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Database: UniProt
Entry: A0A1V4HUG0_NITVU
LinkDB: A0A1V4HUG0_NITVU
Original site: A0A1V4HUG0_NITVU 
ID   A0A1V4HUG0_NITVU        Unreviewed;       392 AA.
AC   A0A1V4HUG0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:OPH81607.1};
GN   ORFNames=B2M20_16655 {ECO:0000313|EMBL:OPH81607.1};
OS   Nitrobacter vulgaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Nitrobacter.
OX   NCBI_TaxID=29421 {ECO:0000313|EMBL:OPH81607.1, ECO:0000313|Proteomes:UP000189940};
RN   [1] {ECO:0000313|EMBL:OPH81607.1, ECO:0000313|Proteomes:UP000189940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ab1 {ECO:0000313|EMBL:OPH81607.1,
RC   ECO:0000313|Proteomes:UP000189940};
RA   Mellbye B.L., Davis E.W., Spieck E., Chang J.H., Bottomley P.J.,
RA   Sayavedra-Soto L.A.;
RT   "Genome sequence of the nitrite-oxidizing bacterium Nitrobacter vulgaris
RT   strain Ab1.";
RL   Submitted (FEB-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:OPH81607.1}.
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DR   EMBL; MWPQ01000058; OPH81607.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4HUG0; -.
DR   STRING; 29421.B2M20_16655; -.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000189940; 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:SF107; 3-KETOACYL-COA THIOLASE, MITOCHONDRIAL; 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; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          5..261
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          270..391
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        89
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        348
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        378
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   392 AA;  40228 MW;  5A8891ED513762A8 CRC64;
     MSDGVVIVSA ARTPVGSFNG ALATTPAHAL GAIAIKAALE RAGIEPGRVS EVIMGQILTA
     AQGQNPARQA SIAAGVPVES PAWGVNQLCG SGLRTVALGY QAILNGDSDI VVAGGQESMS
     MAPHAQHLRG GVKMGGLELI DTMIKDGLWD AFNGYHMGNT AENVAREYQI TRQQQDEFAA
     GSQNKAEAAQ KAGRFKDEIV PVTVKSRKGD VVVDTDEYPK AGVTVDAIAK LRPAFEKDGT
     VTAANASGIN DGAAAVVLMS AAQAAKEGKT PLARIVSWAH AGVDPKIMGT GPIPASRAAL
     KKAGWTIGDL DLIEANEAFA AQACAVNKDL GWDTSKVNVN GGAIAIGHPV GASGARVLVT
     LLHEMQKRNV KKGLATLCIG GGMGIAMCVE RG
//
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