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Database: UniProt
Entry: A0A1W9JV27_9PROT
LinkDB: A0A1W9JV27_9PROT
Original site: A0A1W9JV27_9PROT 
ID   A0A1W9JV27_9PROT        Unreviewed;       395 AA.
AC   A0A1W9JV27;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:OQW75738.1};
GN   ORFNames=BVN33_06670 {ECO:0000313|EMBL:OQW75738.1};
OS   Proteobacteria bacterium ST_bin13.
OC   Bacteria; Pseudomonadota.
OX   NCBI_TaxID=1978761 {ECO:0000313|EMBL:OQW75738.1, ECO:0000313|Proteomes:UP000192661};
RN   [1] {ECO:0000313|EMBL:OQW75738.1, ECO:0000313|Proteomes:UP000192661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST_bin13 {ECO:0000313|EMBL:OQW75738.1};
RX   PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA   Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT   "Comammox in drinking water systems.";
RL   Water Res. 116:332-341(2017).
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:OQW75738.1}.
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DR   EMBL; MSXQ01000006; OQW75738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9JV27; -.
DR   Proteomes; UP000192661; 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; 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   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          6..262
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          271..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   395 AA;  40372 MW;  B73851CEF537D202 CRC64;
     MATDPVVIVS YARTPMGSFQ GALSGASATE LGAAAVGSAV ERAGLSGAAI ERIYMGCVLP
     AGLGQAPARQ AALKAGLPDH IEATTVNKMC GSGMQAAIMA ADALAAGSVD LLIAGGMESM
     TNAPYLSMKH RSGARIGHDV LKDHMYLDGL EDAYEPGKLM GNFAEDTAAA YQFTREQQDD
     YAIASLIRAQ EAQSSGGFDR EITPVEIAGR KGIVTVDKDE QPLKGDPAKI PTLKPAFSKD
     GTVTAANASS ISDGAAALVM TRLSVAEKLG LTPIARIVAT AGHAHAPALF TTAPVFAMRK
     AMEKAGWSAS DIDLFEVNEA FAIVAMIAMR DLGLSHDVVN IHGGACALGH PIGASGARIM
     ATLLSALQTT GGKRGMASLC IGGGEATAVA VEMMG
//
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