ID V2J1A2_9BURK Unreviewed; 392 AA.
AC V2J1A2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ESJ20835.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ESJ20835.1};
GN ORFNames=B551_0209450 {ECO:0000313|EMBL:ESJ20835.1};
OS Cupriavidus sp. HPC(L).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESJ20835.1, ECO:0000313|Proteomes:UP000053474};
RN [1] {ECO:0000313|EMBL:ESJ20835.1, ECO:0000313|Proteomes:UP000053474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA Purohit H.J., Agarwal L.;
RT "Cupriavidus a Desert isolate.";
RL Submitted (AUG-2013) 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:ESJ20835.1}.
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DR EMBL; AMPR02000122; ESJ20835.1; -; Genomic_DNA.
DR RefSeq; WP_006577376.1; NZ_AMPR02000122.1.
DR AlphaFoldDB; V2J1A2; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000053474; Unassembled WGS sequence.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:ESJ20835.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053474};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ESJ20835.1}.
FT DOMAIN 4..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..392
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 349
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 379
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 392 AA; 40465 MW; 5FE6D3441032A17E CRC64;
MTDVVIVSAA RTAVGKFGGS LAKVPAPELG AIVIQAALER AGVKPEQVSE VIMGQVLTAG
SGQNPARQAA IKAGLPHMVP AMTINKVCGS GLKAVMLAAN AIASGDAEIV VAGGQENMSA
APHVLPGSRD GFRMGDAKLI DTMIVDGLWD VYNQYHMGIT AENVAKEYGI SREAQDEFAV
SSQNKAEAAQ KAGRFDEEIV PVMIPQRKGE PVAFATDEFV RHGATLESIA GLKPAFDKAG
TVTAANASGI NDGAAAVVVM SAAKARELGL TPLATIRAFA NAGVDPKVMG MGPVPASQRC
LSRAGWSVQD LDLMEINEAF AAQALAVHKQ MGWDTDKVNV NGGAIAIGHP IGASGCRILV
TLLHEMKRRD AKKGLASLCI GGGMGVALAV ER
//
