHDLG TAVLKELVAR AGVDASEVSE TILGQVLTAA
QGQNPARQAH INAGFPKEAA AWSINQVCGS GLRAVALAAQ HIQLGDANII AAGGQENMTL
APHAQNLRAG QKMGDMQLID TMIKDGLWDA FNGYHMGQTA ENVAEKWQIS RDQQDEFAVS
SQNKAEAAQK AGKFQDEIVA YTVKTRKGDV VVDQDEYIRH GATMEAMQKL RPAFTKDGSV
TAANASGLND GAAGALLMSA EEAEKRGIEP LARIASYATA GLDPSIMGVG PIYASRKALE
KAGWKAEDLD LVEANEAFAA QACAVNKDMG WDPAIVNVNG GAIAIGHPIG ASGARILNTL
LFEMKRRDAK KGLATLCIGG GMGVAMCIER P
//
