ID F4QIS7_9CAUL Unreviewed; 392 AA.
AC F4QIS7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Acetyl-CoA acetyltransferase family protein {ECO:0000313|EMBL:EGF91836.1};
GN ORFNames=ABI_02680 {ECO:0000313|EMBL:EGF91836.1};
OS Asticcacaulis biprosthecium C19.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF91836.1, ECO:0000313|Proteomes:UP000006512};
RN [1] {ECO:0000313|Proteomes:UP000006512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Draft genome sequence of Brevundimonas diminuta.";
RL Submitted (MAR-2011) 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}.
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DR EMBL; GL883077; EGF91836.1; -; Genomic_DNA.
DR RefSeq; WP_006271002.1; NZ_GL883077.1.
DR AlphaFoldDB; F4QIS7; -.
DR STRING; 715226.ABI_02680; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_1_1_5; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000006512; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF22; ACETYL-COA ACETYLTRANSFERASE; 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; PS00737; THIOLASE_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EGF91836.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..389
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 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 392 AA; 40886 MW; 8269C297905C7B12 CRC64;
MNREAVIVAT ARTPIGRAYR GAFNLTPSPT LAAHALTAAV ARAGIDAAQI EDCILGCSLP
QGSQQTIGRM AALRAGFPVD VPGMTLDRQC SSGLMTIATA AKQVIVDRMD IVVAGGVESI
SQVQTPALRI DADPALAAMQ ADAYMPMLET AEIVAARYGI TREACDAYAL ESQQRTAAAQ
TSGRFDAEIV PMTATMQVTD KTTGKTSQRE ITLSRDEGAR ADTTAEGLAA LKTALPGGTV
TAGNASQLSD GASACVVMEA SLAERRGLHP LGRYVGMAVA GTKPDEMGIG PVFAIPRLLQ
KFGVSMDDIG LWELNEAFAV QVIYCRDRLG IPAEQLNVNG GAISIGHPYG MSGARMVGHA
LIEGRRRGVR YVVVTMCVGG GMGAAGLFEV FP
//
