ID B9NL40_9RHOB Unreviewed; 391 AA.
AC B9NL40;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EEE36578.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:EEE36578.1};
GN Name=phbA_2 {ECO:0000313|EMBL:EEE36578.1};
GN ORFNames=RKLH11_411 {ECO:0000313|EMBL:EEE36578.1};
OS Rhodobacteraceae bacterium KLH11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE36578.1, ECO:0000313|Proteomes:UP000005135};
RN [1] {ECO:0000313|Proteomes:UP000005135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX PubMed=21742885; DOI=10.1128/jb.05556-11;
RA Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine Lactone-
RT Producing Bacterium Isolated from the Marine Sponge Mycale laxissima.";
RL J. Bacteriol. 193:5011-5012(2011).
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; DS999531; EEE36578.1; -; Genomic_DNA.
DR AlphaFoldDB; B9NL40; -.
DR STRING; 467661.RKLH11_411; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_5; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000005135; 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:EEE36578.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005135};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EEE36578.1}.
FT DOMAIN 4..260
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..390
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 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 391 AA; 40837 MW; 4FD06094BB8FCA9D CRC64;
MTNVVIASAA RTGVGSFSGS FANTPAHDLG AAVLEAVVER AGIEKGEVSE TIMGQVLTAA
QGQNPARQAH INAGLPQESA AWGINQVCGS GLRAVALGAQ HIQLGDADIV AAGGQENMTL
SPHAATLRAG HKMGDMKYID TMIRDGLWDA FNGYHMGQTA ENVAEKWQIN RDMQDEFAVA
SQNKAEAAQK AGKFADEIVP FIIKTRKGDI VMDKDEYIRH GATMEAMGKL RPAFTKDGSV
TAANASGLND GAAATLLMSA ENAEKRGIEP LARIASYATA GLDPSIMGVG PIHASRKALE
KAGWSVDDLD LVEANEAFAA QACAVNKDMG WDPSIVNVNG GAIAIGHPIG ASGCRVLNTL
LFEMKRRDAK KGLATLCIGG GMGVALCVER D
//
