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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//